CO4A1_MOUSE
ID CO4A1_MOUSE Reviewed; 1669 AA.
AC P02463; Q3UHJ4; Q3UJE7; Q3UQV2; Q53X35; Q6GQS7; Q6PHB5; Q99LQ8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 4.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Collagen alpha-1(IV) chain {ECO:0000305};
DE Contains:
DE RecName: Full=Arresten;
DE Flags: Precursor;
GN Name=Col4a1 {ECO:0000312|MGI:MGI:88454};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2703490; DOI=10.1016/s0021-9258(18)83349-x;
RA Muthukumaran G., Blumberg B., Kurkinen M.;
RT "The complete primary structure for the alpha 1-chain of mouse collagen IV.
RT Differential evolution of collagen IV domains.";
RL J. Biol. Chem. 264:6310-6317(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, Eye, Heart, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Colon, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1154.
RX PubMed=3338568; DOI=10.1016/0014-5793(88)81402-9;
RA Wood L., Theriault N., Vogeli G.;
RT "cDNA clones completing the nucleotide and derived amino acid sequence of
RT the alpha 1 chain of basement membrane (type IV) collagen from mouse.";
RL FEBS Lett. 227:5-8(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-129.
RX PubMed=3379041; DOI=10.1016/s0021-9258(18)68362-0;
RA Killen P.D., Burbelo P.D., Sakurai Y., Yamada Y.;
RT "Structure of the amino-terminal portion of the murine alpha 1(IV) collagen
RT chain and the corresponding region of the gene.";
RL J. Biol. Chem. 263:8706-8709(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX PubMed=2842328; DOI=10.1016/s0021-9258(18)37756-1;
RA Killen P.D., Burbelo P.D., Martin G.R., Yamada Y.;
RT "Characterization of the promoter for the alpha 1 (IV) collagen gene. DNA
RT sequences within the first intron enhance transcription.";
RL J. Biol. Chem. 263:12310-12314(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX PubMed=3198626; DOI=10.1016/s0021-9258(19)77629-7;
RA Kaytes P., Wood L., Theriault N., Kurkinen M., Vogeli G.;
RT "Head-to-head arrangement of murine type IV collagen genes.";
RL J. Biol. Chem. 263:19274-19277(1988).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RX PubMed=3200851; DOI=10.1073/pnas.85.24.9679;
RA Burbelo P.D., Martin G.R., Yamada Y.;
RT "Alpha 1(IV) and alpha 2(IV) collagen genes are regulated by a
RT bidirectional promoter and a shared enhancer.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:9679-9682(1988).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1110-1135.
RX PubMed=3009468; DOI=10.1016/s0021-9258(19)62667-0;
RA Sakurai Y., Sullivan M., Yamada Y.;
RT "Alpha 1 type IV collagen gene evolved differently from fibrillar collagen
RT genes.";
RL J. Biol. Chem. 261:6654-6657(1986).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1149-1424.
RX PubMed=3755692; DOI=10.1016/0378-1119(86)90220-9;
RA Nath P., Laurent M., Horn E., Sobel M.E., Zon G., Vogeli G.;
RT "Isolation of an alpha 1 type-IV collagen cDNA clone using a synthetic
RT oligodeoxynucleotide.";
RL Gene 43:301-304(1986).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1276-1669.
RX PubMed=2578961; DOI=10.1111/j.1432-1033.1985.tb08739.x;
RA Oberbaeumer I., Laurent M., Schwarz U., Sakurai Y., Yamada Y., Vogeli G.,
RA Voss T., Siebold B., Glanville R.W., Kuhn K.;
RT "Amino acid sequence of the non-collagenous globular domain (NC1) of the
RT alpha 1(IV) chain of basement membrane collagen as derived from
RT complementary DNA.";
RL Eur. J. Biochem. 147:217-224(1985).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1441-1669.
RX PubMed=3597383; DOI=10.1016/s0021-9258(18)47441-8;
RA Kurkinen M., Condon M.R., Blumberg B., Barlow D., Quinones S., Saus J.,
RA Pihlajaniemi T.;
RT "Extensive homology between the carboxyl-terminal peptides of mouse alpha
RT 1(IV) and alpha 2(IV) collagen.";
RL J. Biol. Chem. 262:8496-8499(1987).
RN [13]
RP DISRUPTION PHENOTYPE.
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 [14]
RP INTERACTION WITH EFEMP2.
