CO4A3_HUMAN
ID CO4A3_HUMAN Reviewed; 1670 AA.
AC Q01955; Q53QQ1; Q53R14; Q53RW8; Q9BQT2; Q9NYC4; Q9UDJ9; Q9UDK9; Q9UDL0;
AC Q9UDL1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 3.
DT 03-AUG-2022, entry version 231.
DE RecName: Full=Collagen alpha-3(IV) chain;
DE AltName: Full=Goodpasture antigen;
DE Contains:
DE RecName: Full=Tumstatin;
DE Flags: Precursor;
GN Name=COL4A3;
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), TISSUE SPECIFICITY, AND VARIANTS
RP PRO-141; GLY-162 AND LEU-574.
RC TISSUE=Kidney;
RX PubMed=8083201; DOI=10.1016/s0021-9258(17)31612-5;
RA Mariyama M., Leinonen A., Mochizuki T., Tryggvason K., Reeders S.T.;
RT "Complete primary structure of the human alpha 3(IV) collagen chain.
RT Coexpression of the alpha 3(IV) and alpha 4(IV) collagen chains in human
RT tissues.";
RL J. Biol. Chem. 269:23013-23017(1994).
RN [2]
RP SEQUENCE REVISION.
RA Leinonen A.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANTS ATS2 GLU-297;
RP ARG-407; ARG-640; GLU-1207; GLN-1215; SER-1277; THR-1330; GLU-1334;
RP GLU-1347 AND CYS-1661, VARIANT ATS3 ARG-1167, AND VARIANTS ARG-43; PRO-141;
RP TYR-326; HIS-408; ARG-451; LEU-574; GLU-1269 AND PRO-1474.
RX PubMed=11134255; DOI=10.1681/asn.v12197;
RA Heidet L., Arrondel C., Forestier L., Cohen-Solal L., Mollet G.,
RA Gutierrez B., Stavrou C., Gubler M.-C., Antignac C.;
RT "Structure of the human type IV collagen gene COL4A3 and mutations in
RT autosomal Alport syndrome.";
RL J. Am. Soc. Nephrol. 12:97-106(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX PubMed=9537506; DOI=10.1016/s0014-5793(98)00128-8;
RA Momota R., Sugimoto M., Oohashi T., Kigasawa K., Yoshioka H., Ninomiya Y.;
RT "Two genes, COL4A3 and COL4A4 coding for the human alpha3(IV) and
RT alpha4(IV) collagen chains are arranged head-to-head on chromosome 2q36.";
RL FEBS Lett. 424:11-16(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1331-1670 (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=1737849; DOI=10.1172/jci115625;
RA Turner N., Mason P.J., Brown R., Fox M., Povey S., Rees A., Pusey C.D.;
RT "Molecular cloning of the human Goodpasture antigen demonstrates it to be
RT the alpha 3 chain of type IV collagen.";
RL J. Clin. Invest. 89:592-601(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1386-1670 (ISOFORM 1), AND PARTIAL PROTEIN
RP SEQUENCE.
RX PubMed=1400291; DOI=10.1016/s0021-9258(19)88621-0;
RA Quinones S., Bernal D., Garcia-Sogo M., Elena S.F., Saus J.;
RT "Exon/intron structure of the human alpha 3(IV) gene encompassing the
RT Goodpasture antigen (alpha 3(IV)NC1). Identification of a potentially
RT antigenic region at the triple helix/NC1 domain junction.";
RL J. Biol. Chem. 267:19780-19784(1992).
RN [8]
RP ERRATUM OF PUBMED:1400291.
RX PubMed=8006044; DOI=10.1016/s0021-9258(17)32561-9;
RA Quinones S., Bernal D., Garcia-Sogo M., Elena S.F., Saus J.;
RL J. Biol. Chem. 269:17358-17358(1994).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1386-1670 (ISOFORMS 1; 2; 3; 4 AND 5), AND
RP ALTERNATIVE SPLICING.
RC TISSUE=Kidney;
RX PubMed=7758473; DOI=10.1111/j.1432-1033.1995.tb20524.x;
RA Penades J.R., Bernal D., Revert F., Johansson C., Fresquet V.J.,
RA Cervera J., Wieslander J., Quinones S., Saus J.;
RT "Characterization and expression of multiple alternatively spliced
RT transcripts of the Goodpasture antigen gene region. Goodpasture antibodies
RT recognize recombinant proteins representing the autoantigen and one of its
RT alternative forms.";
RL Eur. J. Biochem. 229:754-760(1995).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1426-1670 (ISOFORM 1), AND FUNCTION.
