CO4A2_MOUSE
ID CO4A2_MOUSE Reviewed; 1707 AA.
AC P08122; Q3B7C2; Q3TPV9; Q61375; Q66JS5; Q6RCT6; Q6RCT7; Q6U9X1; Q8BPI9;
AC Q8BPK3; Q91VI3;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 4.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Collagen alpha-2(IV) chain {ECO:0000305};
DE Contains:
DE RecName: Full=Canstatin;
DE Flags: Precursor;
GN Name=Col4a2 {ECO:0000312|MGI:MGI:88455};
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].
RX PubMed=2703491; DOI=10.1016/s0021-9258(18)83350-6;
RA Saus J., Quinones S., Mackrell A., Blumberg B., Muthukumaran G.,
RA Pihlajaniemi T., Kurkinen M.;
RT "The complete primary structure of mouse alpha 2(IV) collagen. Alignment
RT with mouse alpha 1(IV) collagen.";
RL J. Biol. Chem. 264:6318-6324(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-538 AND 1649-1707.
RC STRAIN=C57BL/6J; TISSUE=Eye, and Spinal cord;
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] OF 1-276 AND 1339-1707.
RC 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-60.
RX PubMed=3200851; DOI=10.1073/pnas.85.24.9679;
RA Burbelo P.D., Martin G.R., Yamada Y.;
RT "Alpha 1(IV) and alpha 2(IV) collagen genes are regulated by a
RT bidirectional promoter and a shared enhancer.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:9679-9682(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RX PubMed=3198626; DOI=10.1016/s0021-9258(19)77629-7;
RA Kaytes P., Wood L., Theriault N., Kurkinen M., Vogeli G.;
RT "Head-to-head arrangement of murine type IV collagen genes.";
RL J. Biol. Chem. 263:19274-19277(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 964-1003; 1005-1085 AND
RP 1087-1109.
RX PubMed=3839908; DOI=10.1038/317177a0;
RA Kurkinen M., Bernard M.P., Barlow D.P., Chow L.T.;
RT "Characterization of 64-, 123- and 182-base-pair exons in the mouse alpha
RT 2(IV) collagen gene.";
RL Nature 317:177-179(1985).
RN [7]
RP NUCLEOTIDE SEQUENCE OF 970-1480.
RX PubMed=3011432; DOI=10.1111/j.1432-1033.1986.tb09636.x;
RA Schwarz U., Schuppan D., Oberbaeumer I., Glanville R.W., Deutzmann R.,
RA Timpl R., Kuehn K.;
RT "Structure of mouse type IV collagen. Amino-acid sequence of the C-terminal
RT 511-residue-long triple-helical segment of the alpha 2(IV) chain and its
RT comparison with the alpha 1(IV) chain.";
RL Eur. J. Biochem. 157:49-56(1986).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1041-1489.
RX PubMed=3758345; DOI=10.1016/0014-5793(86)81334-5;
RA Vogeli G., Horn E., Carter J., Kaytes P.S.;
RT "Proposed alignment of helical interruptions in the two subunits of the
RT basement membrane (type IV) collagen.";
RL FEBS Lett. 206:29-32(1986).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1480-1707.
RX PubMed=3780963; DOI=10.1016/0014-5793(86)81018-3;
RA Schwarz-Magdolen U., Oberbaeumer I., Kuehn K.;
RT "cDNA and protein sequence of the NC1 domain of the alpha 2-chain of
RT collagen IV and its comparison with alpha 1(IV).";
RL FEBS Lett. 208:203-207(1986).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1481-1707, AND FUNCTION OF CANSTATIN.
RX PubMed=3597383; DOI=10.1016/s0021-9258(18)47441-8;
RA Kurkinen M., Condon M.R., Blumberg B., Barlow D., Quinones S., Saus J.,
RA Pihlajaniemi T.;
RT "Extensive homology between the carboxyl-terminal peptides of mouse alpha
RT 1(IV) and alpha 2(IV) collagen.";
RL J. Biol. Chem. 262:8496-8499(1987).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1481-1707.
RC STRAIN=BALB/cJ;
RX PubMed=15592653; DOI=10.1093/abbs/36.12.845;
RA Hou W.H., Wang T.Y., Yuan B.M., Chai Y.R., Jia Y.L., Tian F., Wang J.M.,
RA Xue L.X.;
RT "Recombinant mouse canstatin inhibits chicken embryo chorioallantoic
RT membrane angiogenesis and endothelial cell proliferation.";
RL Acta Biochim. Biophys. Sin. 36:845-850(2004).