RX PubMed=17324935; DOI=10.1074/jbc.m611029200;
RA Kobayashi N., Kostka G., Garbe J.H., Keene D.R., Baechinger H.P.,
RA Hanisch F.G., Markova D., Tsuda T., Timpl R., Chu M.L., Sasaki T.;
RT "A comparative analysis of the fibulin protein family. Biochemical
RT characterization, binding interactions, and tissue localization.";
RL J. Biol. Chem. 282:11805-11816(2007).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [16]
RP INTERCHAIN SULFILIMINE BONDS, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP DOMAIN.
RX PubMed=22842973; DOI=10.1038/nchembio.1038;
RA Bhave G., Cummings C.F., Vanacore R.M., Kumagai-Cresse C.,
RA Ero-Tolliver I.A., Rafi M., Kang J.S., Pedchenko V., Fessler L.I.,
RA Fessler J.H., Hudson B.G.;
RT "Peroxidasin forms sulfilimine chemical bonds using hypohalous acids in
RT tissue genesis.";
RL Nat. Chem. Biol. 8:784-790(2012).
RN [17]
RP SUBCELLULAR LOCATION, AND PROLINE HYDROXYLATION.
RX PubMed=24368846; DOI=10.1073/pnas.1307597111;
RA Pokidysheva E., Boudko S., Vranka J., Zientek K., Maddox K., Moser M.,
RA Faessler R., Ware J., Baechinger H.P.;
RT "Biological role of prolyl 3-hydroxylation in type IV collagen.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:161-166(2014).
RN [18]
RP HYDROXYLATION AT PRO-602; PRO-603; PRO-605; PRO-606; PRO-623; PRO-626;
RP PRO-629 AND PRO-632, GLYCOSYLATION OF HYDROXYLATED LYSINE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=25645914; DOI=10.1074/jbc.m114.634915;
RA Hudson D.M., Joeng K.S., Werther R., Rajagopal A., Weis M., Lee B.H.,
RA Eyre D.R.;
RT "Post-translationally abnormal collagens of prolyl 3-hydroxylase-2 null
RT mice offer a pathobiological mechanism for the high myopia linked to human
RT LEPREL1 mutations.";
RL J. Biol. Chem. 290:8613-8622(2015).
RN [19]
RP SULFILIMINE BONDS, AND FUNCTION.
RX PubMed=28424209; DOI=10.1152/ajprenal.00096.2017;
RA Bhave G., Colon S., Ferrell N.;
RT "The Sulfilimine Cross-Link of Collagen IV Contributes to Kidney Tubular
RT Basement Membrane Stiffness.";
RL Am. J. Physiol. 313:F596-F602(2017).
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:0000305|PubMed:28424209}.
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:0000250|UniProtKB:P02462}.
CC -!- SUBUNIT: There are six type IV collagen isoforms, alpha 1(IV)-alpha
CC 6(IV), each of which can form a triple helix structure with 2 other
CC chains to generate type IV collagen network. Interacts with EFEMP2
CC (PubMed:17324935). {ECO:0000250|UniProtKB:Q7SIB2,
CC ECO:0000269|PubMed:17324935}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:24368846}.
CC -!- TISSUE SPECIFICITY: Detected in the basement membrane of the cornea (at
CC protein level). {ECO:0000269|PubMed:24368846}.
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 (PubMed:22842973). {ECO:0000269|PubMed:22842973, 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:25645914}.
CC -!- PTM: Contains 4-hydroxyproline. Prolines at the third position of the
CC tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of
CC the chains. {ECO:0000269|PubMed:25645914}.
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:0000269|PubMed:24368846,
CC ECO:0000269|PubMed:25645914}.
CC -!- PTM: Type IV collagens contain numerous cysteine residues which are
CC involved in inter- and intramolecular disulfide bonding. 12 of these,
CC located in the NC1 domain, are conserved in all known type IV
CC collagens. {ECO:0000250|UniProtKB:P02462}.
CC -!- PTM: The trimeric structure of the NC1 domains is stabilized by
CC covalent bonds (sulfilimine cross-links) between Lys and Met residues.
CC These cross-links are important for the mechanical stability of the
CC basement membrane (PubMed:28424209, PubMed:22842973). Sulfilimine
CC cross-link is catalyzed by PXDN (PubMed:22842973).
CC {ECO:0000269|PubMed:22842973, ECO:0000269|PubMed:28424209}.
CC -!- PTM: Proteolytic processing produces the C-terminal NC1 peptide,
CC arresten. {ECO:0000250|UniProtKB:P02462}.