RX PubMed=10766752; DOI=10.1074/jbc.m001956200;
RA Maeshima Y., Colorado P.C., Torre A., Holthaus K.A., Grunkemeyer J.A.,
RA Ericksen M.B., Hopfer H., Xiao Y., Stillman I.E., Kalluri R.;
RT "Distinct antitumor properties of a type IV collagen domain derived from
RT basement membrane.";
RL J. Biol. Chem. 275:21340-21348(2000).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1439-1670 (ISOFORMS 2 AND 3), AND ALTERNATIVE
RP SPLICING (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=8294492; DOI=10.1016/s0021-9258(17)42173-9;
RA Feng L., Xia Y., Wilson C.B.;
RT "Alternative splicing of the NC1 domain of the human alpha 3(IV) collagen
RT gene. Differential expression of mRNA transcripts that predict three
RT protein variants with distinct carboxyl regions.";
RL J. Biol. Chem. 269:2342-2348(1994).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1453-1670 (ISOFORM 1).
RX PubMed=1882840;
RA Morrison K.E., Mariyama M., Yang-Feng T.L., Reeders S.T.;
RT "Sequence and localization of a partial cDNA encoding the human alpha 3
RT chain of type IV collagen.";
RL Am. J. Hum. Genet. 49:545-554(1991).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1644-1670 (ISOFORM 1).
RC TISSUE=Kidney;
RA Ding J.;
RL Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), ALTERNATIVE
RP SPLICING, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=8505332; DOI=10.1016/s0021-9258(19)50312-x;
RA Bernal D., Quinones S., Saus J.;
RT "The human mRNA encoding the Goodpasture antigen is alternatively
RT spliced.";
RL J. Biol. Chem. 268:12090-12094(1993).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=7523402; DOI=10.1016/s0021-9258(18)47174-8;
RA Leinonen A., Mariyama M., Mochizuki T., Tryggvason K., Reeders S.T.;
RT "Complete primary structure of the human type IV collagen alpha 4(IV)
RT chain. Comparison with structure and expression of the other alpha (IV)
RT chains.";
RL J. Biol. Chem. 269:26172-26177(1994).
RN [16]
RP PHOSPHORYLATION.
RX PubMed=10212244; DOI=10.1074/jbc.274.18.12642;
RA Raya A., Revert F., Navarro S., Saus J.;
RT "Characterization of a novel type of serine/threonine kinase that
RT specifically phosphorylates the human goodpasture antigen.";
RL J. Biol. Chem. 274:12642-12649(1999).
RN [17]
RP FUNCTION.
RX PubMed=10837460; DOI=10.1074/jbc.c000186200;
RA Maeshima Y., Colorado P.C., Kalluri R.;
RT "Two RGD-independent alpha vbeta 3 integrin binding sites on tumstatin
RT regulate distinct anti-tumor properties.";
RL J. Biol. Chem. 275:23745-23750(2000).
RN [18]
RP INVOLVEMENT IN ATS3.
RX PubMed=11044206; DOI=10.1111/j.1523-1755.2000.00358.x;
RA van der Loop F.T.L., Heidet L., Timmer E.D.J., van den Bosch B.J.C.,
RA Leinonen A., Antignac C., Jefferson J.A., Maxwell A.P., Monnens L.A.H.,
RA Schroder C.H., Smeets H.J.M.;
RT "Autosomal dominant Alport syndrome caused by a COL4A3 splice site
RT mutation.";
RL Kidney Int. 58:1870-1875(2000).
RN [19]
RP HEXAMERIZATION.
RX PubMed=12193605; DOI=10.1074/jbc.m207769200;
RA Borza D.B., Bondar O., Todd P., Sundaramoorthy M., Sado Y., Ninomiya Y.,
RA Hudson B.G.;
RT "Quaternary organization of the goodpasture autoantigen, the alpha 3(IV)
RT collagen chain. Sequestration of two cryptic autoepitopes by intrapromoter
RT interactions with the alpha4 and alpha5 NC1 domains.";
RL J. Biol. Chem. 277:40075-40083(2002).
RN [20]
RP FUNCTION, AND INTERACTION WITH ITGB3.
RX PubMed=12682293; DOI=10.1073/pnas.0730882100;
RA Sudhakar A., Sugimoto H., Yang C., Lively J., Zeisberg M., Kalluri R.;
RT "Human tumstatin and human endostatin exhibit distinct antiangiogenic
RT activities mediated by alpha v beta 3 and alpha 5 beta 1 integrins.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:4766-4771(2003).
RN [21]
RP FUNCTION.
RX PubMed=15492988; DOI=10.1016/j.humpath.2004.06.008;
RA Caudroy S., Cucherousset J., Lorenzato M., Zahm J.-M.,
RA Martinella-Catusse C., Polette M., Birembaut P.;
RT "Implication of tumstatin in tumor progression of human bronchopulmonary
RT carcinomas.";
RL Hum. Pathol. 35:1218-1222(2004).
RN [22]
RP VARIANT PRO-1474.
