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CO4A1_HUMAN
ID   CO4A1_HUMAN             Reviewed;        1669 AA.
AC   P02462; A7E2W4; B1AM70; F5H5K0; Q1P9S9; Q5VWF6; Q86X41; Q8NF88; Q9NYC5;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-MAY-2018, sequence version 4.
DT   03-AUG-2022, entry version 224.
DE   RecName: Full=Collagen alpha-1(IV) chain {ECO:0000305};
DE   Contains:
DE     RecName: Full=Arresten;
DE   Flags: Precursor;
GN   Name=COL4A1 {ECO:0000312|HGNC:HGNC:2202};
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 [GENOMIC DNA].
RX   PubMed=2701944; DOI=10.1016/s0021-9258(18)80034-5;
RA   Soininen R., Huotari M., Ganguly A., Prockop D.J., Tryggvason K.;
RT   "Structural organization of the gene for the alpha 1 chain of human type IV
RT   collagen.";
RL   J. Biol. Chem. 264:13565-13571(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT HIS-1334.
RC   TISSUE=Brain;
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 [MRNA] OF 1-943.
RC   TISSUE=Placenta;
RX   PubMed=3311751; DOI=10.1111/j.1432-1033.1987.tb13450.x;
RA   Brazel D., Oberbaeumer I., Dieringer H., Babel W., Glanville R.W.,
RA   Deutzmann R., Kuehn K.;
RT   "Completion of the amino acid sequence of the alpha 1 chain of human
RT   basement membrane collagen (type IV) reveals 21 non-triplet interruptions
RT   located within the collagenous domain.";
RL   Eur. J. Biochem. 168:529-536(1987).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX   PubMed=3182844; DOI=10.1016/s0021-9258(19)77818-1;
RA   Soininen R., Huotari M., Hostikka S.L., Prockop D.J., Tryggvason K.;
RT   "The structural genes for alpha 1 and alpha 2 chains of human type IV
RT   collagen are divergently encoded on opposite DNA strands and have an
RT   overlapping promoter region.";
RL   J. Biol. Chem. 263:17217-17220(1988).
RN   [6]
RP   PROTEIN SEQUENCE OF 28-243.
RX   PubMed=4043082; DOI=10.1111/j.1432-1033.1985.tb09186.x;
RA   Glanville R.W., Qian R.Q., Siebold B., Risteli J., Kuehn K.;
RT   "Amino acid sequence of the N-terminal aggregation and cross-linking region
RT   (7S domain) of the alpha 1 (IV) chain of human basement membrane
RT   collagen.";
RL   Eur. J. Biochem. 152:213-219(1985).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 46-1257.
RC   TISSUE=Placenta;
RX   PubMed=3691802; DOI=10.1016/0014-5793(87)81155-9;
RA   Soininen R., Haka-Risku T., Prockop D.J., Tryggvason K.;
RT   "Complete primary structure of the alpha 1-chain of human basement membrane
RT   (type IV) collagen.";
RL   FEBS Lett. 225:188-194(1987).
RN   [8]
RP   PROTEIN SEQUENCE OF 534-1447, PROLINE HYDROXYLATION, AND LYSINE
RP   HYDROXYLATION.
RX   PubMed=6434307; DOI=10.1111/j.1432-1033.1984.tb08404.x;
RA   Babel W., Glanville R.W.;
RT   "Structure of human-basement-membrane (type IV) collagen. Complete amino-
RT   acid sequence of a 914-residue-long pepsin fragment from the alpha 1(IV)
RT   chain.";
RL   Eur. J. Biochem. 143:545-556(1984).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1256-1669.
RX   PubMed=2581969; DOI=10.1016/s0021-9258(17)39662-x;
RA   Pihlajaniemi T., Tryggvason K., Myers J.C., Kurkinen M., Lebo R.,
RA   Cheung M.-C., Prockop D.J., Boyd C.D.;
RT   "cDNA clones coding for the pro-alpha1(IV) chain of human type IV
RT   procollagen reveal an unusual homology of amino acid sequences in two
RT   halves of the carboxyl-terminal domain.";
RL   J. Biol. Chem. 260:7681-7687(1985).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1259-1669.
RX   PubMed=2582422; DOI=10.1073/pnas.82.11.3649;
RA   Brinker J.M., Gudas L.J., Loidl H.R., Wang S.-Y., Rosenbloom J.,
RA   Kefalides N.A., Myers J.C.;
RT   "Restricted homology between human alpha 1 type IV and other procollagen
RT   chains.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:3649-3653(1985).
RN   [11]
RP   PROTEIN SEQUENCE OF 1441-1669, AND DISULFIDE BONDS.
RC   TISSUE=Placenta;
RX   PubMed=2844531; DOI=10.1111/j.1432-1033.1988.tb14321.x;
RA   Siebold B., Deutzmann R., Kuehn K.;
RT   "The arrangement of intra- and intermolecular disulfide bonds in the
RT   carboxyterminal, non-collagenous aggregation and cross-linking domain of
RT   basement-membrane type IV collagen.";
RL   Eur. J. Biochem. 176:617-624(1988).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669, FUNCTION OF ARRESTEN, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=10811134;
RA   Colorado P.C., Torre A., Kamphaus G., Maeshima Y., Hopfer H., Takahashi K.,
RA   Volk R., Zamborsky E.D., Herman S., Sarkar P.K., Ericksen M.B.,
RA   Dhanabal M., Simons M., Post M., Kufe D.W., Weichselbaum R.R.,
RA   Sukhatme V.P., Kalluri R.;
RT   "Anti-angiogenic cues from vascular basement membrane collagen.";
RL   Cancer Res. 60:2520-2526(2000).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
RA   Fu J., Bai X., Wang W., Ruan C.;
RT   "Arresten, a collagen-derived inhibitor of angiogenesis.";
RL   Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
RA   Peng X., Yin B., Yuan J., Qiang B.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [15]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
RA   Zheng Q.C., Song Z.F., Zheng Y.W., Li Y.Q., Shu X.;
RT   "Molecular cloning and sequencing of human arresten gene.";
RL   Zhonghua Shi Yan Wai Ke Za Zhi 19:46-47(2002).
RN   [16]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
RA   He A.B.;
RT   "Cloning and expression of arresten in Escherichia coli and Pachia
RT   pastoris.";
RL   Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN   [17]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669, FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Placenta;
RX   PubMed=16481288;
RA   Zheng J.P., Tang H.Y., Chen X.J., Yu B.F., Xie J., Wu T.C.;
RT   "Construction of recombinant plasmid and prokaryotic expression in E. coli
RT   and biological activity analysis of human placenta arresten gene.";
RL   Hepatobiliary Pancreat. Dis. Int. 5:74-79(2006).
