(data stored in ACNUC22857 zone)

SWISSPROT: AP1B1_HUMAN

ID   AP1B1_HUMAN             Reviewed;         949 AA.
AC   Q10567; C9JRD1; F8WDL0; P78436; Q20WL3; Q86X54;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 2.
DT   08-MAY-2019, entry version 173.
DE   RecName: Full=AP-1 complex subunit beta-1;
DE   AltName: Full=Adaptor protein complex AP-1 subunit beta-1;
DE   AltName: Full=Adaptor-related protein complex 1 subunit beta-1;
DE   AltName: Full=Beta-1-adaptin;
DE   AltName: Full=Beta-adaptin 1;
DE   AltName: Full=Clathrin assembly protein complex 1 beta large chain;
DE   AltName: Full=Golgi adaptor HA1/AP1 adaptin beta subunit;
GN   Name=AP1B1; Synonyms=ADTB1, BAM22, CLAPB2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND VARIANT ALA-777.
RC   TISSUE=Brain;
RX   PubMed=7987321; DOI=10.1093/hmg/3.8.1393;
RA   Peyrard M., Fransson I., Xie Y.-G., Han F.-Y., Ruttledge M.H.,
RA   Swahn S., Collins J.E., Dunham I., Collins V.P., Dumanski J.P.;
RT   "Characterization of a new member of the human beta-adaptin gene
RT   family from chromosome 22q12, a candidate meningioma gene.";
RL   Hum. Mol. Genet. 3:1393-1399(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C), AND VARIANT
RP   ALA-777.
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:R84.1-R84.11(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA   Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA   Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA   Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA   Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA   Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA   Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA   Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA   Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA   Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA   Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA   Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA   Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA   Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA   Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA   Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA   Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA   Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA   Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA   Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA   Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA   Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA   Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA   Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA   Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA   Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA   Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA   Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA   Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA   Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA   Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA   Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA   O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA   Khan A.S., Lane L., Tilahun Y., Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT
RP   ALA-777.
RC   TISSUE=Lymph;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-922, AND VARIANT ALA-777.
RX   PubMed=8812422; DOI=10.1006/geno.1996.0431;
RA   Peyrard M., Pan H.-Q., Kedra D., Fransson I., Swahn S., Hartman K.,
RA   Clifton S.W., Roe B.A., Dumanski J.P.;
RT   "Structure of the promoter and genomic organization of the human
RT   beta'-adaptin gene (BAM22) from chromosome 22q12.";
RL   Genomics 36:112-117(1996).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-318, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
CC   -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1
CC       that plays a role in protein sorting in the late-Golgi/trans-Golgi
CC       network (TGN) and/or endosomes. The AP complexes mediate both the
CC       recruitment of clathrin to membranes and the recognition of
CC       sorting signals within the cytosolic tails of transmembrane cargo
CC       molecules.
CC   -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer
CC       composed of two large adaptins (gamma-type subunit AP1G1 and beta-
CC       type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or
CC       AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or
CC       AP1S3).
CC   -!- INTERACTION:
CC       P35585:Ap1m1 (xeno); NbExp=5; IntAct=EBI-1171303, EBI-1040251;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle,
CC       clathrin-coated vesicle membrane; Peripheral membrane protein;
CC       Cytoplasmic side. Note=Component of the coat surrounding the
CC       cytoplasmic face of coated vesicles located at the Golgi complex.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC         Comment=Additional isoforms seem to exist.;
CC       Name=A;
CC         IsoId=Q10567-1; Sequence=Displayed;
CC       Name=B;
CC         IsoId=Q10567-2; Sequence=VSP_000163;
CC       Name=C;
CC         IsoId=Q10567-3; Sequence=VSP_000163, VSP_038753;
CC       Name=4;
CC         IsoId=Q10567-4; Sequence=VSP_000163, VSP_044928, VSP_038753;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000305}.
DR   EMBL; L13939; AAC98702.1; -; mRNA.
DR   EMBL; CT841508; CAJ86438.1; -; mRNA.
DR   EMBL; AC000041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC002059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC046242; AAH46242.1; -; mRNA.
DR   EMBL; U36268; AAC50684.2; -; Genomic_DNA.
DR   EMBL; U36250; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36251; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36252; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36253; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36254; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36255; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36256; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36257; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36258; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36259; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36260; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36261; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36262; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36263; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36264; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36265; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36266; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; U36267; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; AF379038; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; AF379039; AAC50684.2; JOINED; Genomic_DNA.
DR   EMBL; L48038; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS13855.1; -. [Q10567-1]
DR   CCDS; CCDS13856.2; -. [Q10567-3]
DR   CCDS; CCDS54515.1; -. [Q10567-4]
DR   PIR; I54360; I54360.
DR   RefSeq; NP_001118.3; NM_001127.3.
DR   RefSeq; NP_001159491.1; NM_001166019.1.
DR   RefSeq; NP_663782.2; NM_145730.2.
DR   PDB; 4HMY; X-ray; 7.00 A; B=1-584.
DR   PDB; 4P6Z; X-ray; 3.00 A; B=1-584.
DR   PDB; 6CM9; EM; 3.73 A; B=1-584.