RX PubMed=7987301; DOI=10.1093/hmg/3.8.1269;
RA Lemmink H.H., Mochizuki T., van den Heuvel L.P.W.J., Schroeder C.H.,
RA Barrientos A., Monnens L.A.H., van Oost B.A., Brunner H.G., Reeders S.T.,
RA Smeets H.J.M.;
RT "Mutations in the type IV collagen alpha 3 (COL4A3) gene in autosomal
RT recessive Alport syndrome.";
RL Hum. Mol. Genet. 3:1269-1273(1994).
RN [23]
RP VARIANTS BFH VAL-985 AND GLU-1015.
RX PubMed=11961012; DOI=10.1681/asn.v1351248;
RA Badenas C., Praga M., Tazon B., Heidet L., Arrondel C., Armengol A.,
RA Andres A., Morales E., Camacho J.A., Lens X., Davila S., Mila M.,
RA Antignac C., Darnell A., Torra R.;
RT "Mutations in the COL4A4 and COL4A3 genes cause familial benign
RT hematuria.";
RL J. Am. Soc. Nephrol. 13:1248-1254(2002).
RN [24]
RP VARIANTS ATS2 ASP-532; ARG-739; ARG-853 AND ARG-1216.
RX PubMed=15954103; DOI=10.1002/humu.9349;
RA Nagel M., Nagorka S., Gross O.;
RT "Novel COL4A5, COL4A4, and COL4A3 mutations in Alport syndrome.";
RL Hum. Mutat. 26:60-60(2005).
RN [25]
RP VARIANTS ATS2 VAL-631 AND CYS-1661.
RX PubMed=29946535; DOI=10.3389/fped.2018.00171;
RA Braunisch M.C., Buettner-Herold M., Guenthner R., Satanovskij R.,
RA Riedhammer K.M., Herr P.M., Klein H.G., Wahl D., Kuechle C., Renders L.,
RA Heemann U., Schmaderer C., Hoefele J.;
RT "Heterozygous COL4A3 variants in histologically diagnosed focal segmental
RT glomerulosclerosis.";
RL Front. Pediatr. 6:171-171(2018).
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 -!- 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 -!- 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:12193605).
CC Interacts with ITGB3 (PubMed:12682293). Associates with LAMB2 at the
CC neuromuscular junction and in GBM (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12193605, ECO:0000269|PubMed:12682293}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane. Note=Colocalizes with COL4A4 and COL4A5 in
CC GBM, tubular basement membrane (TBM) and synaptic basal lamina (BL).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Comment=The majority of isoforms differ in the C-terminal part of the
CC NC1 domain.;
CC Name=1; Synonyms=GP;
CC IsoId=Q01955-1; Sequence=Displayed;
CC Name=2; Synonyms=V, GP-V;
CC IsoId=Q01955-2; Sequence=VSP_001170;
CC Name=3; Synonyms=L5, GP-III, GP-III/V;
CC IsoId=Q01955-3; Sequence=VSP_001171;
CC Name=4; Synonyms=GP-III/IV/V;
CC IsoId=Q01955-4; Sequence=VSP_023500;
CC Name=5; Synonyms=GP-II/III/IV/V;
CC IsoId=Q01955-5; Sequence=VSP_023498, VSP_023499;
CC -!- TISSUE SPECIFICITY: Alpha 3 and alpha 4 type IV collagens are
CC colocalized and present in kidney, eye, basement membranes of lens
CC capsule, cochlea, lung, skeletal muscle, aorta, synaptic fibers, fetal
CC kidney and fetal lung. PubMed:8083201 reports similar levels of
CC expression of alpha 3 and alpha 4 type IV collagens in kidney, but
CC PubMed:7523402 reports that in kidney levels of alpha 3 type IV
CC collagen are significantly lower than those of alpha 4 type IV
CC collagen. According to PubMed:8083201, alpha 3 type IV collagen is not
CC detected in heart, brain, placenta, liver, pancreas, extrasynaptic
CC muscle fibers, endoneurial and perineurial nerves, fetal brain, fetal
CC heart and fetal liver. According to PubMed:7523402, alpha 3 type IV
CC collagen is strongly expressed in pancreas, neuroretina and calvaria
CC and not expressed in adrenal, ileum and skin. Isoform 1 and isoform 3
CC are strongly expressed in kidney, lung, suprarenal capsule, muscle and
CC spleen, in each of these tissues isoform 1 is more abundant than
CC isoform 3. Isoform 1 and isoform 3 are expressed at low levels in
CC artery, fat, pericardium and peripherical nerve, but not in placenta,
CC mesangium, skin, pleura and cultured umbilical endothelial cells.
CC {ECO:0000269|PubMed:7523402, ECO:0000269|PubMed:8083201,
CC ECO:0000269|PubMed:8505332}.
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: Isoform 2 contains an additional N-linked glycosylation site.
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: 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:0000269|PubMed:10212244}.