RN   [18]
RP   RETRACTED PAPER.
RX   PubMed=16151532; DOI=10.1172/jci24813;
RA   Sudhakar A., Nyberg P., Keshamouni V.G., Mannam A.P., Li J., Sugimoto H.,
RA   Cosgrove D., Kalluri R.;
RT   "Human alpha1 type IV collagen NC1 domain exhibits distinct antiangiogenic
RT   activity mediated by alpha1beta1 integrin.";
RL   J. Clin. Invest. 115:2801-2810(2005).
RN   [19]
RP   RETRACTION NOTICE OF PUBMED:16151532.
RX   PubMed=31895054; DOI=10.1172/jci135305;
RA   Sudhakar A., Nyberg P., Keshamouni V.G., Mannam A.P., Li J., Sugimoto H.,
RA   Cosgrove D., Kalluri R.;
RL   J. Clin. Invest. 130:552-552(2020).
RN   [20]
RP   IDENTIFICATION OF RECEPTOR, AND FUNCTION OF ARRESTEN.
RX   PubMed=18775695; DOI=10.1016/j.yexcr.2008.08.011;
RA   Nyberg P., Xie L., Sugimoto H., Colorado P., Sund M., Holthaus K.,
RA   Sudhakar A., Salo T., Kalluri R.;
RT   "Characterization of the anti-angiogenic properties of arresten, an
RT   alpha1beta1 integrin-dependent collagen-derived tumor suppressor.";
RL   Exp. Cell Res. 314:3292-3305(2008).
RN   [21]
RP   INVOLVEMENT IN ICH, VARIANTS ICH LEU-352 AND GLY-538, VARIANTS VAL-144 AND
RP   VAL-1531, AND CHARACTERIZATION OF VARIANTS ICH LEU-352 AND GLY-538.
RX   PubMed=22522439; DOI=10.1002/ana.22682;
RA   Weng Y.C., Sonni A., Labelle-Dumais C., de Leau M., Kauffman W.B.,
RA   Jeanne M., Biffi A., Greenberg S.M., Rosand J., Gould D.B.;
RT   "COL4A1 mutations in patients with sporadic late-onset intracerebral
RT   hemorrhage.";
RL   Ann. Neurol. 71:470-477(2012).
RN   [22]
RP   INVOLVEMENT IN BSVD1, AND VARIANTS BSVD1 ARG-755; ARG-773; ASP-882 AND
RP   ARG-1266.
RX   PubMed=22574627; DOI=10.1111/j.1469-8749.2011.04198.x;
RA   Shah S., Ellard S., Kneen R., Lim M., Osborne N., Rankin J., Stoodley N.,
RA   van der Knaap M., Whitney A., Jardine P.;
RT   "Childhood presentation of COL4A1 mutations.";
RL   Dev. Med. Child. Neurol. 54:569-574(2012).
RN   [23]
RP   INVOLVEMENT IN BSVD1, AND VARIANT BSVD1 LYS-1627.
RX   PubMed=23394911; DOI=10.1016/j.ajo.2012.11.028;
RA   Rodahl E., Knappskog P.M., Majewski J., Johansson S., Telstad W.,
RA   Krakenes J., Boman H.;
RT   "Variants of anterior segment dysgenesis and cerebral involvement in a
RT   large family with a novel COL4A1 mutation.";
RL   Am. J. Ophthalmol. 155:946-953(2013).
RN   [24]
RP   INVOLVEMENT IN SCHZ, AND VARIANTS SCHZC ARG-655; ARG-870; SER-897; SER-948;
RP   GLU-1041; GLU-1082; ARG-1326; ASP-1332 AND LYS-1615.
RX   PubMed=23225343; DOI=10.1002/ana.23736;
RA   Yoneda Y., Haginoya K., Kato M., Osaka H., Yokochi K., Arai H., Kakita A.,
RA   Yamamoto T., Otsuki Y., Shimizu S., Wada T., Koyama N., Mino Y., Kondo N.,
RA   Takahashi S., Hirabayashi S., Takanashi J., Okumura A., Kumagai T.,
RA   Hirai S., Nabetani M., Saitoh S., Hattori A., Yamasaki M., Kumakura A.,
RA   Sugo Y., Nishiyama K., Miyatake S., Tsurusaki Y., Doi H., Miyake N.,
RA   Matsumoto N., Saitsu H.;
RT   "Phenotypic spectrum of COL4A1 mutations: porencephaly to schizencephaly.";
RL   Ann. Neurol. 73:48-57(2013).
RN   [25]
RP   INVOLVEMENT IN RATOR, AND VARIANT RATOR ARG-510.
RX   PubMed=25228067; DOI=10.1007/s00417-014-2800-6;
RA   Zenteno J.C., Crespi J., Buentello-Volante B., Buil J.A., Bassaganyas F.,
RA   Vela-Segarra J.I., Diaz-Cascajosa J., Marieges M.T.;
RT   "Next generation sequencing uncovers a missense mutation in COL4A1 as the
RT   cause of familial retinal arteriolar tortuosity.";
RL   Graefes Arch. Clin. Exp. Ophthalmol. 252:1789-1794(2014).
RN   [26]
RP   INVOLVEMENT IN BSVD1, AND VARIANTS BSVD1 ARG-708 AND ARG-773.
RX   PubMed=24628545; DOI=10.1111/cge.12379;
RA   Deml B., Reis L.M., Maheshwari M., Griffis C., Bick D., Semina E.V.;
RT   "Whole exome analysis identifies dominant COL4A1 mutations in patients with
RT   complex ocular phenotypes involving microphthalmia.";
RL   Clin. Genet. 86:475-481(2014).
RN   [27]
RP   INVOLVEMENT IN PADMAL.
RX   PubMed=27666438; DOI=10.1002/ana.24782;
RA   Verdura E., Herve D., Bergametti F., Jacquet C., Morvan T.,
RA   Prieto-Morin C., Mackowiak A., Manchon E., Hosseini H., Cordonnier C.,
RA   Girard-Buttaz I., Rosenstingl S., Hagel C., Kuhlenbauemer G., Leca-Radu E.,
RA   Goux D., Fleming L., Van Agtmael T., Chabriat H., Chapon F.,
RA   Tournier-Lasserve E.;
RT   "Disruption of a miR-29 binding site leading to COL4A1 upregulation causes
RT   pontine autosomal dominant microangiopathy with leukoencephalopathy.";
RL   Ann. Neurol. 80:741-753(2016).
