(data stored in ACNUC8465 zone)

SWISSPROT: MP2K5_MOUSE

ID   MP2K5_MOUSE             Reviewed;         448 AA.
AC   Q9WVS7; Q8CFM3; Q8K360; Q9D222;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   11-DEC-2019, entry version 159.
DE   RecName: Full=Dual specificity mitogen-activated protein kinase kinase 5;
DE            Short=MAP kinase kinase 5;
DE            Short=MAPKK 5;
DE            EC=2.7.12.2;
DE   AltName: Full=MAPK/ERK kinase 5;
DE            Short=MEK 5;
GN   Name=Map2k5; Synonyms=Mek5, Mkk5, Prkmk5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND MUTAGENESIS OF
RP   SER-311 AND THR-315.
RC   TISSUE=Brain;
RX   PubMed=10473620; DOI=10.1074/jbc.274.37.26563;
RA   Kamakura S., Moriguchi T., Nishida E.;
RT   "Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases.
RT   Identification and characterization of a signaling pathway to the
RT   nucleus.";
RL   J. Biol. Chem. 274:26563-26571(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   STRAIN=C57BL/6J; TISSUE=Head, and Hypothalamus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=Czech II; TISSUE=Mammary gland;
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).
RN   [4]
RP   INTERACTION WITH SQSTM1; PRKCZ; PRKCI; PARD6A AND MAP3K3, AND DOMAIN.
RX   PubMed=12813044; DOI=10.1074/jbc.m303221200;
RA   Lamark T., Perander M., Outzen H., Kristiansen K., Oevervatn A.,
RA   Michaelsen E., Bjoerkoey G., Johansen T.;
RT   "Interaction codes within the family of mammalian Phox and Bem1p domain-
RT   containing proteins.";
RL   J. Biol. Chem. 278:34568-34581(2003).
RN   [5]
RP   FUNCTION, DOMAIN, INTERACTION WITH MAP3K2 AND MAPK7, AND MUTAGENESIS OF
RP   ARG-20; ILE-21; ASP-64; GLU-65; GLY-67 AND ASP-68.
RX   PubMed=16507987; DOI=10.1128/mcb.26.6.2065-2079.2006;
RA   Nakamura K., Uhlik M.T., Johnson N.L., Hahn K.M., Johnson G.L.;
RT   "PB1 domain-dependent signaling complex is required for extracellular
RT   signal-regulated kinase 5 activation.";
RL   Mol. Cell. Biol. 26:2065-2079(2006).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   STRUCTURE BY NMR OF 7-107.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the PB1 domain of mouse mitogen activated protein
RT   kinase kinase 5 (MAP2K5).";
RL   Submitted (JAN-2006) to the PDB data bank.
CC   -!- FUNCTION: Acts as a scaffold for the formation of a ternary
CC       MAP3K2/MAP3K3-MAP3K5-MAPK7 signaling complex. Activation of this
CC       pathway appears to play a critical role in protecting cells from
CC       stress-induced apoptosis, neuronal survival and cardiac development and
CC       angiogenesis. {ECO:0000269|PubMed:10473620,
CC       ECO:0000269|PubMed:16507987}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.12.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- SUBUNIT: Interacts with PARD6A, MAP3K3 and MAPK7. Forms a complex with
CC       SQSTM1 and PRKCZ or PRKCI. {ECO:0000269|PubMed:12813044,
CC       ECO:0000269|PubMed:16507987}.
CC   -!- INTERACTION:
CC       Q61083:Map3k2; NbExp=4; IntAct=EBI-446144, EBI-446134;
CC       Q61084:Map3k3; NbExp=15; IntAct=EBI-446144, EBI-446250;
CC       P28656:Nap1l1; NbExp=20; IntAct=EBI-446144, EBI-645055;
CC       Q64337:Sqstm1; NbExp=3; IntAct=EBI-446144, EBI-645025;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9WVS7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9WVS7-2; Sequence=VSP_015840;
CC       Name=3;
CC         IsoId=Q9WVS7-3; Sequence=VSP_015838, VSP_015839;
CC       Name=4;
CC         IsoId=Q9WVS7-4; Sequence=VSP_015836, VSP_015837;
CC   -!- DOMAIN: Binds MAP3K2/MAP3K3 and MAPK7 via non-overlapping residues of
CC       the PB1 domain. This domain also mediates interactions with SQSTM1 and
CC       PARD6A. {ECO:0000269|PubMed:12813044, ECO:0000269|PubMed:16507987}.