CC -!- DISEASE: Note=Autoantibodies against the NC1 domain of alpha 3(IV) are
CC found in Goodpasture syndrome, an autoimmune disease of lung and
CC kidney.
CC -!- DISEASE: Alport syndrome 2, autosomal recessive (ATS2) [MIM:203780]: A
CC syndrome characterized by progressive glomerulonephritis, glomerular
CC basement membrane defects, renal failure, sensorineural deafness and
CC specific eye abnormalities (lenticonous and macular flecks). The
CC disorder shows considerable heterogeneity in that families differ in
CC the age of end-stage renal disease and the occurrence of deafness.
CC {ECO:0000269|PubMed:11134255, ECO:0000269|PubMed:15954103,
CC ECO:0000269|PubMed:29946535}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Hematuria, benign familial (BFH) [MIM:141200]: An autosomal
CC dominant condition characterized by non-progressive isolated
CC microscopic hematuria that does not result in renal failure. It is
CC characterized pathologically by thinning of the glomerular basement
CC membrane. {ECO:0000269|PubMed:11961012}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Alport syndrome 3, autosomal dominant (ATS3) [MIM:104200]: A
CC syndrome characterized by progressive glomerulonephritis, glomerular
CC basement membrane defects, renal failure, sensorineural deafness and
CC specific eye abnormalities (lenticonous and macular flecks). The
CC disorder shows considerable heterogeneity in that families differ in
CC the age of end-stage renal disease and the occurrence of deafness.
CC {ECO:0000269|PubMed:11044206, ECO:0000269|PubMed:11134255}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: The epitopes recognized by the Goodpasture
CC autoantibodies are sequestered within the NC1 hexamer of the type IV
CC collagen network.
CC -!- SIMILARITY: Belongs to the type IV collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00736}.
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DR EMBL; X80031; CAA56335.1; -; mRNA.
DR EMBL; AJ288487; CAC36101.1; -; Genomic_DNA.
DR EMBL; AJ288488; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288489; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288490; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288491; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288492; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288493; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288494; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288495; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288496; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288497; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288498; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288499; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288500; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288501; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288502; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288503; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288504; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288505; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288506; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288507; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288508; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288509; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288510; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288511; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288512; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288513; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288514; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288515; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288516; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288517; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288518; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288519; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288520; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288521; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288522; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288523; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288524; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288525; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288526; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288527; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288528; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288529; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288530; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288531; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288532; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288533; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288534; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288535; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288536; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288537; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AJ288538; CAC36101.1; JOINED; Genomic_DNA.
DR EMBL; AC079235; AAY14671.1; -; Genomic_DNA.
DR EMBL; AC097662; AAY24251.1; -; Genomic_DNA.
DR EMBL; AC107069; AAX93111.1; -; Genomic_DNA.
DR EMBL; AB008496; BAA25064.1; -; Genomic_DNA.
DR EMBL; M81379; AAA51556.1; -; mRNA.
DR EMBL; M92993; AAA21610.1; -; mRNA.
DR EMBL; AF258351; AAF72632.1; -; mRNA.
DR EMBL; U02519; AAA18942.1; -; mRNA.
DR EMBL; U02520; AAA18943.1; -; mRNA.
DR EMBL; S55790; AAB19637.1; -; mRNA.
DR EMBL; L08650; AAA52044.1; -; Genomic_DNA.
DR CCDS; CCDS42829.1; -. [Q01955-1]
DR PIR; A49736; A49736.
DR PIR; A54763; CGHU3B.
DR PIR; B49736; B49736.
DR PIR; S69113; S69113.
DR RefSeq; NP_000082.2; NM_000091.4. [Q01955-1]
DR PDB; 5NB0; X-ray; 2.70 A; A/B/C/D/E/F/G/H=1441-1670.
DR PDB; 6WKU; X-ray; 1.76 A; A=1439-1666.
DR PDBsum; 5NB0; -.
DR PDBsum; 6WKU; -.
DR AlphaFoldDB; Q01955; -.
DR SMR; Q01955; -.
DR BioGRID; 107682; 6.
DR ComplexPortal; CPX-1725; Collagen type IV trimer variant 3.
DR CORUM; Q01955; -.
DR IntAct; Q01955; 2.
DR STRING; 9606.ENSP00000379823; -.
DR ChEMBL; CHEMBL2364188; -.
DR GlyGen; Q01955; 1 site.
DR iPTMnet; Q01955; -.
DR PhosphoSitePlus; Q01955; -.
DR BioMuta; COL4A3; -.
DR DMDM; 134035067; -.
DR EPD; Q01955; -.
DR jPOST; Q01955; -.
DR MassIVE; Q01955; -.
DR MaxQB; Q01955; -.
DR PaxDb; Q01955; -.
DR PeptideAtlas; Q01955; -.
DR PRIDE; Q01955; -.