RN   [28]
RP   INVOLVEMENT IN PADMAL.
RX   PubMed=28369186; DOI=10.1093/brain/awx062;
RA   Siitonen M., Boerjesson-Hanson A., Poeyhoenen M., Ora A., Pasanen P.,
RA   Bras J., Kern S., Kern J., Andersen O., Stanescu H., Kleta R., Baumann M.,
RA   Kalaria R., Kalimo H., Singleton A., Hardy J., Viitanen M., Myllykangas L.,
RA   Guerreiro R.;
RT   "Multi-infarct dementia of Swedish type is caused by a 3'UTR mutation of
RT   COL4A1.";
RL   Brain 140:E29-E29(2017).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1441-1669, AND ADDITIONAL
RP   INTERCHAIN LINKS.
RX   PubMed=12011424; DOI=10.1073/pnas.062183499;
RA   Than M.E., Henrich S., Huber R., Ries A., Mann K., Kuhn K., Timpl R.,
RA   Bourenkov G.P., Bartunik H.D., Bode W.;
RT   "The 1.9-A crystal structure of the noncollagenous (NC1) domain of human
RT   placenta collagen IV shows stabilization via a novel type of covalent Met-
RT   Lys cross-link.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:6607-6612(2002).
RN   [30]
RP   VARIANTS BSVD1 SER-749 AND ARG-1236.
RX   PubMed=15905400; DOI=10.1126/science.1109418;
RA   Gould D.B., Phalan F.C., Breedveld G.J., van Mil S.E., Smith R.S.,
RA   Schimenti J.C., Aguglia U., van der Knaap M.S., Heutink P., John S.W.M.;
RT   "Mutations in Col4a1 cause perinatal cerebral hemorrhage and
RT   porencephaly.";
RL   Science 308:1167-1171(2005).
RN   [31]
RP   VARIANTS BSVD1 ASP-1130 AND ARG-1423.
RX   PubMed=16107487; DOI=10.1136/jmg.2005.035584;
RA   Breedveld G., de Coo I.F., Lequin M.H., Arts W.F.M., Heutink P.,
RA   Gould D.B., John S.W.M., Oostra B., Mancini G.M.S.;
RT   "Novel mutations in three families confirm a major role of COL4A1 in
RT   hereditary porencephaly.";
RL   J. Med. Genet. 43:490-495(2006).
RN   [32]
RP   VARIANT BSVD1 GLU-562.
RX   PubMed=16598045; DOI=10.1056/nejmoa053727;
RA   Gould D.B., Phalan F.C., van Mil S.E., Sundberg J.P., Vahedi K., Massin P.,
RA   Bousser M.G., Heutink P., Miner J.H., Tournier-Lasserve E., John S.W.M.;
RT   "Role of COL4A1 in small-vessel disease and hemorrhagic stroke.";
RL   N. Engl. J. Med. 354:1489-1496(2006).
RN   [33]
RP   VARIANT BSVD1 ASP-720.
RX   PubMed=17696175; DOI=10.1002/ana.21191;
RA   Sibon I., Coupry I., Menegon P., Bouchet J.P., Gorry P., Burgelin I.,
RA   Calvas P., Orignac I., Dousset V., Lacombe D., Orgogozo J.M., Arveiler B.,
RA   Goizet C.;
RT   "COL4A1 mutation in Axenfeld-Rieger anomaly with leukoencephalopathy and
RT   stroke.";
RL   Ann. Neurol. 62:177-184(2007).
RN   [34]
RP   VARIANTS HANAC VAL-498; ARG-519 AND GLU-528.
RX   PubMed=18160688; DOI=10.1056/nejmoa071906;
RA   Plaisier E., Gribouval O., Alamowitch S., Mougenot B., Prost C.,
RA   Verpont M.C., Marro B., Desmettre T., Cohen S.Y., Roullet E., Dracon M.,
RA   Fardeau M., Van Agtmael T., Kerjaschki D., Antignac C., Ronco P.;
RT   "COL4A1 mutations and hereditary angiopathy, nephropathy, aneurysms, and
RT   muscle cramps.";
RL   N. Engl. J. Med. 357:2687-2695(2007).
RN   [35]
RP   VARIANT BSVD1 ARG-805.
RX   PubMed=17379824; DOI=10.1161/strokeaha.106.475194;
RA   Vahedi K., Kubis N., Boukobza M., Arnoult M., Massin P.,
RA   Tournier-Lasserve E., Bousser M.G.;
RT   "COL4A1 mutation in a patient with sporadic, recurrent intracerebral
RT   hemorrhage.";
RL   Stroke 38:1461-1464(2007).
RN   [36]
RP   VARIANT BSVD1 ARG-1580.
RX   PubMed=19194877; DOI=10.1002/ana.21525;
RA   de Vries L.S., Koopman C., Groenendaal F., Van Schooneveld M.,
RA   Verheijen F.W., Verbeek E., Witkamp T.D., van der Worp H.B., Mancini G.;
RT   "COL4A1 mutation in two preterm siblings with antenatal onset of
RT   parenchymal hemorrhage.";
RL   Ann. Neurol. 65:12-18(2009).
RN   [37]
RP   VARIANTS HANAC ARG-498; ARG-510 AND LEU-525.
RX   PubMed=20818663; DOI=10.1002/ajmg.a.33659;
RA   Plaisier E., Chen Z., Gekeler F., Benhassine S., Dahan K., Marro B.,
RA   Alamowitch S., Paques M., Ronco P.;
RT   "Novel COL4A1 mutations associated with HANAC syndrome: a role for the
RT   triple helical CB3[IV] domain.";
RL   Am. J. Med. Genet. A 152:2550-2555(2010).
RN   [38]
RP   VARIANTS BSVD1 ASP-720 AND ARG-755.
RX   PubMed=20385946; DOI=10.1001/archophthalmol.2010.42;
RA   Coupry I., Sibon I., Mortemousque B., Rouanet F., Mine M., Goizet C.;
RT   "Ophthalmological features associated with COL4A1 mutations.";
RL   Arch. Ophthalmol. 128:483-489(2010).
RN   [39]
RP   VARIANT BSVD1 ARG-755.
