CO4A3_MOUSE
ID CO4A3_MOUSE Reviewed; 1669 AA.
AC Q9QZS0; Q61430; Q61435; Q8CCD6;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Collagen alpha-3(IV) chain;
DE Contains:
DE RecName: Full=Tumstatin;
DE Flags: Precursor;
GN Name=Col4a3 {ECO:0000312|MGI:MGI:104688};
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] {ECO:0000312|EMBL:AAD50449.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryonic kidney {ECO:0000312|EMBL:AAD50449.1};
RX PubMed=10534397; DOI=10.1006/geno.1999.5943;
RA Lu W., Phillips C.L., Killen P.D., Hlaing T., Harrison W.R., Elder F.F.B.,
RA Miner J.H., Overbeek P.A., Meisler M.H.;
RT "Insertional mutation of the collagen genes Col4a3 and Col4a4 in a mouse
RT model of Alport syndrome.";
RL Genomics 61:113-124(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:CAA84529.1, ECO:0000312|PIR:I48302}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1424-1669, FUNCTION, INTERACTION WITH LAMB2,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:CAA84529.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:CAA84529.1};
RX PubMed=7962065; DOI=10.1083/jcb.127.3.879;
RA Miner J.H., Sanes J.R.;
RT "Collagen IV alpha 3, alpha 4, and alpha 5 chains in rodent basal laminae:
RT sequence, distribution, association with laminins, and developmental
RT switches.";
RL J. Cell Biol. 127:879-891(1994).
RN [4] {ECO:0000305, ECO:0000312|EMBL:CAA57689.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1491-1651.
RC STRAIN=129 {ECO:0000312|EMBL:CAA57689.1};
RC TISSUE=Epithelium {ECO:0000312|EMBL:CAA57689.1};
RA Oberbaeumer I.;
RT "Cloning of the NC1 domains fo the minor collagen IV chains of mouse via
RT PCR (RACE) reveals the presence of the mRNAs for alpha3 (IV) and alpha5
RT (IV) in differentiated teratocarcinoma cells.";
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:BAC28260.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1558-1669.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC28260.1};
RC TISSUE=Embryonic lung {ECO:0000312|EMBL:BAC28260.1};
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 [6] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=8956999; DOI=10.1101/gad.10.23.2981;
RA Cosgrove D., Meehan D.T., Grunkemeyer J.A., Kornak J.M., Sayers R.,
RA Hunter W.J., Samuelson G.C.;
RT "Collagen COL4A3 knockout: a mouse model for autosomal Alport syndrome.";
RL Genes Dev. 10:2981-2992(1996).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=12842087; DOI=10.1016/s1535-6108(03)00133-8;
RA Hamano Y., Zeisberg M., Sugimoto H., Lively J.C., Maeshima Y., Yang C.,
RA Hynes R.O., Werb Z., Sudhakar A., Kalluri R.;
RT "Physiological levels of tumstatin, a fragment of collagen IV alpha3 chain,
RT are generated by MMP-9 proteolysis and suppress angiogenesis via alphaV
RT beta3 integrin.";
RL Cancer Cell 3:589-601(2003).
RN [8] {ECO:0000305}
RP IDENTIFICATION IN A COMPLEX WITH COL4A4 AND COL4A5.
RX PubMed=14633121; DOI=10.1046/j.1523-1755.2003.00323.x;
RA Kobayashi T., Uchiyama M.;
RT "Characterization of assembly of recombinant type IV collagen alpha3,
RT alpha4, and alpha5 chains in transfected cell strains.";
RL Kidney Int. 64:1986-1996(2003).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=16877525; DOI=10.1096/fj.05-5565fje;
RA Miyoshi T., Hirohata S., Ogawa H., Doi M., Obika M., Yonezawa T., Sado Y.,
RA Kusachi S., Kyo S., Kondo S., Shiratori Y., Hudson B.G., Ninomiya Y.;
RT "Tumor-specific expression of the RGD-alpha3(IV)NC1 domain suppresses
RT endothelial tube formation and tumor growth in mice.";
RL FASEB J. 20:1904-1906(2006).
CC -!- FUNCTION: Type IV collagen is the major structural component of
CC glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork
CC together with laminins, proteoglycans and entactin/nidogen.
CC {ECO:0000250|UniProtKB:Q01955, ECO:0000269|PubMed:7962065}.
CC -!- FUNCTION: Tumstatin, a cleavage fragment corresponding to the collagen
CC alpha 3(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor
CC cell activity; these two anti-tumor properties may be regulated via
CC RGD-independent ITGB3-mediated mechanisms.
