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   27-MAR-2024, entry version 164.
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   SMR; Q9QZS0; -.
DR   BioGRID; 198818; 4.
DR   ComplexPortal; CPX-2961; Collagen type IV trimer variant 3.
DR   STRING; 10090.ENSMUSP00000109084; -.
DR   GlyCosmos; Q9QZS0; 2 sites, No reported glycans.
DR   GlyGen; Q9QZS0; 2 sites.
DR   iPTMnet; Q9QZS0; -.
DR   PhosphoSitePlus; Q9QZS0; -.
DR   MaxQB; Q9QZS0; -.
DR   PaxDb; 10090-ENSMUSP00000109084; -.
DR   PeptideAtlas; Q9QZS0; -.
DR   ProteomicsDB; 283474; -.
DR   Antibodypedia; 34379; 346 antibodies from 32 providers.
DR   DNASU; 12828; -.
DR   Ensembl; ENSMUST00000113457.9; ENSMUSP00000109084.3; ENSMUSG00000079465.9.
DR   GeneID; 12828; -.
DR   KEGG; mmu:12828; -.
DR   UCSC; uc007brv.1; mouse.
DR   AGR; MGI:104688; -.
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; KGPPGRC; -.
DR   OrthoDB; 2882192at2759; -.
DR   PhylomeDB; Q9QZS0; -.
DR   TreeFam; TF316865; -.
DR   BioGRID-ORCS; 12828; 2 hits in 75 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 cell types or tissues.
DR   ExpressionAtlas; Q9QZS0; baseline and differential.
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:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; 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; Collagen IV, non-collagenous; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR001442; Collagen_IV_NC.
DR   InterPro; IPR036954; Collagen_IV_NC_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1077; COLLAGEN ALPHA-3(IV) CHAIN; 1.
DR   Pfam; PF01413; C4; 2.
DR   Pfam; PF01391; Collagen; 19.
DR   SMART; SM00111; C4; 2.
DR   SUPFAM; SSF56436; C-type lectin-like; 2.
DR   PROSITE; PS51403; NC1_IV; 1.
DR   Genevisible; Q9QZS0; MM.
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
//