RX   PubMed=19477666; DOI=10.1016/j.ejpn.2009.04.010;
RA   Shah S., Kumar Y., McLean B., Churchill A., Stoodley N., Rankin J.,
RA   Rizzu P., van der Knaap M., Jardine P.;
RT   "A dominantly inherited mutation in collagen IV A1 (COL4A1) causing
RT   childhood onset stroke without porencephaly.";
RL   Eur. J. Paediatr. Neurol. 14:182-187(2010).
RN   [40]
RP   VARIANTS LEU-7 AND HIS-1334.
RX   PubMed=21527998;
RA   Karolak J.A., Kulinska K., Nowak D.M., Pitarque J.A., Molinari A.,
RA   Rydzanicz M., Bejjani B.A., Gajecka M.;
RT   "Sequence variants in COL4A1 and COL4A2 genes in Ecuadorian families with
RT   keratoconus.";
RL   Mol. Vis. 17:827-843(2011).
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:P02463}.
CC   -!- FUNCTION: Arresten, comprising the C-terminal NC1 domain, inhibits
CC       angiogenesis and tumor formation. The C-terminal half is found to
CC       possess the anti-angiogenic activity. Specifically inhibits endothelial
CC       cell proliferation, migration and tube formation.
CC       {ECO:0000269|PubMed:10811134, ECO:0000269|PubMed:18775695}.
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 (By
CC       similarity). {ECO:0000250|UniProtKB:P02463,
CC       ECO:0000250|UniProtKB:Q7SIB2}.
CC   -!- INTERACTION:
CC       P02462; P08572: COL4A2; NbExp=2; IntAct=EBI-2432478, EBI-2432506;
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000250|UniProtKB:P02463}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P02462-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P02462-2; Sequence=VSP_059564, VSP_059565;
CC   -!- TISSUE SPECIFICITY: Highly expressed in placenta.
CC       {ECO:0000269|PubMed:10811134, ECO:0000269|PubMed:16481288}.
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       NC1 domain mediates hexamerization of alpha chains of type IV collagen
CC       (By similarity). {ECO:0000250|UniProtKB:P02463, ECO:0000305}.
CC   -!- PTM: Lysines at the third position of the tripeptide repeating unit (G-
CC       X-Y) are hydroxylated. The modified lysines can be O-glycosylated.
CC       {ECO:0000269|PubMed:6434307}.
CC   -!- PTM: Contains 4-hydroxyproline (Probable). Prolines at the third
CC       position of the tripeptide repeating unit (G-X-Y) are hydroxylated in
CC       some or all of the chains (By similarity).
CC       {ECO:0000250|UniProtKB:P02463, ECO:0000305|PubMed:6434307}.
CC   -!- PTM: Contains 3-hydroxyproline. This modification occurs on the first
CC       proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-
CC       hydroxyproline. {ECO:0000250|UniProtKB:P02463,
CC       ECO:0000250|UniProtKB:Q7SIB2}.
CC   -!- PTM: Type IV collagens contain numerous cysteine residues which are
CC       involved in inter- and intramolecular disulfide bonding
CC       (PubMed:2844531). 12 of these, located in the NC1 domain, are conserved
CC       in all known type IV collagens. {ECO:0000269|PubMed:2844531,
CC       ECO:0000305}.
CC   -!- PTM: The trimeric structure of the NC1 domains is stabilized by
CC       covalent bonds (sulfilimine cross-links) between Lys and Met residues
CC       (PubMed:12011424). These cross-links are important for the mechanical
CC       stability of the basement membrane (By similarity). Sulfilimine cross-
CC       link is catalyzed by PXDN (By similarity).
CC       {ECO:0000250|UniProtKB:P02463, ECO:0000269|PubMed:12011424}.
CC   -!- PTM: Proteolytic processing produces the C-terminal NC1 peptide,
CC       arresten. {ECO:0000269|PubMed:10811134}.
CC   -!- DISEASE: Hereditary angiopathy with nephropathy aneurysms and muscle
CC       cramps (HANAC) [MIM:611773]: The clinical renal manifestations include
CC       hematuria and bilateral large cysts. Histologic analysis revealed
CC       complex basement membrane defects in kidney and skin. The systemic
CC       angiopathy appears to affect both small vessels and large arteries.
CC       {ECO:0000269|PubMed:18160688, ECO:0000269|PubMed:20818663}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Brain small vessel disease 1 with or without ocular anomalies
CC       (BSVD1) [MIM:175780]: An autosomal dominant cerebrovascular disorder
CC       with variable manifestations reflecting the location and severity of
CC       the vascular defect. BSVD1 features include cerebral hemorrage,
CC       unilateral fluid-filled cysts or cavities within the cerebral
CC       hemispheres, leukoencephalopathy, hemiplegia, seizures, intellectual
CC       disability, and facial paresis. Affected individuals may manifest
CC       variable visual defects and ocular anomalies.
CC       {ECO:0000269|PubMed:15905400, ECO:0000269|PubMed:16107487,
CC       ECO:0000269|PubMed:16598045, ECO:0000269|PubMed:17379824,
CC       ECO:0000269|PubMed:17696175, ECO:0000269|PubMed:19194877,
CC       ECO:0000269|PubMed:19477666, ECO:0000269|PubMed:20385946,
CC       ECO:0000269|PubMed:22574627, ECO:0000269|PubMed:23394911,
CC       ECO:0000269|PubMed:24628545}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Intracerebral hemorrhage (ICH) [MIM:614519]: A pathological
CC       condition characterized by bleeding into one or both cerebral
CC       hemispheres including the basal ganglia and the cerebral cortex. It is
CC       often associated with hypertension and craniocerebral trauma.
CC       Intracerebral bleeding is a common cause of stroke.
CC       {ECO:0000269|PubMed:22522439}. Note=Disease susceptibility is
CC       associated with variants affecting the gene represented in this entry.
CC   -!- DISEASE: Tortuosity of retinal arteries (RATOR) [MIM:180000]: A disease
CC       characterized by marked tortuosity of second- and third-order retinal
CC       arteries with normal first-order arteries and venous system. Most
CC       patients manifest variable degrees of symptomatic transient vision loss
CC       due to retinal hemorrhage following minor stress or trauma.
CC       {ECO:0000269|PubMed:25228067}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- DISEASE: Schizencephaly (SCHZC) [MIM:269160]: Extremely rare human
CC       congenital disorder characterized by a full-thickness cleft within the
CC       cerebral hemispheres. These clefts are lined with gray matter and most
CC       commonly involve the parasylvian regions. Large portions of the
CC       cerebral hemispheres may be absent and replaced by cerebro-spinal
CC       fluid. {ECO:0000269|PubMed:23225343}. Note=The disease is caused by
CC       variants affecting the gene represented in this entry.