RN [12]
RP INTERACTION WITH EFEMP2.
RX PubMed=17324935; DOI=10.1074/jbc.m611029200;
RA Kobayashi N., Kostka G., Garbe J.H., Keene D.R., Baechinger H.P.,
RA Hanisch F.G., Markova D., Tsuda T., Timpl R., Chu M.L., Sasaki T.;
RT "A comparative analysis of the fibulin protein family. Biochemical
RT characterization, binding interactions, and tissue localization.";
RL J. Biol. Chem. 282:11805-11816(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
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 [14]
RP BROMINATION AT TYR-1485, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=32571911; DOI=10.1073/pnas.2007749117;
RA He C., Song W., Weston T.A., Tran C., Kurtz I., Zuckerman J.E.,
RA Guagliardo P., Miner J.H., Ivanov S.V., Bougoure J., Hudson B.G., Colon S.,
RA Voziyan P.A., Bhave G., Fong L.G., Young S.G., Jiang H.;
RT "Peroxidasin-mediated bromine enrichment of basement membranes.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:15827-15836(2020).
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:0000269|PubMed:3597383}.
CC -!- FUNCTION: Canstatin, a cleavage product corresponding to the collagen
CC alpha 2(IV) NC1 domain, possesses both anti-angiogenic and anti-tumor
CC cell activity. It inhibits proliferation and migration of endothelial
CC cells, reduces mitochondrial membrane potential, and induces apoptosis.
CC Specifically induces Fas-dependent apoptosis and activates procaspase-8
CC and -9 activity. Ligand for alphavbeta3 and alphavbeta5 integrins (By
CC similarity). {ECO:0000250}.
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. Interacts with EFEMP2
CC (PubMed:17324935). {ECO:0000269|PubMed:17324935}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000255|PROSITE-ProRule:PRU00736}.
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 -!- 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 -!- 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.
CC -!- PTM: Proteolytic processing produces the C-terminal NC1 peptide,
CC canstatin. {ECO:0000250}.
CC -!- PTM: The trimeric structure of the NC1 domains is stabilized by
CC covalent bonds between Lys and Met residues. {ECO:0000250}.
CC -!- PTM: Brominated by PXDN. {ECO:0000269|PubMed:32571911}.
CC -!- SIMILARITY: Belongs to the type IV collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00736}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH80789.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 277.; Evidence={ECO:0000305};
CC Sequence=AAI07686.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 277.; Evidence={ECO:0000305};
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DR EMBL; J04695; AAA50293.1; -; mRNA.
DR EMBL; AK053858; BAC35559.1; -; mRNA.
DR EMBL; AK075619; BAC35863.1; -; mRNA.
DR EMBL; AK164096; BAE37626.1; -; mRNA.
DR EMBL; BC013560; AAH13560.2; -; mRNA.
DR EMBL; BC080789; AAH80789.1; ALT_SEQ; mRNA.
DR EMBL; BC107685; AAI07686.1; ALT_SEQ; mRNA.
DR EMBL; M23334; AAA51626.1; -; mRNA.
DR EMBL; M23333; AAA51626.1; JOINED; Genomic_DNA.
DR EMBL; J04448; AAA37438.1; -; Genomic_DNA.
DR EMBL; X02896; CAA26655.1; -; mRNA.
DR EMBL; X02897; CAB51614.1; -; Genomic_DNA.
DR EMBL; X02898; CAA26657.1; -; Genomic_DNA.
DR EMBL; X02899; CAA26658.1; -; Genomic_DNA.
DR EMBL; X04410; CAA27998.1; -; mRNA.
DR EMBL; X04647; CAA28308.1; -; mRNA.
DR EMBL; M15833; AAA37341.1; -; mRNA.
DR EMBL; AY375463; AAQ83370.1; -; mRNA.
DR EMBL; AY502946; AAR89901.1; -; mRNA.
DR EMBL; AY502947; AAR89902.1; -; mRNA.
DR CCDS; CCDS40220.1; -.
DR PIR; A33526; A33526.
DR RefSeq; NP_034062.3; NM_009932.4.
DR AlphaFoldDB; P08122; -.