DR ProteomicsDB; 58016; -. [Q01955-1]
DR ProteomicsDB; 58017; -. [Q01955-2]
DR ProteomicsDB; 58018; -. [Q01955-3]
DR ProteomicsDB; 58019; -. [Q01955-4]
DR ProteomicsDB; 58020; -. [Q01955-5]
DR ABCD; Q01955; 1 sequenced antibody.
DR Antibodypedia; 34379; 312 antibodies from 32 providers.
DR DNASU; 1285; -.
DR Ensembl; ENST00000396578.8; ENSP00000379823.3; ENSG00000169031.21. [Q01955-1]
DR GeneID; 1285; -.
DR KEGG; hsa:1285; -.
DR MANE-Select; ENST00000396578.8; ENSP00000379823.3; NM_000091.5; NP_000082.2.
DR UCSC; uc002vom.2; human. [Q01955-1]
DR CTD; 1285; -.
DR DisGeNET; 1285; -.
DR GeneCards; COL4A3; -.
DR GeneReviews; COL4A3; -.
DR HGNC; HGNC:2204; COL4A3.
DR HPA; ENSG00000169031; Tissue enhanced (retina).
DR MalaCards; COL4A3; -.
DR MIM; 104200; phenotype.
DR MIM; 120070; gene.
DR MIM; 141200; phenotype.
DR MIM; 203780; phenotype.
DR neXtProt; NX_Q01955; -.
DR OpenTargets; ENSG00000169031; -.
DR Orphanet; 88918; Autosomal dominant Alport syndrome.
DR Orphanet; 88919; Autosomal recessive Alport syndrome.
DR Orphanet; 656; Genetic steroid-resistant nephrotic syndrome.
DR Orphanet; 97562; NON RARE IN EUROPE: Benign familial hematuria.
DR PharmGKB; PA26719; -.
DR VEuPathDB; HostDB:ENSG00000169031; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000161675; -.
DR HOGENOM; CLU_002023_0_0_1; -.
DR InParanoid; Q01955; -.
DR OMA; CVCKDKG; -.
DR OrthoDB; 63831at2759; -.
DR PhylomeDB; Q01955; -.
DR TreeFam; TF344135; -.
DR PathwayCommons; Q01955; -.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1474244; Extracellular matrix organization.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-186797; Signaling by PDGF.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-2214320; Anchoring fibril formation.
DR Reactome; R-HSA-2243919; Crosslinking of collagen fibrils.
DR Reactome; R-HSA-3000157; Laminin interactions.
DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-419037; NCAM1 interactions.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; Q01955; -.
DR SIGNOR; Q01955; -.
DR BioGRID-ORCS; 1285; 9 hits in 1067 CRISPR screens.
DR ChiTaRS; COL4A3; human.
DR GeneWiki; Collagen_alpha-3(IV)_chain; -.
DR GenomeRNAi; 1285; -.
DR Pharos; Q01955; Tbio.
DR PRO; PR:Q01955; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q01955; protein.
DR Bgee; ENSG00000169031; Expressed in skeletal muscle tissue of biceps brachii and 149 other tissues.
DR ExpressionAtlas; Q01955; baseline and differential.
DR Genevisible; Q01955; HS.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0005587; C:collagen type IV trimer; IDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
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; IBA:GO_Central.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; NAS:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; NAS:ProtInc.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0008015; P:blood circulation; TAS:ProtInc.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:UniProtKB.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0072577; P:endothelial cell apoptotic process; IDA:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0032836; P:glomerular basement membrane development; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; IDA:UniProtKB.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; TAS:ProtInc.
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; 21.
DR SMART; SM00111; C4; 2.
DR SUPFAM; SSF56436; SSF56436; 2.
