(data stored in ACNUC4482 zone)

SWISSPROT: ITA10_HUMAN

ID   ITA10_HUMAN             Reviewed;        1167 AA.
AC   O75578; B2RAM4; B2RTV5; Q6UXJ6; Q9UHZ8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   11-DEC-2019, entry version 178.
DE   RecName: Full=Integrin alpha-10;
DE   Flags: Precursor;
GN   Name=ITGA10; ORFNames=UNQ468/PRO827;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Articular chondrocyte;
RX   PubMed=9685391; DOI=10.1074/jbc.273.32.20383;
RA   Camper L., Hellman U., Lundgren-Aakerlund E.;
RT   "Isolation, cloning, and sequence analysis of the integrin subunit alpha10,
RT   a beta1-associated collagen binding integrin expressed on chondrocytes.";
RL   J. Biol. Chem. 273:20383-20389(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Endothelial cell, and Heart;
RX   PubMed=10702680; DOI=10.1159/000015434;
RA   Lehnert K., Ni J., Leung E., Gough S.M., Morris C.M., Liu D., Wang S.-X.,
RA   Langley R., Krissansen G.W.;
RT   "The integrin alpha10 subunit: expression pattern, partial gene structure,
RT   and chromosomal localization.";
RL   Cytogenet. Cell Genet. 87:238-244(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Trachea;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Integrin alpha-10/beta-1 is a receptor for collagen.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Alpha-10
CC       associates with beta-1.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O75578-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O75578-2; Sequence=VSP_013114, VSP_013115;
CC       Name=3;
CC         IsoId=O75578-3; Sequence=VSP_054483;
CC   -!- TISSUE SPECIFICITY: Widely expressed with highest expression in muscle
CC       and heart. Found in articular cartilage.
CC   -!- DOMAIN: The integrin I-domain (insert) is a VWFA domain. Integrins with
CC       I-domains do not undergo protease cleavage.
CC   -!- SIMILARITY: Belongs to the integrin alpha chain family. {ECO:0000305}.
DR   EMBL; AF074015; AAC31952.1; -; mRNA.
DR   EMBL; AF112345; AAF21944.1; -; mRNA.
DR   EMBL; AF172723; AAF61638.1; -; Genomic_DNA.
DR   EMBL; AY358325; AAQ88691.1; -; mRNA.
DR   EMBL; AK314255; BAG36921.1; -; mRNA.
DR   EMBL; AL160282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471244; EAW71425.1; -; Genomic_DNA.
DR   EMBL; BC140831; AAI40832.1; -; mRNA.
DR   EMBL; BC144637; AAI44638.1; -; mRNA.
DR   CCDS; CCDS72869.1; -. [O75578-1]
DR   CCDS; CCDS76204.1; -. [O75578-3]
DR   RefSeq; NP_001289969.1; NM_001303040.1.
DR   RefSeq; NP_001289970.1; NM_001303041.1. [O75578-3]
DR   RefSeq; NP_003628.2; NM_003637.4. [O75578-1]
DR   SMR; O75578; -.
DR   BioGrid; 114087; 1.
DR   ComplexPortal; CPX-1817; Integrin alpha10-beta1 complex.
DR   CORUM; O75578; -.
DR   IntAct; O75578; 1.
DR   STRING; 9606.ENSP00000358310; -.
DR   ChEMBL; CHEMBL5882; -.
DR   iPTMnet; O75578; -.
DR   PhosphoSitePlus; O75578; -.
DR   BioMuta; ITGA10; -.
DR   EPD; O75578; -.
DR   jPOST; O75578; -.
DR   MassIVE; O75578; -.
DR   PaxDb; O75578; -.
DR   PeptideAtlas; O75578; -.
DR   PRIDE; O75578; -.
DR   ProteomicsDB; 3449; -.
DR   ProteomicsDB; 50095; -. [O75578-1]
DR   ProteomicsDB; 50096; -. [O75578-2]
DR   DNASU; 8515; -.
DR   Ensembl; ENST00000369304; ENSP00000358310; ENSG00000143127. [O75578-1]
DR   Ensembl; ENST00000539363; ENSP00000439894; ENSG00000143127. [O75578-3]
DR   GeneID; 8515; -.