DR BioGRID; 198817; 8.
DR ComplexPortal; CPX-2959; Collagen type IV trimer variant 1.
DR STRING; 10090.ENSMUSP00000033899; -.
DR GlyGen; P08122; 2 sites.
DR iPTMnet; P08122; -.
DR PhosphoSitePlus; P08122; -.
DR SwissPalm; P08122; -.
DR MaxQB; P08122; -.
DR PaxDb; P08122; -.
DR PRIDE; P08122; -.
DR ProteomicsDB; 283542; -.
DR Antibodypedia; 4381; 232 antibodies from 28 providers.
DR DNASU; 12827; -.
DR Ensembl; ENSMUST00000033899; ENSMUSP00000033899; ENSMUSG00000031503.
DR GeneID; 12827; -.
DR KEGG; mmu:12827; -.
DR UCSC; uc009kvc.2; mouse.
DR CTD; 1284; -.
DR MGI; MGI:88455; Col4a2.
DR VEuPathDB; HostDB:ENSMUSG00000031503; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000157234; -.
DR HOGENOM; CLU_002023_1_0_1; -.
DR InParanoid; P08122; -.
DR OMA; HNGTEWI; -.
DR OrthoDB; 63831at2759; -.
DR PhylomeDB; P08122; -.
DR TreeFam; TF344135; -.
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; 12827; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Col4a2; mouse.
DR PRO; PR:P08122; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P08122; protein.
DR Bgee; ENSMUSG00000031503; Expressed in epithelium of lens and 261 other tissues.
DR ExpressionAtlas; P08122; baseline and differential.
DR Genevisible; P08122; 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:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:UniProtKB.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IGI:MGI.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
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; 16.
DR SMART; SM00111; C4; 2.
DR SUPFAM; SSF56436; SSF56436; 2.
DR PROSITE; PS51403; NC1_IV; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Basement membrane; Bromination; Collagen; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..25
FT PROPEP 26..183
FT /note="N-terminal propeptide (7S domain)"
FT /id="PRO_0000005826"
FT CHAIN 184..1707
FT /note="Collagen alpha-2(IV) chain"
FT /id="PRO_0000005827"
FT CHAIN 1481..1707
FT /note="Canstatin"
FT /id="PRO_0000390487"
FT DOMAIN 1484..1707
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT REGION 60..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..1479
FT /note="Triple-helical region"
FT REGION 266..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..442
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..651
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 745..763
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1485
FT /note="3'-bromotyrosine"
FT /evidence="ECO:0000269|PubMed:32571911"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1499..1588
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1532..1585
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1544..1550
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1607..1703
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1641..1700
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1653..1660
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT CONFLICT 275