CC   -!- PTM: Activated by phosphorylation on Ser/Thr by MAP kinase kinase
CC       kinases. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
DR   EMBL; AB019374; BAA82040.1; -; mRNA.
DR   EMBL; AK020716; BAB32187.1; -; mRNA.
DR   EMBL; BC013697; AAH13697.1; -; mRNA.
DR   EMBL; BC028260; AAH28260.1; -; mRNA.
DR   CCDS; CCDS23269.1; -. [Q9WVS7-1]
DR   RefSeq; NP_035970.1; NM_011840.2. [Q9WVS7-1]
DR   RefSeq; XP_006511208.1; XM_006511145.2.
DR   PDB; 1WI0; NMR; -; A=8-107.
DR   PDBsum; 1WI0; -.
DR   SMR; Q9WVS7; -.
DR   CORUM; Q9WVS7; -.
DR   IntAct; Q9WVS7; 11.
DR   STRING; 10090.ENSMUSP00000034920; -.
DR   iPTMnet; Q9WVS7; -.
DR   PhosphoSitePlus; Q9WVS7; -.
DR   PaxDb; Q9WVS7; -.
DR   PRIDE; Q9WVS7; -.
DR   Ensembl; ENSMUST00000034920; ENSMUSP00000034920; ENSMUSG00000058444. [Q9WVS7-1]
DR   GeneID; 23938; -.
DR   KEGG; mmu:23938; -.
DR   UCSC; uc009qaw.1; mouse. [Q9WVS7-1]
DR   UCSC; uc009qaz.1; mouse. [Q9WVS7-4]
DR   UCSC; uc012guv.1; mouse. [Q9WVS7-2]
DR   CTD; 5607; -.
DR   MGI; MGI:1346345; Map2k5.
DR   eggNOG; KOG0581; Eukaryota.
DR   eggNOG; ENOG410XQ5A; LUCA.
DR   GeneTree; ENSGT00940000157505; -.
DR   HOGENOM; HOG000234206; -.
DR   InParanoid; Q9WVS7; -.
DR   KO; K04463; -.
DR   OMA; QIYPRAC; -.
DR   OrthoDB; 688282at2759; -.
DR   PhylomeDB; Q9WVS7; -.
DR   TreeFam; TF106468; -.
DR   ChiTaRS; Map2k5; mouse.
DR   EvolutionaryTrace; Q9WVS7; -.
DR   PRO; PR:Q9WVS7; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q9WVS7; protein.
DR   Bgee; ENSMUSG00000058444; Expressed in 281 organ(s), highest expression level in internal carotid artery.
DR   Genevisible; Q9WVS7; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005819; C:spindle; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; ISO:MGI.
DR   GO; GO:0004708; F:MAP kinase kinase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000187; P:activation of MAPK activity; ISO:MGI.
DR   GO; GO:0032147; P:activation of protein kinase activity; IBA:GO_Central.
DR   GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:MGI.
DR   GO; GO:0070375; P:ERK5 cascade; ISO:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR   GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; ISO:MGI.
DR   GO; GO:2000342; P:negative regulation of chemokine (C-X-C motif) ligand 2 production; ISO:MGI.
DR   GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR   GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
DR   GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISO:MGI.
DR   GO; GO:0045415; P:negative regulation of interleukin-8 biosynthetic process; ISO:MGI.
DR   GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR   GO; GO:0060761; P:negative regulation of response to cytokine stimulus; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISO:MGI.
DR   GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
DR   GO; GO:0023014; P:signal transduction by protein phosphorylation; IBA:GO_Central.
DR   CDD; cd06395; PB1_Map2k5; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000270; PB1_dom.
DR   InterPro; IPR034851; PB1_MAP2K5.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00564; PB1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00666; PB1; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS51745; PB1; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q9WVS7.
DR   SWISS-2DPAGE; Q9WVS7.
KW   3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Kinase;
KW   Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Tyrosine-protein kinase.
FT   CHAIN           1..448
FT                   /note="Dual specificity mitogen-activated protein kinase
FT                   kinase 5"
FT                   /id="PRO_0000086384"
FT   DOMAIN          18..109
FT                   /note="PB1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT   DOMAIN          166..419
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         172..180
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          18..25
FT                   /note="Interaction with MAPK7"
FT                   /evidence="ECO:0000269|PubMed:16507987"
FT   REGION          64..68
FT                   /note="Interaction with MAP3K2/MAP3K3"
FT                   /evidence="ECO:0000269|PubMed:12813044,
FT                   ECO:0000269|PubMed:16507987"
FT   REGION          117..131
FT                   /note="Interaction with MAPK7"
FT                   /evidence="ECO:0000269|PubMed:16507987"
FT   ACT_SITE        283
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         195
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         311
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13163"
FT   MOD_RES         315
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13163"
FT   VAR_SEQ         108..118
FT                   /note="ACKPPGERNIH -> GYRRGSRLREY (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_015836"
FT   VAR_SEQ         119..448
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_015837"
FT   VAR_SEQ         183..186
FT                   /note="AHHV -> LLHI (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_015838"
FT   VAR_SEQ         187..448
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_015839"
FT   VAR_SEQ         359..367
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_015840"
FT   MUTAGEN         20
FT                   /note="R->A: Loss of MAPK7 binding; when associated with A-
FT                   21."