CC {ECO:0000250|UniProtKB:Q01955, ECO:0000269|PubMed:12842087,
CC ECO:0000269|PubMed:7962065}.
CC -!- SUBUNIT: There are six type IV collagen isoforms, alpha 1(IV)-alpha
CC 6(IV), each of which can form a triple helix structure with 2 other
CC chains to generate type IV collagen network. The alpha 3(IV) chain
CC forms a triple helical protomer with alpha 4(IV) and alpha 5(IV); this
CC triple helical structure dimerizes through NC1-NC1 domain interactions
CC such that the alpha 3(IV), alpha 4(IV) and alpha 5(IV) chains of one
CC protomer connect with the alpha 5(IV), alpha 4(IV) and alpha 3(IV)
CC chains of the opposite promoter, respectively (PubMed:14633121).
CC Interacts with ITGB3 (By similarity). Associates with LAMB2 at the
CC neuromuscular junction and in GBM (PubMed:7962065).
CC {ECO:0000250|UniProtKB:Q01955, ECO:0000269|PubMed:14633121,
CC ECO:0000269|PubMed:7962065}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000255|PROSITE-ProRule:PRU00736,
CC ECO:0000269|PubMed:7962065}. Note=Colocalizes with COL4A4 and COL4A5 in
CC GBM, tubular basement membrane (TBM) and synaptic basal lamina (BL).
CC {ECO:0000250|UniProtKB:Q01955, ECO:0000269|PubMed:7962065}.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney and lung. Detected at
CC lower levels in heart, muscle and skin. {ECO:0000269|PubMed:7962065}.
CC -!- DOMAIN: Alpha chains of type IV collagen have a non-collagenous domain
CC (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats
CC in the long central triple-helical domain (which may cause flexibility
CC in the triple helix), and a short N-terminal triple-helical 7S domain.
CC {ECO:0000250|UniProtKB:Q01955, ECO:0000255|PROSITE-ProRule:PRU00736}.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC {ECO:0000250|UniProtKB:Q01955, ECO:0000255|PROSITE-ProRule:PRU00736}.
CC -!- PTM: Type IV collagens contain numerous cysteine residues which are
CC involved in inter- and intramolecular disulfide bonding. 12 of these,
CC located in the NC1 domain, are conserved in all known type IV
CC collagens. {ECO:0000250|UniProtKB:Q01955, ECO:0000255|PROSITE-
CC ProRule:PRU00736}.
CC -!- PTM: The trimeric structure of the NC1 domains is stabilized by
CC covalent bonds between Lys and Met residues. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Thought to be phosphorylated by CERT, but CERT
CC does not have kinase activity. {ECO:0000250|UniProtKB:Q01955}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit normal pregnancy and wound healing,
CC but consistent with the human hereditary disorder Alport syndrome they
CC develop a progressive glomerulonephritis with microhematuria and
CC proteinuria. {ECO:0000269|PubMed:8956999}.
CC -!- SIMILARITY: Belongs to the type IV collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00736}.
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DR EMBL; AF169387; AAD50449.1; -; mRNA.
DR EMBL; AC123746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z35166; CAA84529.1; -; mRNA.
DR EMBL; X82205; CAA57689.1; -; mRNA.
DR EMBL; AK033387; BAC28260.1; -; mRNA.
DR CCDS; CCDS35631.1; -.
DR PIR; I48302; I48302.
DR PIR; S49488; S49488.
DR RefSeq; NP_031760.2; NM_007734.2.
DR AlphaFoldDB; Q9QZS0; -.
DR BioGRID; 198818; 4.
DR ComplexPortal; CPX-2961; Collagen type IV trimer variant 3.
DR STRING; 10090.ENSMUSP00000109084; -.
DR GlyGen; Q9QZS0; 2 sites.
DR iPTMnet; Q9QZS0; -.
DR PhosphoSitePlus; Q9QZS0; -.
DR MaxQB; Q9QZS0; -.
DR PaxDb; Q9QZS0; -.
DR PeptideAtlas; Q9QZS0; -.
DR PRIDE; Q9QZS0; -.
DR ProteomicsDB; 283474; -.
DR Antibodypedia; 34379; 312 antibodies from 32 providers.
DR DNASU; 12828; -.
DR Ensembl; ENSMUST00000113457; ENSMUSP00000109084; ENSMUSG00000079465.
DR GeneID; 12828; -.
DR KEGG; mmu:12828; -.