DR   PDB; 6CRI; EM; 6.80 A; B/I/J=14-583.
DR   PDB; 6D83; EM; 4.27 A; B=1-584.
DR   PDB; 6D84; EM; 6.72 A; B/F=1-584.
DR   PDB; 6DFF; EM; 3.90 A; B=1-584.
DR   PDBsum; 4HMY; -.
DR   PDBsum; 4P6Z; -.
DR   PDBsum; 6CM9; -.
DR   PDBsum; 6CRI; -.
DR   PDBsum; 6D83; -.
DR   PDBsum; 6D84; -.
DR   PDBsum; 6DFF; -.
DR   SMR; Q10567; -.
DR   BioGrid; 106671; 91.
DR   CORUM; Q10567; -.
DR   DIP; DIP-24207N; -.
DR   ELM; Q10567; -.
DR   IntAct; Q10567; 63.
DR   MINT; Q10567; -.
DR   STRING; 9606.ENSP00000350199; -.
DR   TCDB; 9.B.278.1.1; the organellar-targeting adaptor protein complex (o-apc) family.
DR   iPTMnet; Q10567; -.
DR   PhosphoSitePlus; Q10567; -.
DR   SwissPalm; Q10567; -.
DR   BioMuta; AP1B1; -.
DR   DMDM; 290457628; -.
DR   EPD; Q10567; -.
DR   jPOST; Q10567; -.
DR   MaxQB; Q10567; -.
DR   PaxDb; Q10567; -.
DR   PeptideAtlas; Q10567; -.
DR   PRIDE; Q10567; -.
DR   ProteomicsDB; 58857; -.
DR   ProteomicsDB; 58858; -. [Q10567-2]
DR   ProteomicsDB; 58859; -. [Q10567-3]
DR   DNASU; 162; -.
DR   Ensembl; ENST00000317368; ENSP00000319361; ENSG00000100280.
DR   Ensembl; ENST00000357586; ENSP00000350199; ENSG00000100280.
DR   Ensembl; ENST00000402502; ENSP00000386071; ENSG00000100280.
DR   Ensembl; ENST00000405198; ENSP00000384194; ENSG00000100280.
DR   Ensembl; ENST00000415447; ENSP00000387612; ENSG00000100280.
DR   Ensembl; ENST00000432560; ENSP00000400065; ENSG00000100280.
DR   GeneID; 162; -.
DR   KEGG; hsa:162; -.
DR   UCSC; uc003afi.4; human. [Q10567-1]
DR   CTD; 162; -.
DR   DisGeNET; 162; -.
DR   GeneCards; AP1B1; -.
DR   HGNC; HGNC:554; AP1B1.
DR   HPA; HPA065226; -.
DR   HPA; HPA068520; -.
DR   MIM; 600157; gene.
DR   neXtProt; NX_Q10567; -.
DR   PharmGKB; PA24844; -.
DR   eggNOG; KOG1061; Eukaryota.
DR   eggNOG; COG5096; LUCA.
DR   HOGENOM; HOG000163270; -.
DR   InParanoid; Q10567; -.
DR   KO; K12392; -.
DR   OrthoDB; 323029at2759; -.
DR   PhylomeDB; Q10567; -.
DR   TreeFam; TF300318; -.
DR   Reactome; R-HSA-164940; Nef mediated downregulation of MHC class I complex cell surface expression.
DR   Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR   Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR   Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR   ChiTaRS; AP1B1; human.
DR   GeneWiki; AP1B1; -.
DR   GenomeRNAi; 162; -.
DR   PRO; PR:Q10567; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   Bgee; ENSG00000100280; Expressed in 228 organ(s), highest expression level in prostate gland.
DR   ExpressionAtlas; Q10567; baseline and differential.
DR   Genevisible; Q10567; HS.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR   GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR   GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR   GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0005215; F:transporter activity; TAS:ProtInc.
DR   GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR   GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   Gene3D; 1.25.10.10; -; 1.
DR   Gene3D; 2.60.40.1150; -; 1.
DR   Gene3D; 3.30.310.10; -; 1.
DR   InterPro; IPR026739; AP_beta.
DR   InterPro; IPR016342; AP_complex_bsu_1_2_4.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR015151; B-adaptin_app_sub_C.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR   InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR   InterPro; IPR013037; Clathrin_b-adaptin_app_Ig-like.
DR   InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR   InterPro; IPR012295; TBP_dom_sf.
DR   PANTHER; PTHR11134; PTHR11134; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF02883; Alpha_adaptinC2; 1.
DR   Pfam; PF09066; B2-adapt-app_C; 1.
DR   PIRSF; PIRSF002291; AP_complex_beta; 1.
DR   SMART; SM00809; Alpha_adaptinC2; 1.
DR   SMART; SM00185; ARM; 2.
DR   SMART; SM01020; B2-adapt-app_C; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF49348; SSF49348; 1.
DR   SUPFAM; SSF55711; SSF55711; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q10567.
DR   SWISS-2DPAGE; Q10567.