DR PROSITE; PS51403; NC1_IV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alport syndrome; Alternative splicing; Basement membrane;
KW Cell adhesion; Collagen; Deafness; Direct protein sequencing;
KW Disease variant; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Hydroxylation; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1670
FT /note="Collagen alpha-3(IV) chain"
FT /id="PRO_0000005844"
FT CHAIN 1426..1670
FT /note="Tumstatin"
FT /id="PRO_0000279684"
FT DOMAIN 1445..1669
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT REGION 29..42
FT /note="7S domain"
FT REGION 43..1438
FT /note="Triple-helical region"
FT REGION 49..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1427..1444
FT /note="Epitope recognized by Goodpasture antibodies"
FT REGION 1479..1557
FT /note="Required for the anti-angiogenic activity of
FT tumstatin"
FT REGION 1610..1628
FT /note="Required for the anti-tumor cell activity of
FT tumstatin"
FT MOTIF 791..793
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 996..998
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1154..1156
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1306..1308
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1345..1347
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1432..1434
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 178..204
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..383
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..442
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..619
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..674
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..709
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1092..1113
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1387
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 1426..1427
FT /note="Cleavage; by collagenase"
FT /evidence="ECO:0000250"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 1460..1551
FT /note="Or C-1460 with C-1548"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1493..1548
FT /note="Or C-1493 with C-1551"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1505..1511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1570..1665
FT /note="Or C-1570 with C-1662"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1604..1662
FT /note="Or C-1604 with C-1665"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 1616..1622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT CROSSLNK 1533
FT /note="S-Lysyl-methionine sulfilimine (Met-Lys) (interchain
FT with K-1651)"
FT /evidence="ECO:0000250"
FT CROSSLNK 1651
FT /note="S-Lysyl-methionine sulfilimine (Lys-Met) (interchain
FT with M-1533)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1418..1424
FT /note="GPAGSDG -> ESLFHQL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:7758473"
FT /id="VSP_023498"
FT VAR_SEQ 1425..1670
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:7758473"
FT /id="VSP_023499"
FT VAR_SEQ 1488..1670
FT /note="GTLGSCLQRFTTMPFLFCNVNDVCNFASRNDYSYWLSTPALMPMNMAPITGR
FT ALEPYISRCTVCEGPAIAIAVHSQTTDIPPCPHGWISLWKGFSFIMFTSAGSEGTGQAL
FT ASPGSCLEEFRASPFLECHGRGTCNYYSNSYSFWLASLNPERMFRKPIPSTVKAGELEK
FT IISRCQVCMKKRH -> DALFVKVLRSP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:7758473,
FT ECO:0000303|PubMed:8294492"
FT /id="VSP_001171"
FT VAR_SEQ 1488..1670
FT /note="GTLGSCLQRFTTMPFLFCNVNDVCNFASRNDYSYWLSTPALMPMNMAPITGR
FT ALEPYISRCTVCEGPAIAIAVHSQTTDIPPCPHGWISLWKGFSFIMFTSAGSEGTGQAL
FT ASPGSCLEEFRASPFLECHGRGTCNYYSNSYSFWLASLNPERMFRKPIPSTVKAGELEK
FT IISRCQVCMKKRH -> ESLFHQL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:7758473"
FT /id="VSP_023500"
FT VAR_SEQ 1586..1670
FT /note="FTSAGSEGTGQALASPGSCLEEFRASPFLECHGRGTCNYYSNSYSFWLASLN
FT PERMFRKPIPSTVKAGELEKIISRCQVCMKKRH -> KAYSINCESWGIRKNNKSLSGV
FT HEEKTLKLKKTAELVFFILKNKVMTEHAVI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7758473,