CC   -!- DISEASE: Microangiopathy and leukoencephalopathy, pontine, autosomal
CC       dominant (PADMAL) [MIM:618564]: A form of cerebral small vessel disease
CC       characterized by the recurrence of ischemic strokes starting in the
CC       thirties or forties, and associated with progressive imbalance and
CC       cognitive impairment. MRI examination shows ischemic lacunas in the
CC       pons and cerebral hemispheres, and diffuse leukoencephalopathy
CC       affecting various brain regions. {ECO:0000269|PubMed:27666438,
CC       ECO:0000269|PubMed:28369186}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry. Causative mutations
CC       affect a binding site for miR-29 microRNA located within the 3'UTR of
CC       COL4A1 and lead to an up-regulation of this gene.
CC       {ECO:0000269|PubMed:27666438}.
CC   -!- SIMILARITY: Belongs to the type IV collagen family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00736}.
CC   -!- CAUTION: Was shown to inhibit expression of hypoxia-inducible factor
CC       1alpha and ERK1/2 and p38 MAPK activation, and to function as a ligand
CC       for alpha1/beta1 integrin. However, this study was later retracted.
CC       {ECO:0000305|PubMed:16151532, ECO:0000305|PubMed:31895054}.
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DR   EMBL; M26576; AAA53098.1; -; Genomic_DNA.
DR   EMBL; J04217; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26550; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26540; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26542; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26543; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26544; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26545; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26546; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26547; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26537; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26538; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26548; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26549; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26551; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26552; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26553; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26554; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26555; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26556; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26557; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26539; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26558; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26559; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26560; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26561; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26562; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26536; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26563; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26541; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26564; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26565; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26566; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26567; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26568; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26569; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26570; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26571; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26572; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26573; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26574; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; M26575; AAA53098.1; JOINED; Genomic_DNA.
DR   EMBL; AL161773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL390755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF455822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC047305; AAH47305.1; -; mRNA.
DR   EMBL; BC151220; AAI51221.1; -; mRNA.
DR   EMBL; X05561; CAA29075.1; -; mRNA.
DR   EMBL; Y00706; CAA68698.1; -; mRNA.
DR   EMBL; M10940; AAA52006.1; -; mRNA.
DR   EMBL; M11315; AAA52042.1; -; mRNA.
DR   EMBL; AF258349; AAF72630.1; -; mRNA.
DR   EMBL; AF363672; AAK53382.1; -; mRNA.
DR   EMBL; AF400431; AAK92480.1; -; mRNA.
DR   EMBL; AY285780; AAP43112.1; -; mRNA.
DR   EMBL; AF536207; AAM97359.1; -; mRNA.
DR   EMBL; DQ464183; ABE73157.1; -; mRNA.
DR   CCDS; CCDS76649.1; -. [P02462-2]
DR   CCDS; CCDS9511.1; -. [P02462-1]
DR   PIR; S16876; CGHU4B.
DR   RefSeq; NP_001290039.1; NM_001303110.1. [P02462-2]
DR   RefSeq; NP_001836.3; NM_001845.5. [P02462-1]
DR   PDB; 1LI1; X-ray; 1.90 A; A/B/D/E=1441-1669.
DR   PDB; 5NAX; X-ray; 2.82 A; A/B/D/F=1441-1669.
DR   PDB; 5NAY; X-ray; 1.80 A; A/B/C/D/E/F=1441-1669.
DR   PDB; 6MPX; X-ray; 1.90 A; A=1438-1666.
DR   PDBsum; 1LI1; -.
DR   PDBsum; 5NAX; -.
DR   PDBsum; 5NAY; -.
DR   PDBsum; 6MPX; -.
DR   AlphaFoldDB; P02462; -.
DR   SMR; P02462; -.
DR   BioGRID; 107679; 29.
DR   ComplexPortal; CPX-1723; Collagen type IV trimer variant 1.
DR   IntAct; P02462; 31.
DR   MINT; P02462; -.
DR   STRING; 9606.ENSP00000364979; -.
DR   ChEMBL; CHEMBL2364188; -.
DR   GlyGen; P02462; 3 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; P02462; -.
DR   PhosphoSitePlus; P02462; -.
DR   SwissPalm; P02462; -.
DR   BioMuta; COL4A1; -.
DR   DMDM; 125987809; -.
DR   EPD; P02462; -.
DR   jPOST; P02462; -.
DR   MassIVE; P02462; -.
DR   PaxDb; P02462; -.
DR   PeptideAtlas; P02462; -.
DR   PRIDE; P02462; -.
DR   ProteomicsDB; 26899; -.
DR   ProteomicsDB; 51524; -. [P02462-1]
DR   ProteomicsDB; 51525; -. [P02462-2]
DR   Antibodypedia; 3436; 827 antibodies from 39 providers.
DR   DNASU; 1282; -.
DR   Ensembl; ENST00000375820.10; ENSP00000364979.4; ENSG00000187498.16. [P02462-1]
DR   Ensembl; ENST00000543140.6; ENSP00000443348.1; ENSG00000187498.16. [P02462-2]
DR   GeneID; 1282; -.
DR   KEGG; hsa:1282; -.
DR   MANE-Select; ENST00000375820.10; ENSP00000364979.4; NM_001845.6; NP_001836.3.
DR   UCSC; uc001vqw.4; human. [P02462-1]
DR   CTD; 1282; -.
DR   DisGeNET; 1282; -.
DR   GeneCards; COL4A1; -.
DR   GeneReviews; COL4A1; -.
DR   HGNC; HGNC:2202; COL4A1.
DR   HPA; ENSG00000187498; Tissue enhanced (placenta).
DR   MalaCards; COL4A1; -.
DR   MIM; 120130; gene.
DR   MIM; 175780; phenotype.
DR   MIM; 180000; phenotype.
DR   MIM; 269160; phenotype.
DR   MIM; 611773; phenotype.
DR   MIM; 614519; phenotype.
DR   MIM; 618564; phenotype.
DR   neXtProt; NX_P02462; -.
DR   OpenTargets; ENSG00000187498; -.
DR   Orphanet; 36383; COL4A1-related familial vascular leukoencephalopathy.
DR   Orphanet; 99810; Familial porencephaly.
DR   Orphanet; 481986; Familial schizencephaly.
DR   Orphanet; 73229; HANAC syndrome.
DR   Orphanet; 477749; Pontine autosomal dominant microangiopathy with leukoencephalopathy.