DR UCSC; uc007brv.1; mouse.
DR CTD; 1285; -.
DR MGI; MGI:104688; Col4a3.
DR VEuPathDB; HostDB:ENSMUSG00000079465; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000161675; -.
DR HOGENOM; CLU_002023_0_0_1; -.
DR InParanoid; Q9QZS0; -.
DR OMA; CVCKDKG; -.
DR OrthoDB; 63831at2759; -.
DR PhylomeDB; Q9QZS0; -.
DR TreeFam; TF316865; -.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1474244; Extracellular matrix organization.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-186797; Signaling by PDGF.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-2214320; Anchoring fibril formation.
DR Reactome; R-MMU-2243919; Crosslinking of collagen fibrils.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-MMU-419037; NCAM1 interactions.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12828; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Col4a3; mouse.
DR PRO; PR:Q9QZS0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9QZS0; protein.
DR Bgee; ENSMUSG00000079465; Expressed in epithelium of lens and 101 other tissues.
DR ExpressionAtlas; Q9QZS0; baseline and differential.
DR Genevisible; Q9QZS0; MM.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0005587; C:collagen type IV trimer; IDA:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IGI:MGI.
DR GO; GO:0072577; P:endothelial cell apoptotic process; ISS:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0032836; P:glomerular basement membrane development; IMP:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR Gene3D; 2.170.240.10; -; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR001442; Collagen_IV_NC.
DR InterPro; IPR036954; Collagen_IV_NC_sf.
DR InterPro; IPR016187; CTDL_fold.
DR Pfam; PF01413; C4; 2.
DR Pfam; PF01391; Collagen; 19.
DR SMART; SM00111; C4; 2.
DR SUPFAM; SSF56436; SSF56436; 2.
DR PROSITE; PS51403; NC1_IV; 1.
PE 1: Evidence at protein level;
KW Basement membrane; Cell adhesion; Collagen; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Phosphoprotein; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1669
FT /note="Collagen alpha-3(IV) chain"
FT /evidence="ECO:0000255"
FT /id="PRO_0000279698"
FT CHAIN 1424..1669
FT /note="Tumstatin"
FT /evidence="ECO:0000269|PubMed:7962065"
FT /id="PRO_0000279699"
FT DOMAIN 1444..1668
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT REGION 29..42
FT /note="7S domain"
FT /evidence="ECO:0000250|UniProtKB:Q01955"
FT REGION 43..1436
FT /note="Triple-helical region"
FT REGION 44..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..1439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1425..1443
FT /note="Epitope recognized by Goodpasture antibodies"
FT /evidence="ECO:0000250|UniProtKB:Q01955"
FT REGION 1478..1556
FT /note="Required for the anti-angiogenic activity of
FT tumstatin"
FT /evidence="ECO:0000250|UniProtKB:Q01955"
FT REGION 1609..1627
FT /note="Required for the anti-tumor cell activity of
FT tumstatin"
FT /evidence="ECO:0000250|UniProtKB:Q01955"
FT MOTIF 830..832
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 994..996
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1152..1154
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1304..1306
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 189..204
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..383
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..438
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..621
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..670