DR   KEGG; hsa:8515; -.
DR   UCSC; uc001eoa.4; human. [O75578-1]
DR   CTD; 8515; -.
DR   DisGeNET; 8515; -.
DR   EuPathDB; HostDB:ENSG00000143127.12; -.
DR   GeneCards; ITGA10; -.
DR   HGNC; HGNC:6135; ITGA10.
DR   MIM; 604042; gene.
DR   neXtProt; NX_O75578; -.
DR   OpenTargets; ENSG00000143127; -.
DR   PharmGKB; PA29936; -.
DR   eggNOG; KOG3637; Eukaryota.
DR   eggNOG; ENOG410XPVZ; LUCA.
DR   GeneTree; ENSGT00940000158423; -.
DR   HOGENOM; HOG000059610; -.
DR   InParanoid; O75578; -.
DR   KO; K06586; -.
DR   OMA; HSAPCAK; -.
DR   OrthoDB; 52951at2759; -.
DR   PhylomeDB; O75578; -.
DR   TreeFam; TF105391; -.
DR   Reactome; R-HSA-216083; Integrin cell surface interactions.
DR   Reactome; R-HSA-447041; CHL1 interactions.
DR   Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
DR   SIGNOR; O75578; -.
DR   ChiTaRS; ITGA10; human.
DR   GeneWiki; ITGA10; -.
DR   GenomeRNAi; 8515; -.
DR   Pharos; O75578; Tbio.
DR   PRO; PR:O75578; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; O75578; protein.
DR   Bgee; ENSG00000143127; Expressed in 131 organ(s), highest expression level in tibia.
DR   Genevisible; O75578; HS.
DR   GO; GO:0034680; C:integrin alpha10-beta1 complex; IDA:UniProtKB.
DR   GO; GO:0008305; C:integrin complex; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005518; F:collagen binding; TAS:ProtInc.
DR   GO; GO:0098639; F:collagen binding involved in cell-matrix adhesion; IMP:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007160; P:cell-matrix adhesion; IMP:UniProtKB.
DR   GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
DR   Gene3D; 2.130.10.130; -; 1.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR013517; FG-GAP.
DR   InterPro; IPR013519; Int_alpha_beta-p.
DR   InterPro; IPR000413; Integrin_alpha.
DR   InterPro; IPR013649; Integrin_alpha-2.
DR   InterPro; IPR028994; Integrin_alpha_N.
DR   InterPro; IPR032695; Integrin_dom_sf.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF01839; FG-GAP; 2.
DR   Pfam; PF08441; Integrin_alpha2; 1.
DR   Pfam; PF00092; VWA; 1.
DR   PRINTS; PR01185; INTEGRINA.
DR   SMART; SM00191; Int_alpha; 5.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF69179; SSF69179; 3.
DR   PROSITE; PS51470; FG_GAP; 7.
DR   PROSITE; PS50234; VWFA; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; O75578.
DR   SWISS-2DPAGE; O75578.
KW   Alternative splicing; Calcium; Cell adhesion; Disulfide bond; Glycoprotein;
KW   Integrin; Magnesium; Membrane; Metal-binding; Polymorphism; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..1167
FT                   /note="Integrin alpha-10"
FT                   /id="PRO_0000016317"
FT   TOPO_DOM        23..1122
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1123..1145
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1146..1167
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          24..85
FT                   /note="FG-GAP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          95..154
FT                   /note="FG-GAP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   DOMAIN          167..350
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REPEAT          361..412
FT                   /note="FG-GAP 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          417..470
FT                   /note="FG-GAP 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          472..534
FT                   /note="FG-GAP 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          535..593
FT                   /note="FG-GAP 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   REPEAT          597..657
FT                   /note="FG-GAP 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00803"
FT   CA_BIND         494..502
FT                   /evidence="ECO:0000255"
FT   CA_BIND         558..566
FT                   /evidence="ECO:0000255"
FT   CA_BIND         620..628