DR   Orphanet; 75326; Retinal arterial tortuosity.
DR   Orphanet; 899; Walker-Warburg syndrome.
DR   PharmGKB; PA26717; -.
DR   VEuPathDB; HostDB:ENSG00000187498; -.
DR   eggNOG; KOG3544; Eukaryota.
DR   GeneTree; ENSGT00940000157678; -.
DR   HOGENOM; CLU_002023_1_0_1; -.
DR   InParanoid; P02462; -.
DR   OMA; ETEDMFT; -.
DR   OrthoDB; 63831at2759; -.
DR   PhylomeDB; P02462; -.
DR   TreeFam; TF316865; -.
DR   PathwayCommons; P02462; -.
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-3000480; Scavenging by Class A Receptors.
DR   Reactome; R-HSA-419037; NCAM1 interactions.
DR   Reactome; R-HSA-8948216; Collagen chain trimerization.
DR   SignaLink; P02462; -.
DR   SIGNOR; P02462; -.
DR   BioGRID-ORCS; 1282; 10 hits in 1067 CRISPR screens.
DR   ChiTaRS; COL4A1; human.
DR   EvolutionaryTrace; P02462; -.
DR   GeneWiki; Collagen,_type_IV,_alpha_1; -.
DR   GenomeRNAi; 1282; -.
DR   Pharos; P02462; Tbio.
DR   PRO; PR:P02462; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; P02462; protein.
DR   Bgee; ENSG00000187498; Expressed in visceral pleura and 203 other tissues.
DR   ExpressionAtlas; P02462; baseline and differential.
DR   Genevisible; P02462; HS.
DR   GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR   GO; GO:0005587; C:collagen type IV trimer; IMP:BHF-UCL.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
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:0005201; F:extracellular matrix structural constituent; IMP:BHF-UCL.
DR   GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IMP:BHF-UCL.
DR   GO; GO:0048407; F:platelet-derived growth factor binding; IDA:MGI.
DR   GO; GO:0071711; P:basement membrane organization; IMP:BHF-UCL.
DR   GO; GO:0048514; P:blood vessel morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0007420; P:brain development; IMP:BHF-UCL.
DR   GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR   GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR   GO; GO:0061333; P:renal tubule morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0061304; P:retinal blood vessel morphogenesis; IMP:BHF-UCL.
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   3D-structure; Alternative splicing; Angiogenesis; Basement membrane;
KW   Collagen; Direct protein sequencing; Disease variant; Disulfide bond;
KW   Extracellular matrix; Glycoprotein; Hydroxylation; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000269|PubMed:4043082"
FT   PROPEP          28..172
FT                   /note="N-terminal propeptide (7S domain)"
FT                   /id="PRO_0000005748"
FT   CHAIN           173..1669
FT                   /note="Collagen alpha-1(IV) chain"
FT                   /id="PRO_0000005749"
FT   CHAIN           1445..1669
FT                   /note="Arresten"
FT                   /id="PRO_0000390482"
FT   DOMAIN          1445..1669
FT                   /note="Collagen IV NC1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT   REGION          48..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..1440
FT                   /note="Triple-helical region"
FT   REGION          504..1382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1404..1431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..123
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..154
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..215
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..299
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..380
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        409..423
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        627..655
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..817
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1341..1366
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1417..1431
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         204
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB2"
FT   MOD_RES         207
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB2"
FT   MOD_RES         210
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB2"
FT   MOD_RES         587
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB2"
FT   MOD_RES         602
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB2"
FT   MOD_RES         603
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P02463"
FT   MOD_RES         605
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB2"
FT   MOD_RES         606
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P02463"
FT   MOD_RES         623
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P02463"
FT   MOD_RES         626
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P02463"
FT   MOD_RES         629
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P02463"
FT   MOD_RES         632
FT                   /note="4-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:P02463"
FT   MOD_RES         647
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB2"
FT   MOD_RES         1214
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB2"
FT   MOD_RES         1424
FT                   /note="3-hydroxyproline"
FT                   /evidence="ECO:0000250|UniProtKB:Q7SIB2"
FT   CARBOHYD        126
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        1460..1551
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736,
FT                   ECO:0000269|PubMed:2844531"
FT   DISULFID        1493..1548
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736,
FT                   ECO:0000269|PubMed:2844531"
FT   DISULFID        1505..1511
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736,
FT                   ECO:0000269|PubMed:2844531"
FT   DISULFID        1570..1665
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736,
FT                   ECO:0000269|PubMed:2844531"
FT   DISULFID        1604..1662
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736,
FT                   ECO:0000269|PubMed:2844531"
FT   DISULFID        1616..1622
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00736,
FT                   ECO:0000269|PubMed:2844531"
FT   CROSSLNK        1533
FT                   /note="S-Lysyl-methionine sulfilimine (Met-Lys) (interchain
FT                   with K-1651)"
FT                   /evidence="ECO:0000269|PubMed:12011424"
FT   CROSSLNK        1651
FT                   /note="S-Lysyl-methionine sulfilimine (Lys-Met) (interchain
FT                   with M-1533)"
FT                   /evidence="ECO:0000269|PubMed:12011424"
FT   VAR_SEQ         513..519
FT                   /note="GPQGTPG -> LLFQIHK (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_059564"
FT   VAR_SEQ         520..1669