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..707
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1111
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1146
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1231
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1424..1425
FT /note="Cleavage; by collagenase"
FT /evidence="ECO:0000250"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1459..1550
FT /note="Or C-1459 with C-1547"
FT /evidence="ECO:0000250|UniProtKB:Q01955,
FT ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1492..1547
FT /note="Or C-1492 with C-1550"
FT /evidence="ECO:0000250|UniProtKB:Q01955,
FT ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1504..1510
FT /evidence="ECO:0000250|UniProtKB:Q01955,
FT ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1569..1664
FT /note="Or C-1569 with C-1661"
FT /evidence="ECO:0000250|UniProtKB:Q01955,
FT ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1603..1661
FT /note="Or C-1603 with C-1664"
FT /evidence="ECO:0000250|UniProtKB:Q01955,
FT ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1615..1621
FT /evidence="ECO:0000250|UniProtKB:Q01955,
FT ECO:0000255|PROSITE-ProRule:PRU00736"
FT CROSSLNK 1532
FT /note="S-Lysyl-methionine sulfilimine (Met-Lys) (interchain
FT with K-1650)"
FT /evidence="ECO:0000250"
FT CROSSLNK 1650
FT /note="S-Lysyl-methionine sulfilimine (Lys-Met) (interchain
FT with M-1532)"
FT /evidence="ECO:0000250"
FT CONFLICT 1041
FT /note="L -> R (in Ref. 1; AAD50449)"
FT /evidence="ECO:0000305"
FT CONFLICT 1594
FT /note="G -> R (in Ref. 3; CAA57689)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1669 AA; 161726 MW; 2E976B2F2E66D28E CRC64;
MHSKTAPRFL VFLLLTLLLL LAASPVASKG CVCKGKGQCL CAGTKGEKGE KGVPGSPGFP
GQKGFPGPEG LPGPQGPKGS PGLPGLTGPK GIRGITGLPG FAGPPGLPGL PGHPGPRGLA
GLPGCNGSKG EQGFPGFPGT PGYAGLPGPD GLKGQKGEPA QGEDRGFNGK GDPGPPGVPG
FQGFPGLPGF PGPAGPPGPP GFFGLPGAMG PRGPKGHMGD SVIGQKGERG MKGLTGPPGP
PGTVIFTLTQ PYNKSDFKGE KGDEGERGEP GPPGPSGPPG DSYGSEKGAP GEPGPRGKPG
KDGAPGFPGT EGAKGNRGFP GLRGEAGIKG RKGDIGPPGF PGPTEYYDAY LEKGERGMPG
LPGPKGARGP QGPSGPPGVP GSPGLSRPGL RGPIGWPGLK GSKGERGPPG KDTVGPPGPL
GCPGSPGPPG PPGPPGCPGD IVFKCSPGEH GMPGDTGPPG VPGLDGPKGE PGSPCTECHC
FPGPPGVPGF PGLDGIKGIP GGRGVPGLKG NPGSPGSAGL PGFAGFPGDQ GHPGLKGDKG
DTPLPWGQVG NPGDPGLRGL PGRKGFDGTP GGPGAKGPPG PQGEPALSGR KGDQGPPGPP
GFPGPPGPAG PAGPPGYGPQ GEPGPKGAQG VPGVLGPPGE AGLKGEPSTS TPDLGPPGPP
GPPGQAGPRG LPGLPGPVGK CDPGLPGPDG EPGIPEAGCP GPPGPKGNQG FPGTKGSPGC
PGEMGKPGRP GEPGIPGAKG EPSVGRPGKP GKPGFPGERG NAGENGDIGL PGLPGLPGTP
GRGGLDGPPG DPGQPGSPGA KGSPGRCIPG PRGTQGLPGL NGLKGQPGRR GDTGPKGDPG
IPGMDRSGVP GDPGPPGTPG CPGEMGPPGQ KGYPGAPGFP GPPGEKGEVG MMGYPGTTGP
PGLPGKPGSQ GQRGSLGIPG MKGEKGRPGA KGERGEKGKP GPSQTTLLKG DKGEPGLKGF
VGNPGEKGNR GNPGLPGPKG LEGLPGLPGP PGPRGDTGSR GNPGRPGPHG MPGSMGIMGV
PGPKGRKGTS GLPGLAGRPG LTGIHGPQGD KGEPGYSEGA RPGPPGPKGD PGLPGDKGKK
GERGVPGPPG QSGPAGPDGA PGSPGSPGHP GKPGPAGDLG LKGQKGFPGP PGSTGPPGPP
GLPGLPGPMG MRGDQGRDGI PGPPGEKGET GLLGAYPGPK GSPGVPGAKG DRGVPGLSGL
PGRKGVMGDV GPQGPPGTAG LPGPPGLPGA IIPGPKGDRG LPGLRGNPGE PGPPGPPGPI
GKGIKGDKGF MGPPGPKGLP GTVGDMGPPG FPGAPGTPGL PGVRGDPGFP GFPGIKGEKG
NPGFLGPIGH PGPVGPKGPP GPRGKPGTLK VISLPGSPGP PGVPGQPGMK GDPGPLGLPG
IPGPCGPRGK PGKDGKPGTP GPAGTKGNKG LKGQQGPPGL DGLPGLKGNP GDRGTPATGT
RMRGFIFTRH SQTTAIPSCP EGTQPLYSGF SLLFVQGNKR AHGQDLGTLG SCLQRFTTMP
FLFCNINNVC NFASRNDYSY WLSTPALMPM DMAPISGRAL EPYISRCTVC EGPAMAIAVH
SQTTAIPPCP QDWVSLWKGF SFIMFTSAGS EGAGQALASP GSCLEEFRAS PFIECHGRGT
CNYYSNSYSF WLASLNPERM FRKPIPSTVK AGDLEKIISR CQVCMKKRH