FT /note="E -> K (in Ref. 3; AAH80789)"
FT /evidence="ECO:0000305"
FT CONFLICT 626
FT /note="E -> R (in Ref. 1; AAA50293)"
FT /evidence="ECO:0000305"
FT CONFLICT 837
FT /note="G -> A (in Ref. 1; AAA50293)"
FT /evidence="ECO:0000305"
FT CONFLICT 1051
FT /note="P -> R (in Ref. 8; CAA27998)"
FT /evidence="ECO:0000305"
FT CONFLICT 1097
FT /note="S -> G (in Ref. 6; CAA26655)"
FT /evidence="ECO:0000305"
FT CONFLICT 1171
FT /note="G -> S (in Ref. 8; CAA27998)"
FT /evidence="ECO:0000305"
FT CONFLICT 1179
FT /note="P -> R (in Ref. 8; CAA27998)"
FT /evidence="ECO:0000305"
FT CONFLICT 1241
FT /note="Q -> E (in Ref. 8; CAA27998)"
FT /evidence="ECO:0000305"
FT CONFLICT 1328
FT /note="P -> A (in Ref. 8; CAA27998)"
FT /evidence="ECO:0000305"
FT CONFLICT 1573
FT /note="V -> L (in Ref. 9; CAA28308)"
FT /evidence="ECO:0000305"
FT CONFLICT 1583
FT /note="S -> I (in Ref. 11; AAR89902/AAQ83370)"
FT /evidence="ECO:0000305"
FT CONFLICT 1623
FT /note="H -> Y (in Ref. 1; AAA50293 and 10; AAA37341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1707 AA; 167325 MW; 67CB3E3CB2A5B1F6 CRC64;
MDRVRFKASG PPLRGWLLLA TVTVGLLAQS VLGGVKKLDV PCGGRDCSGG CQCYPEKGAR
GQPGAVGPQG YNGPPGLQGF PGLQGRKGDK GERGVPGPTG PKGDVGARGV SGFPGADGIP
GHPGQGGPRG RPGYDGCNGT RGDAGPQGPS GSGGFPGLPG PQGPKGQKGE PYALSKEDRD
KYRGEPGEPG LVGYQGPPGR PGPIGQMGPM GAPGRPGPPG PPGPKGQPGN RGLGFYGQKG
EKGDIGQPGP NGIPSDITLV GPTTSTIHPD LYKGEKGDEG EQGIPGVISK GEEGIMGFPG
IRGFPGLDGE KGVVGQKGSR GLDGFQGPSG PRGPKGERGE QGPPGPSVYS PHPSLAKGAR
GDPGFQGAHG EPGSRGEPGE PGTAGPPGPS VGDEDSMRGL PGEMGPKGFS GEPGSPARYL
GPPGADGRPG PQGVPGPAGP PGPDGFLFGL KGSEGRVGYP GPSGFPGTRG QKGWKGEAGD
CQCGQVIGGL PGLPGPKGFP GVNGELGKKG DQGDPGLHGI PGFPGFKGAP GVAGAPGPKG
IKGDSRTITT KGERGQPGIP GVHGMKGDDG VPGRDGLDGF PGLPGPPGDG IKGPPGDAGL
PGVPGTKGFP GDIGPPGQGL PGPKGERGFP GDAGLPGPPG FPGPPGPPGT PGQRDCDTGV
KRPIGGGQQV VVQPGCIEGP TGSPGQPGPP GPTGAKGVRG MPGFPGASGE QGLKGFPGDP
GREGFPGPPG FMGPRGSKGT TGLPGPDGPP GPIGLPGPAG PPGDRGIPGE VLGAQPGTRG
DAGLPGQPGL KGLPGETGAP GFRGSQGMPG MPGLKGQPGF PGPSGQPGQS GPPGQHGFPG
TPGREGPLGQ PGSPGLGGLP GDRGEPGDPG VPGPVGMKGL SGDRGDAGMS GERGHPGSPG
FKGMAGMPGI PGQKGDRGSP GMDGFQGMLG LKGRQGFPGT KGEAGFFGVP GLKGLPGEPG
VKGNRGDRGP PGPPPLILPG MKDIKGEKGD EGPMGLKGYL GLKGIQGMPG VPGVSGFPGL
PGRPGFIKGV KGDIGVPGTP GLPGFPGVSG PPGITGFPGF TGSRGEKGTP GVAGVFGETG
PTGDFGDIGD TVDLPGSPGL KGERGITGIP GLKGFFGEKG AAGDIGFPGI TGMAGAQGSP
GLKGQTGFPG LTGLQGPQGE PGRIGIPGDK GDFGWPGVPG LPGFPGIRGI SGLHGLPGTK
GFPGSPGVDA HGDPGFPGPT GDRGDRGEAN TLPGPVGVPG QKGERGTPGE RGPAGSPGLQ
GFPGISPPSN ISGSPGDVGA PGIFGLQGYQ GPPGPPGPNA LPGIKGDEGS SGAAGFPGQK
GWVGDPGPQG QPGVLGLPGE KGPKGEQGFM GNTGPSGAVG DRGPKGPKGD QGFPGAPGSM
GSPGIPGIPQ KIAVQPGTLG PQGRRGLPGA LGEIGPQGPP GDPGFRGAPG KAGPQGRGGV
SAVPGFRGDQ GPMGHQGPVG QEGEPGRPGS PGLPGMPGRS VSIGYLLVKH SQTDQEPMCP
VGMNKLWSGY SLLYFEGQEK AHNQDLGLAG SCLARFSTMP FLYCNPGDVC YYASRNDKSY
WLSTTAPLPM MPVAEEEIKP YISRCSVCEA PAVAIAVHSQ DTSIPHCPAG WRSLWIGYSF
LMHTAAGDEG GGQSLVSPGS CLEDFRATPF IECNGGRGTC HYFANKYSFW LTTIPEQNFQ
STPSADTLKA GLIRTHISRC QVCMKNL