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_059565"
FT   VARIANT         7
FT                   /note="V -> L (in dbSNP:rs9515185)"
FT                   /evidence="ECO:0000269|PubMed:21527998"
FT                   /id="VAR_030027"
FT   VARIANT         144
FT                   /note="A -> V"
FT                   /evidence="ECO:0000269|PubMed:22522439"
FT                   /id="VAR_073809"
FT   VARIANT         304
FT                   /note="P -> L (in dbSNP:rs34843786)"
FT                   /id="VAR_044158"
FT   VARIANT         352
FT                   /note="P -> L (in ICH; the mutant protein is retained
FT                   intracellularly and is not secreted normally;
FT                   dbSNP:rs200786329)"
FT                   /evidence="ECO:0000269|PubMed:22522439"
FT                   /id="VAR_073810"
FT   VARIANT         498
FT                   /note="G -> R (in HANAC; dbSNP:rs267606744)"
FT                   /evidence="ECO:0000269|PubMed:20818663"
FT                   /id="VAR_064493"
FT   VARIANT         498
FT                   /note="G -> V (in HANAC; dbSNP:rs113994104)"
FT                   /evidence="ECO:0000269|PubMed:18160688"
FT                   /id="VAR_044159"
FT   VARIANT         510
FT                   /note="G -> R (in HANAC and RATOR; dbSNP:rs267606743)"
FT                   /evidence="ECO:0000269|PubMed:20818663,
FT                   ECO:0000269|PubMed:25228067"
FT                   /id="VAR_064494"
FT   VARIANT         519
FT                   /note="G -> R (in HANAC; dbSNP:rs113994105)"
FT                   /evidence="ECO:0000269|PubMed:18160688"
FT                   /id="VAR_044160"
FT   VARIANT         525
FT                   /note="G -> L (in HANAC; requires 2 nucleotide
FT                   substitutions; dbSNP:rs281865426)"
FT                   /evidence="ECO:0000269|PubMed:20818663"
FT                   /id="VAR_064495"
FT   VARIANT         528
FT                   /note="G -> E (in HANAC; dbSNP:rs113994106)"
FT                   /evidence="ECO:0000269|PubMed:18160688"
FT                   /id="VAR_044161"
FT   VARIANT         538
FT                   /note="R -> G (in ICH; the mutant protein is retained
FT                   intracellularly and is not secreted normally;
FT                   dbSNP:rs397514624)"
FT                   /evidence="ECO:0000269|PubMed:22522439"
FT                   /id="VAR_073811"
FT   VARIANT         555
FT                   /note="P -> T (in dbSNP:rs536174)"
FT                   /id="VAR_030511"
FT   VARIANT         562
FT                   /note="G -> E (in BSVD1; dbSNP:rs121912857)"
FT                   /evidence="ECO:0000269|PubMed:16598045"
FT                   /id="VAR_030028"
FT   VARIANT         655
FT                   /note="G -> R (in SCHZC)"
FT                   /evidence="ECO:0000269|PubMed:23225343"
FT                   /id="VAR_073812"
FT   VARIANT         708
FT                   /note="G -> R (in BSVD1; dbSNP:rs672601349)"
FT                   /evidence="ECO:0000269|PubMed:24628545"
FT                   /id="VAR_073813"
FT   VARIANT         720
FT                   /note="G -> D (in BSVD1; diffuse small vessel disease of
FT                   the brain associated with Axenfeld-Rieger anomaly and
FT                   leukoencephalopathy; dbSNP:rs113994108)"
FT                   /evidence="ECO:0000269|PubMed:17696175,
FT                   ECO:0000269|PubMed:20385946"
FT                   /id="VAR_064496"
FT   VARIANT         749
FT                   /note="G -> S (in BSVD1; dbSNP:rs113994109)"
FT                   /evidence="ECO:0000269|PubMed:15905400"
FT                   /id="VAR_030029"
FT   VARIANT         755
FT                   /note="G -> R (in BSVD1; associated with ocular anomalies
FT                   of variable severity in some patients; dbSNP:rs672601346)"
FT                   /evidence="ECO:0000269|PubMed:19477666,
FT                   ECO:0000269|PubMed:20385946, ECO:0000269|PubMed:22574627"
FT                   /id="VAR_064497"
FT   VARIANT         773
FT                   /note="G -> R (in BSVD1; dbSNP:rs672601347)"
FT                   /evidence="ECO:0000269|PubMed:22574627,
FT                   ECO:0000269|PubMed:24628545"
FT                   /id="VAR_073814"
FT   VARIANT         805
FT                   /note="G -> R (in BSVD1; dbSNP:rs113994110)"
FT                   /evidence="ECO:0000269|PubMed:17379824"
FT                   /id="VAR_064498"
FT   VARIANT         870
FT                   /note="G -> R (in SCHZC)"
FT                   /evidence="ECO:0000269|PubMed:23225343"
FT                   /id="VAR_073815"
FT   VARIANT         882
FT                   /note="G -> D (in BSVD1)"
FT                   /evidence="ECO:0000269|PubMed:22574627"
FT                   /id="VAR_073816"
FT   VARIANT         897
FT                   /note="G -> S (in SCHZC)"
FT                   /evidence="ECO:0000269|PubMed:23225343"
FT                   /id="VAR_073817"
FT   VARIANT         948
FT                   /note="G -> S (in SCHZC; dbSNP:rs1555303073)"
FT                   /evidence="ECO:0000269|PubMed:23225343"
FT                   /id="VAR_073818"
FT   VARIANT         1041
FT                   /note="G -> E (in SCHZC)"
FT                   /evidence="ECO:0000269|PubMed:23225343"
FT                   /id="VAR_073819"
FT   VARIANT         1082
FT                   /note="G -> E (in SCHZC)"
FT                   /evidence="ECO:0000269|PubMed:23225343"
FT                   /id="VAR_073820"
FT   VARIANT         1130
FT                   /note="G -> D (in BSVD1; dbSNP:rs113994111)"
FT                   /evidence="ECO:0000269|PubMed:16107487"
FT                   /id="VAR_030030"
FT   VARIANT         1236
FT                   /note="G -> R (in BSVD1; dbSNP:rs113994112)"
FT                   /evidence="ECO:0000269|PubMed:15905400"
FT                   /id="VAR_030031"
FT   VARIANT         1266
FT                   /note="G -> R (in BSVD1)"
FT                   /evidence="ECO:0000269|PubMed:22574627"
FT                   /id="VAR_073821"
FT   VARIANT         1326
FT                   /note="G -> R (in SCHZC; dbSNP:rs587777379)"
FT                   /evidence="ECO:0000269|PubMed:23225343"
FT                   /id="VAR_073822"
FT   VARIANT         1332
FT                   /note="G -> D (in SCHZC)"
FT                   /evidence="ECO:0000269|PubMed:23225343"
FT                   /id="VAR_073823"
FT   VARIANT         1334
FT                   /note="Q -> H (in dbSNP:rs3742207)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:21527998"
FT                   /id="VAR_020013"
FT   VARIANT         1423