KW   3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW   Cytoplasmic vesicle; Golgi apparatus; Membrane; Nitration;
KW   Polymorphism; Protein transport; Reference proteome; Transport.
FT   CHAIN         1    949       AP-1 complex subunit beta-1.
FT                                /FTId=PRO_0000193738.
FT   COMPBIAS    576    725       Pro-rich (stalk region).
FT   MOD_RES     318    318       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     574    574       Nitrated tyrosine.
FT                                {ECO:0000250|UniProtKB:O35643}.
FT   VAR_SEQ     667    673       Missing (in isoform B, isoform C and
FT                                isoform 4). {ECO:0000303|PubMed:15461802,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:7987321}.
FT                                /FTId=VSP_000163.
FT   VAR_SEQ     722    741       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_044928.
FT   VAR_SEQ     923    925       Missing (in isoform C and isoform 4).
FT                                {ECO:0000303|PubMed:15461802,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_038753.
FT   VARIANT     777    777       T -> A (in dbSNP:rs2857465).
FT                                {ECO:0000269|PubMed:15461802,
FT                                ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:7987321,
FT                                ECO:0000269|PubMed:8812422}.
FT                                /FTId=VAR_062816.
FT   HELIX        15     23       {ECO:0000244|PDB:4P6Z}.
FT   HELIX        27     42       {ECO:0000244|PDB:4P6Z}.
FT   HELIX        48     50       {ECO:0000244|PDB:4P6Z}.
FT   HELIX        51     55       {ECO:0000244|PDB:4P6Z}.
FT   HELIX        63     76       {ECO:0000244|PDB:4P6Z}.
FT   TURN         77     79       {ECO:0000244|PDB:4P6Z}.
FT   HELIX        83     87       {ECO:0000244|PDB:4P6Z}.
FT   HELIX        88     94       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       100    110       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       116    130       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       135    151       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       153    159       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       161    168       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       174    190       {ECO:0000244|PDB:4P6Z}.
FT   STRAND      191    193       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       201    213       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       216    228       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       234    244       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       245    249       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       253    266       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       267    269       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       275    290       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       291    293       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       296    312       {ECO:0000244|PDB:4P6Z}.
FT   TURN        314    319       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       321    324       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       332    345       {ECO:0000244|PDB:4P6Z}.
FT   TURN        348    350       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       351    361       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       367    383       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       387    399       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       404    420       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       428    431       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       432    434       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       442    454       {ECO:0000244|PDB:4P6Z}.
FT   TURN        455    458       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       462    467       {ECO:0000244|PDB:4P6Z}.
FT   TURN        471    475       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       478    494       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       500    511       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       517    532       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       534    540       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       557    564       {ECO:0000244|PDB:4P6Z}.
FT   TURN        565    568       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       570    574       {ECO:0000244|PDB:4P6Z}.
FT   HELIX       578    580       {ECO:0000244|PDB:4P6Z}.
SQ   SEQUENCE   949 AA;  104637 MW;  FE1BA762F9318585 CRC64;
     MTDSKYFTTT KKGEIFELKA ELNSDKKEKK KEAVKKVIAS MTVGKDVSAL FPDVVNCMQT
     DNLELKKLVY LYLMNYAKSQ PDMAIMAVNT FVKDCEDPNP LIRALAVRTM GCIRVDKITE
     YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD INAQLVEDQG FLDTLKDLIS DSNPMVVANA
     VAALSEIAES HPSSNLLDLN PQSINKLLTA LNECTEWGQI FILDCLANYM PKDDREAQSI
     CERVTPRLSH ANSAVVLSAV KVLMKFMEML SKDLDYYGTL LKKLAPPLVT LLSAEPELQY
     VALRNINLIV QKRPEILKHE MKVFFVKYND PIYVKLEKLD IMIRLASQAN IAQVLAELKE
     YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ TKVNYVVQEA IVVIKDIFRK
     YPNKYESVIA TLCENLDSLD EPEARAAMIW IVGEYAERID NADELLESFL EGFHDESTQV
     QLQLLTAIVK LFLKKPTETQ ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVAAKEV
     VLAEKPLISE ETDLIEPTLL DELICYIGTL ASVYHKPPSA FVEGGRGVVH KSLPPRTASS
     ESAESPETAP TGAPPGEQPD VIPAQGDLLG DLLNLDLGPP VSGPPLATSS VQMGAVDLLG
     GGLDSLMGDE PEGIGGTNFV APPTAAVPAN LGAPIGSGLS DLFDLTSGVG TLSGSYVAPK
     AVWLPAMKAK GLEISGTFTR QVGSISMDLQ LTNKALQVMT DFAIQFNRNS FGLAPATPLQ
     VHAPLSPNQT VEISLPLSTV GSVMKMEPLN NLQVAVKNNI DVFYFSTLYP LHILFVEDGK
     MDRQMFLATW KDIPNENEAQ FQIRDCPLNA EAASSKLQSS NIFTVAKRNV EGQDMLYQSL
     KLTNGIWVLA ELRIQPGNPS CTDLELSLKC RAPEVSQHVY QAYETILKN
//

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