FT                   /evidence="ECO:0000269|PubMed:16507987"
FT   MUTAGEN         21
FT                   /note="I->A: Loss of MAPK7 binding; when associated with A-
FT                   20."
FT                   /evidence="ECO:0000269|PubMed:16507987"
FT   MUTAGEN         64
FT                   /note="D->A: Loss of MAP3K2/MAP3K3 binding; when associated
FT                   with A-65."
FT                   /evidence="ECO:0000269|PubMed:16507987"
FT   MUTAGEN         65
FT                   /note="E->A: Loss of MAP3K2/MAP3K3 binding; when associated
FT                   with A-64."
FT                   /evidence="ECO:0000269|PubMed:16507987"
FT   MUTAGEN         67
FT                   /note="G->A: Loss of MAP3K2/MAP3K3 binding; when associated
FT                   with A-68."
FT                   /evidence="ECO:0000269|PubMed:16507987"
FT   MUTAGEN         68
FT                   /note="D->A: Loss of MAP3K2/MAP3K3 binding; when associated
FT                   with A-67."
FT                   /evidence="ECO:0000269|PubMed:16507987"
FT   MUTAGEN         311
FT                   /note="S->A: Dominant negative form; when associated with
FT                   V-315."
FT                   /evidence="ECO:0000269|PubMed:10473620"
FT   MUTAGEN         311
FT                   /note="S->D: Dominant active form; when associated with D-
FT                   315."
FT                   /evidence="ECO:0000269|PubMed:10473620"
FT   MUTAGEN         315
FT                   /note="T->D: Dominant active form; when associated with D-
FT                   311."
FT                   /evidence="ECO:0000269|PubMed:10473620"
FT   MUTAGEN         315
FT                   /note="T->V: Dominant negative form; when associated with
FT                   A-311."
FT                   /evidence="ECO:0000269|PubMed:10473620"
FT   STRAND          17..22
FT                   /evidence="ECO:0000244|PDB:1WI0"
FT   STRAND          28..34
FT                   /evidence="ECO:0000244|PDB:1WI0"
FT   STRAND          36..38
FT                   /evidence="ECO:0000244|PDB:1WI0"
FT   HELIX           41..51
FT                   /evidence="ECO:0000244|PDB:1WI0"
FT   STRAND          60..62
FT                   /evidence="ECO:0000244|PDB:1WI0"
FT   STRAND          70..74
FT                   /evidence="ECO:0000244|PDB:1WI0"
FT   HELIX           75..95
FT                   /evidence="ECO:0000244|PDB:1WI0"
FT   STRAND          102..106
FT                   /evidence="ECO:0000244|PDB:1WI0"
SQ   SEQUENCE   448 AA;  50105 MW;  50C50E8F0F712BE7 CRC64;
     MLWLALGPFC AMENQVLVIR IKIPNSGAVD WTVHSGPQLL FRDVLDVIGQ VLPEATTTAF
     EYEDEDGDRI TVRSDEEMKA MLSYYYSTVM EQQVNGQLIE PLQIFPRACK PPGERNIHGL
     KVNTRAGPSQ HTSPVVSDSL PSNSLKKSSA ELRKILANGQ MNEQDIRYRD TLGHGNGGTV
     YKAHHVPSGK ILAVKVILLD ITLELQKQIM SELEILYKCD SSYIIGFYGA FFVENRISIC
     TEFMDGGSLD VYRKIPEHVL GRIAVAVVKG LTYLWSLKIL HRDVKPSNML VNTGGQVKLC
     DFGVSTQLVN SIAKTYVGTN AYMAPERISG EQYGIHSDVW SLGISFMELA LGRFPYPQIQ
     KNQGSLMPLQ LLQCIVDEDS PVLPLGEFSE PFVHFITQCM RKQPKERPAP EELMGHPFIV
     QFNDGNSTVV SMWVCRALEE RRSQQGPP
//

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