FT                   /note="G -> R (in BSVD1; dbSNP:rs113994113)"
FT                   /evidence="ECO:0000269|PubMed:16107487"
FT                   /id="VAR_030032"
FT   VARIANT         1531
FT                   /note="M -> V (in dbSNP:rs1343193102)"
FT                   /evidence="ECO:0000269|PubMed:22522439"
FT                   /id="VAR_073824"
FT   VARIANT         1580
FT                   /note="G -> R (in BSVD1; dbSNP:rs113994114)"
FT                   /evidence="ECO:0000269|PubMed:19194877"
FT                   /id="VAR_064499"
FT   VARIANT         1615
FT                   /note="E -> K (in SCHZC)"
FT                   /evidence="ECO:0000269|PubMed:23225343"
FT                   /id="VAR_073825"
FT   VARIANT         1627
FT                   /note="N -> K (in BSVD1; dbSNP:rs672601348)"
FT                   /evidence="ECO:0000269|PubMed:23394911"
FT                   /id="VAR_073826"
FT   CONFLICT        237..238
FT                   /note="SG -> KE (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        241
FT                   /note="G -> K (in Ref. 6; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        319
FT                   /note="Q -> A (in Ref. 4; CAA29075)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        719
FT                   /note="N -> D (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        837
FT                   /note="D -> Y (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        842
FT                   /note="K -> P (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        896
FT                   /note="V -> W (in Ref. 7; CAA68698)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        904
FT                   /note="E -> Q (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        914
FT                   /note="S -> K (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        998
FT                   /note="S -> K (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1010
FT                   /note="K -> P (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1012
FT                   /note="S -> K (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1358
FT                   /note="E -> Q (in Ref. 8; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1490
FT                   /note="A -> T (in Ref. 17; ABE73157)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1507
FT                   /note="I -> T (in Ref. 17; ABE73157)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1519
FT                   /note="Y -> C (in Ref. 17; ABE73157)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1570
FT                   /note="C -> Y (in Ref. 16; AAM97359)"
FT                   /evidence="ECO:0000305"
FT   STRAND          1446..1451
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1453..1456
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1465..1478
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1481..1484
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   HELIX           1490..1492
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1493..1496
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1502..1505
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1511..1514
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1519..1524
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   HELIX           1538..1544
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1547..1555
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1557..1561
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1563..1566
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1574..1587
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   HELIX           1589..1591
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1593..1595
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   HELIX           1601..1603
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1604..1607
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1613..1617
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1620..1623
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1629..1634
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   HELIX           1638..1640
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1641..1643
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1648..1650
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   HELIX           1655..1658
FT                   /evidence="ECO:0007829|PDB:5NAY"
FT   STRAND          1661..1667
FT                   /evidence="ECO:0007829|PDB:5NAY"
SQ   SEQUENCE   1669 AA;  160611 MW;  3BEBA6DFFB9B8A84 CRC64;
     MGPRLSVWLL LLPAALLLHE EHSRAAAKGG CAGSGCGKCD CHGVKGQKGE RGLPGLQGVI
     GFPGMQGPEG PQGPPGQKGD TGEPGLPGTK GTRGPPGASG YPGNPGLPGI PGQDGPPGPP
     GIPGCNGTKG ERGPLGPPGL PGFAGNPGPP GLPGMKGDPG EILGHVPGML LKGERGFPGI
     PGTPGPPGLP GLQGPVGPPG FTGPPGPPGP PGPPGEKGQM GLSFQGPKGD KGDQGVSGPP
     GVPGQAQVQE KGDFATKGEK GQKGEPGFQG MPGVGEKGEP GKPGPRGKPG KDGDKGEKGS
     PGFPGEPGYP GLIGRQGPQG EKGEAGPPGP PGIVIGTGPL GEKGERGYPG TPGPRGEPGP
     KGFPGLPGQP GPPGLPVPGQ AGAPGFPGER GEKGDRGFPG TSLPGPSGRD GLPGPPGSPG
     PPGQPGYTNG IVECQPGPPG DQGPPGIPGQ PGFIGEIGEK GQKGESCLIC DIDGYRGPPG
     PQGPPGEIGF PGQPGAKGDR GLPGRDGVAG VPGPQGTPGL IGQPGAKGEP GEFYFDLRLK
     GDKGDPGFPG QPGMPGRAGS PGRDGHPGLP GPKGSPGSVG LKGERGPPGG VGFPGSRGDT
     GPPGPPGYGP AGPIGDKGQA GFPGGPGSPG LPGPKGEPGK IVPLPGPPGA EGLPGSPGFP
     GPQGDRGFPG TPGRPGLPGE KGAVGQPGIG FPGPPGPKGV DGLPGDMGPP GTPGRPGFNG
     LPGNPGVQGQ KGEPGVGLPG LKGLPGLPGI PGTPGEKGSI GVPGVPGEHG AIGPPGLQGI
     RGEPGPPGLP GSVGSPGVPG IGPPGARGPP GGQGPPGLSG PPGIKGEKGF PGFPGLDMPG
     PKGDKGAQGL PGITGQSGLP GLPGQQGAPG IPGFPGSKGE MGVMGTPGQP GSPGPVGAPG
     LPGEKGDHGF PGSSGPRGDP GLKGDKGDVG LPGKPGSMDK VDMGSMKGQK GDQGEKGQIG
     PIGEKGSRGD PGTPGVPGKD GQAGQPGQPG PKGDPGISGT PGAPGLPGPK GSVGGMGLPG
     TPGEKGVPGI PGPQGSPGLP GDKGAKGEKG QAGPPGIGIP GLRGEKGDQG IAGFPGSPGE
     KGEKGSIGIP GMPGSPGLKG SPGSVGYPGS PGLPGEKGDK GLPGLDGIPG VKGEAGLPGT
     PGPTGPAGQK GEPGSDGIPG SAGEKGEPGL PGRGFPGFPG AKGDKGSKGE VGFPGLAGSP
     GIPGSKGEQG FMGPPGPQGQ PGLPGSPGHA TEGPKGDRGP QGQPGLPGLP GPMGPPGLPG
     IDGVKGDKGN PGWPGAPGVP GPKGDPGFQG MPGIGGSPGI TGSKGDMGPP GVPGFQGPKG
     LPGLQGIKGD QGDQGVPGAK GLPGPPGPPG PYDIIKGEPG LPGPEGPPGL KGLQGLPGPK
     GQQGVTGLVG IPGPPGIPGF DGAPGQKGEM GPAGPTGPRG FPGPPGPDGL PGSMGPPGTP
     SVDHGFLVTR HSQTIDDPQC PSGTKILYHG YSLLYVQGNE RAHGQDLGTA GSCLRKFSTM
     PFLFCNINNV CNFASRNDYS YWLSTPEPMP MSMAPITGEN IRPFISRCAV CEAPAMVMAV
     HSQTIQIPPC PSGWSSLWIG YSFVMHTSAG AEGSGQALAS PGSCLEEFRS APFIECHGRG
     TCNYYANAYS FWLATIERSE MFKKPTPSTL KAGELRTHVS RCQVCMRRT
 
 
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