FT ECO:0000303|PubMed:8294492"
FT /id="VSP_001170"
FT VARIANT 43
FT /note="G -> R (in dbSNP:rs13424243)"
FT /evidence="ECO:0000269|PubMed:11134255"
FT /id="VAR_011202"
FT VARIANT 141
FT /note="L -> P (in dbSNP:rs10178458)"
FT /evidence="ECO:0000269|PubMed:11134255,
FT ECO:0000269|PubMed:8083201"
FT /id="VAR_030944"
FT VARIANT 162
FT /note="E -> G (in dbSNP:rs6436669)"
FT /evidence="ECO:0000269|PubMed:8083201"
FT /id="VAR_011203"
FT VARIANT 297
FT /note="G -> E (in ATS2; dbSNP:rs1422638161)"
FT /evidence="ECO:0000269|PubMed:11134255"
FT /id="VAR_011204"
FT VARIANT 326
FT /note="D -> Y (in dbSNP:rs55703767)"
FT /evidence="ECO:0000269|PubMed:11134255"
FT /id="VAR_011205"
FT VARIANT 407
FT /note="G -> R (in ATS2; dbSNP:rs1559878862)"
FT /evidence="ECO:0000269|PubMed:11134255"
FT /id="VAR_011206"
FT VARIANT 408
FT /note="R -> H (in dbSNP:rs34505188)"
FT /evidence="ECO:0000269|PubMed:11134255"
FT /id="VAR_011207"
FT VARIANT 451
FT /note="H -> R (in dbSNP:rs11677877)"
FT /evidence="ECO:0000269|PubMed:11134255"
FT /id="VAR_011208"
FT VARIANT 532
FT /note="G -> D (in ATS2; dbSNP:rs371405814)"
FT /evidence="ECO:0000269|PubMed:15954103"
FT /id="VAR_030945"
FT VARIANT 574
FT /note="P -> L (in dbSNP:rs28381984)"
FT /evidence="ECO:0000269|PubMed:11134255,
FT ECO:0000269|PubMed:8083201"
FT /id="VAR_011209"
FT VARIANT 631
FT /note="G -> V (in ATS2; unknown pathological significance;
FT dbSNP:rs1315862965)"
FT /evidence="ECO:0000269|PubMed:29946535"
FT /id="VAR_080826"
FT VARIANT 640
FT /note="G -> R (in ATS2; dbSNP:rs200672668)"
FT /evidence="ECO:0000269|PubMed:11134255"
FT /id="VAR_011210"
FT VARIANT 739
FT /note="G -> R (in ATS2; dbSNP:rs375040636)"
FT /evidence="ECO:0000269|PubMed:15954103"
FT /id="VAR_030946"
FT VARIANT 834
FT /note="K -> R (in dbSNP:rs56226424)"
FT /id="VAR_061118"
FT VARIANT 853
FT /note="G -> R (in ATS2; dbSNP:rs763726708)"
FT /evidence="ECO:0000269|PubMed:15954103"
FT /id="VAR_030947"
FT VARIANT 985
FT /note="G -> V (in BFH; dbSNP:rs121912827)"
FT /evidence="ECO:0000269|PubMed:11961012"
FT /id="VAR_030948"
FT VARIANT 1015
FT /note="G -> E (in BFH; dbSNP:rs121912826)"
FT /evidence="ECO:0000269|PubMed:11961012"
FT /id="VAR_030949"
FT VARIANT 1167
FT /note="G -> R (in ATS3; in isolated microhematuria at
FT heterozygosity; dbSNP:rs267606745)"
FT /evidence="ECO:0000269|PubMed:11134255"
FT /id="VAR_011211"
FT VARIANT 1207
FT /note="G -> E (in ATS2; in isolated microhematuria at
FT heterozygosity; dbSNP:rs1553764136)"
FT /evidence="ECO:0000269|PubMed:11134255"
FT /id="VAR_011212"
FT VARIANT 1215
FT /note="R -> Q (in ATS2; unknown pathological significance;
FT dbSNP:rs200443942)"
FT /evidence="ECO:0000269|PubMed:11134255"
FT /id="VAR_011213"
FT VARIANT 1216
FT /note="G -> R (in ATS2)"
FT /evidence="ECO:0000269|PubMed:15954103"
FT /id="VAR_030950"
FT VARIANT 1269
FT /note="D -> E (in dbSNP:rs57611801)"
FT /evidence="ECO:0000269|PubMed:11134255"
FT /id="VAR_011214"
FT VARIANT 1277
FT /note="G -> S (in ATS2; dbSNP:rs190598500)"
FT /evidence="ECO:0000269|PubMed:11134255"
FT /id="VAR_011215"
FT VARIANT 1330
FT /note="I -> T (in ATS2; unknown pathological significance;
FT dbSNP:rs767033956)"
FT /evidence="ECO:0000269|PubMed:11134255"
FT /id="VAR_011216"
FT VARIANT 1334
FT /note="G -> E (in ATS2; dbSNP:rs375290088)"
FT /evidence="ECO:0000269|PubMed:11134255"
FT /id="VAR_011217"
FT VARIANT 1347
FT /note="D -> E (in ATS2; unknown pathological significance;
FT dbSNP:rs73996414)"
FT /evidence="ECO:0000269|PubMed:11134255"
FT /id="VAR_011218"
FT VARIANT 1474
FT /note="L -> P (in dbSNP:rs200302125)"
FT /evidence="ECO:0000269|PubMed:11134255,
FT ECO:0000269|PubMed:7987301"
FT /id="VAR_001908"
FT VARIANT 1495
FT /note="Q -> R (in dbSNP:rs77964815)"
FT /id="VAR_001909"
FT VARIANT 1661
FT /note="R -> C (in ATS2; unknown pathological significance;
FT dbSNP:rs201697532)"
FT /evidence="ECO:0000269|PubMed:11134255,
FT ECO:0000269|PubMed:29946535"