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1134..1140
FT                   /note="Poly-Leu"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        234
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        336
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        364
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        733
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        763
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        839
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        921
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1011
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1018
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        1039
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        76..86
FT                   /evidence="ECO:0000250"
FT   DISULFID        666..675
FT                   /evidence="ECO:0000250"
FT   DISULFID        681..736
FT                   /evidence="ECO:0000250"
FT   DISULFID        789..795
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         19..161
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_054483"
FT   VAR_SEQ         123..124
FT                   /note="AC -> VS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_013114"
FT   VAR_SEQ         125..1167
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_013115"
FT   VARIANT         381
FT                   /note="R -> Q (in dbSNP:rs6665210)"
FT                   /id="VAR_027768"
FT   VARIANT         668
FT                   /note="R -> W (in dbSNP:rs36073645)"
FT                   /id="VAR_034026"
FT   VARIANT         691
FT                   /note="R -> H (in dbSNP:rs2274618)"
FT                   /id="VAR_027769"
FT   VARIANT         702
FT                   /note="A -> T (in dbSNP:rs35515885)"
FT                   /id="VAR_034027"
FT   VARIANT         725
FT                   /note="R -> Q (in dbSNP:rs2274616)"
FT                   /id="VAR_027770"
FT   CONFLICT        844
FT                   /note="L -> I (in Ref. 1; AAC31952)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        909
FT                   /note="V -> G (in Ref. 1; AAC31952)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        926
FT                   /note="D -> E (in Ref. 1; AAC31952)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1167 AA;  127602 MW;  2F7FF938B4C0CBAC CRC64;
     MELPFVTHLF LPLVFLTGLC SPFNLDEHHP RLFPGPPEAE FGYSVLQHVG GGQRWMLVGA
     PWDGPSGDRR GDVYRCPVGG AHNAPCAKGH LGDYQLGNSS HPAVNMHLGM SLLETDGDGG
     FMACAPLWSR ACGSSVFSSG ICARVDASFQ PQGSLAPTAQ RCPTYMDVVI VLDGSNSIYP
     WSEVQTFLRR LVGKLFIDPE QIQVGLVQYG ESPVHEWSLG DFRTKEEVVR AAKNLSRREG
     RETKTAQAIM VACTEGFSQS HGGRPEAARL LVVVTDGESH DGEELPAALK ACEAGRVTRY
     GIAVLGHYLR RQRDPSSFLR EIRTIASDPD ERFFFNVTDE AALTDIVDAL GDRIFGLEGS
     HAENESSFGL EMSQIGFSTH RLKDGILFGM VGAYDWGGSV LWLEGGHRLF PPRMALEDEF
     PPALQNHAAY LGYSVSSMLL RGGRRLFLSG APRFRHRGKV IAFQLKKDGA VRVAQSLQGE
     QIGSYFGSEL CPLDTDRDGT TDVLLVAAPM FLGPQNKETG RVYVYLVGQQ SLLTLQGTLQ
     PEPPQDARFG FAMGALPDLN QDGFADVAVG APLEDGHQGA LYLYHGTQSG VRPHPAQRIA
     AASMPHALSY FGRSVDGRLD LDGDDLVDVA VGAQGAAILL SSRPIVHLTP SLEVTPQAIS
     VVQRDCRRRG QEAVCLTAAL CFQVTSRTPG RWDHQFYMRF TASLDEWTAG ARAAFDGSGQ
     RLSPRRLRLS VGNVTCEQLH FHVLDTSDYL RPVALTVTFA LDNTTKPGPV LNEGSPTSIQ
     KLVPFSKDCG PDNECVTDLV LQVNMDIRGS RKAPFVVRGG RRKVLVSTTL ENRKENAYNT
     SLSLIFSRNL HLASLTPQRE SPIKVECAAP SAHARLCSVG HPVFQTGAKV TFLLEFEFSC
     SSLLSQVFVK LTASSDSLER NGTLQDNTAQ TSAYIQYEPH LLFSSESTLH RYEVHPYGTL
     PVGPGPEFKT TLRVQNLGCY VVSGLIISAL LPAVAHGGNY FLSLSQVITN NASCIVQNLT
     EPPGPPVHPE ELQHTNRLNG SNTQCQVVRC HLGQLAKGTE VSVGLLRLVH NEFFRRAKFK
     SLTVVSTFEL GTEEGSVLQL TEASRWSESL LEVVQTRPIL ISLWILIGSV LGGLLLLALL
     VFCLWKLGFF AHKKIPEEEK REEKLEQ
//

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