FT /id="VAR_011219"
FT CONFLICT 911
FT /note="T -> R (in Ref. 3; CAC36101)"
FT /evidence="ECO:0000305"
FT CONFLICT 1539
FT /note="R -> I (in Ref. 11; AAA18942)"
FT /evidence="ECO:0000305"
FT CONFLICT 1594
FT /note="T -> A (in Ref. 12; AAB19637)"
FT /evidence="ECO:0000305"
FT CONFLICT 1663..1664
FT /note="QV -> HL (in Ref. 13; AAA52044)"
FT /evidence="ECO:0000305"
FT STRAND 1445..1451
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1453..1456
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1465..1478
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1481..1484
FT /evidence="ECO:0007829|PDB:6WKU"
FT HELIX 1490..1492
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1493..1496
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1502..1505
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1511..1514
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1519..1524
FT /evidence="ECO:0007829|PDB:6WKU"
FT HELIX 1538..1544
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1547..1555
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1557..1561
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1563..1566
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1575..1587
FT /evidence="ECO:0007829|PDB:6WKU"
FT HELIX 1589..1591
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1593..1595
FT /evidence="ECO:0007829|PDB:6WKU"
FT HELIX 1601..1603
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1604..1607
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1613..1617
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1629..1634
FT /evidence="ECO:0007829|PDB:6WKU"
FT HELIX 1638..1640
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1641..1643
FT /evidence="ECO:0007829|PDB:5NB0"
FT STRAND 1648..1651
FT /evidence="ECO:0007829|PDB:6WKU"
FT HELIX 1655..1658
FT /evidence="ECO:0007829|PDB:6WKU"
FT STRAND 1661..1666
FT /evidence="ECO:0007829|PDB:6WKU"
FT CONFLICT Q01955-2:1539
FT /note="R -> I (in Ref. 11; AAA18942)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1670 AA; 161813 MW; AA65D50903D82B99 CRC64;
MSARTAPRPQ VLLLPLLLVL LAAAPAASKG CVCKDKGQCF CDGAKGEKGE KGFPGPPGSP
GQKGFTGPEG LPGPQGPKGF PGLPGLTGSK GVRGISGLPG FSGSPGLPGT PGNTGPYGLV
GVPGCSGSKG EQGFPGLPGT LGYPGIPGAA GLKGQKGAPA KEEDIELDAK GDPGLPGAPG
PQGLPGPPGF PGPVGPPGPP GFFGFPGAMG PRGPKGHMGE RVIGHKGERG VKGLTGPPGP
PGTVIVTLTG PDNRTDLKGE KGDKGAMGEP GPPGPSGLPG ESYGSEKGAP GDPGLQGKPG
KDGVPGFPGS EGVKGNRGFP GLMGEDGIKG QKGDIGPPGF RGPTEYYDTY QEKGDEGTPG
PPGPRGARGP QGPSGPPGVP GSPGSSRPGL RGAPGWPGLK GSKGERGRPG KDAMGTPGSP
GCAGSPGLPG SPGPPGPPGD IVFRKGPPGD HGLPGYLGSP GIPGVDGPKG EPGLLCTQCP
YIPGPPGLPG LPGLHGVKGI PGRQGAAGLK GSPGSPGNTG LPGFPGFPGA QGDPGLKGEK
GETLQPEGQV GVPGDPGLRG QPGRKGLDGI PGTPGVKGLP GPKGELALSG EKGDQGPPGD
PGSPGSPGPA GPAGPPGYGP QGEPGLQGTQ GVPGAPGPPG EAGPRGELSV STPVPGPPGP
PGPPGHPGPQ GPPGIPGSLG KCGDPGLPGP DGEPGIPGIG FPGPPGPKGD QGFPGTKGSL
GCPGKMGEPG LPGKPGLPGA KGEPAVAMPG GPGTPGFPGE RGNSGEHGEI GLPGLPGLPG
TPGNEGLDGP RGDPGQPGPP GEQGPPGRCI EGPRGAQGLP GLNGLKGQQG RRGKTGPKGD
PGIPGLDRSG FPGETGSPGI PGHQGEMGPL GQRGYPGNPG ILGPPGEDGV IGMMGFPGAI
GPPGPPGNPG TPGQRGSPGI PGVKGQRGTP GAKGEQGDKG NPGPSEISHV IGDKGEPGLK
GFAGNPGEKG NRGVPGMPGL KGLKGLPGPA GPPGPRGDLG STGNPGEPGL RGIPGSMGNM
GMPGSKGKRG TLGFPGRAGR PGLPGIHGLQ GDKGEPGYSE GTRPGPPGPT GDPGLPGDMG
KKGEMGQPGP PGHLGPAGPE GAPGSPGSPG LPGKPGPHGD LGFKGIKGLL GPPGIRGPPG
LPGFPGSPGP MGIRGDQGRD GIPGPAGEKG ETGLLRAPPG PRGNPGAQGA KGDRGAPGFP
GLPGRKGAMG DAGPRGPTGI EGFPGPPGLP GAIIPGQTGN RGPPGSRGSP GAPGPPGPPG
SHVIGIKGDK GSMGHPGPKG PPGTAGDMGP PGRLGAPGTP GLPGPRGDPG FQGFPGVKGE
KGNPGFLGSI GPPGPIGPKG PPGVRGDPGT LKIISLPGSP GPPGTPGEPG MQGEPGPPGP
PGNLGPCGPR GKPGKDGKPG TPGPAGEKGN KGSKGEPGPA GSDGLPGLKG KRGDSGSPAT
WTTRGFVFTR HSQTTAIPSC PEGTVPLYSG FSFLFVQGNQ RAHGQDLGTL GSCLQRFTTM
PFLFCNVNDV CNFASRNDYS YWLSTPALMP MNMAPITGRA LEPYISRCTV CEGPAIAIAV
HSQTTDIPPC PHGWISLWKG FSFIMFTSAG SEGTGQALAS PGSCLEEFRA SPFLECHGRG
TCNYYSNSYS FWLASLNPER MFRKPIPSTV KAGELEKIIS RCQVCMKKRH