CC -!- DISRUPTION PHENOTYPE: Mice develop perinatal cerebral hemorrhage and
CC porencephaly. The mutant protein inhibits the secretion of mutant and
CC normal proteins into the basement membrane of embryonic origin. The
CC mutation is semidominant. {ECO:0000269|PubMed:15905400}.
CC -!- SIMILARITY: Belongs to the type IV collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00736}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH72650.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH72650.1; Type=Miscellaneous discrepancy; Note=Insertion sequence.; Evidence={ECO:0000305};
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DR EMBL; J04694; AAA50292.1; -; mRNA.
DR EMBL; AK142097; BAE24936.1; -; mRNA.
DR EMBL; AK146487; BAE27208.1; -; mRNA.
DR EMBL; AK147284; BAE27820.1; -; mRNA.
DR EMBL; AK147355; BAE27863.1; -; mRNA.
DR EMBL; AK147661; BAE28055.1; -; mRNA.
DR EMBL; BC002269; AAH02269.1; -; mRNA.
DR EMBL; BC056620; AAH56620.1; -; mRNA.
DR EMBL; BC072650; AAH72650.1; ALT_SEQ; mRNA.
DR EMBL; X06777; CAA29946.1; -; mRNA.
DR EMBL; J03758; AAA37439.1; -; mRNA.
DR EMBL; J03944; AAA37442.1; -; Genomic_DNA.
DR EMBL; J04448; AAA37437.1; -; Genomic_DNA.
DR EMBL; M23333; AAA51625.1; -; Genomic_DNA.
DR EMBL; M12879; AAA37343.1; -; Genomic_DNA.
DR EMBL; M13024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M13025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M13026; AAA37344.1; -; Genomic_DNA.
DR EMBL; M13027; AAA37345.1; -; Genomic_DNA.
DR EMBL; M13043; AAA37346.1; -; Genomic_DNA.
DR EMBL; M14042; AAA37342.1; -; mRNA.
DR EMBL; X02201; CAA26132.1; -; mRNA.
DR EMBL; M15832; AAA37340.1; -; mRNA.
DR CCDS; CCDS40219.1; -.
DR PIR; A33525; CGMS4B.
DR RefSeq; NP_034061.2; NM_009931.2.
DR AlphaFoldDB; P02463; -.
DR BioGRID; 198816; 3.
DR ComplexPortal; CPX-2959; Collagen type IV trimer variant 1.
DR CORUM; P02463; -.
DR STRING; 10090.ENSMUSP00000033898; -.
DR GlyGen; P02463; 1 site.
DR iPTMnet; P02463; -.
DR PhosphoSitePlus; P02463; -.
DR EPD; P02463; -.
DR MaxQB; P02463; -.
DR PaxDb; P02463; -.
DR PeptideAtlas; P02463; -.
DR PRIDE; P02463; -.
DR ProteomicsDB; 279129; -.
DR Antibodypedia; 3436; 827 antibodies from 39 providers.
DR DNASU; 12826; -.
DR Ensembl; ENSMUST00000033898; ENSMUSP00000033898; ENSMUSG00000031502.
DR GeneID; 12826; -.
DR KEGG; mmu:12826; -.
DR UCSC; uc009kvb.2; mouse.
DR CTD; 1282; -.
DR MGI; MGI:88454; Col4a1.
DR VEuPathDB; HostDB:ENSMUSG00000031502; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000157678; -.
DR HOGENOM; CLU_002023_0_0_1; -.
DR InParanoid; P02463; -.
DR OMA; NINNICH; -.
DR OrthoDB; 1372287at2759; -.
DR PhylomeDB; P02463; -.
DR TreeFam; TF316865; -.
DR Reactome; R-MMU-1442490; Collagen degradation.
DR Reactome; R-MMU-1474244; Extracellular matrix organization.
DR Reactome; R-MMU-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-MMU-186797; Signaling by PDGF.
DR Reactome; R-MMU-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-2214320; Anchoring fibril formation.
DR Reactome; R-MMU-2243919; Crosslinking of collagen fibrils.
DR Reactome; R-MMU-3000157; Laminin interactions.
DR Reactome; R-MMU-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-MMU-419037; NCAM1 interactions.
DR Reactome; R-MMU-8948216; Collagen chain trimerization.
DR BioGRID-ORCS; 12826; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Col4a1; mouse.
DR PRO; PR:P02463; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P02463; protein.
DR Bgee; ENSMUSG00000031502; Expressed in epithelium of lens and 290 other tissues.
DR ExpressionAtlas; P02463; baseline and differential.
DR Genevisible; P02463; MM.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0005587; C:collagen type IV trimer; IDA:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0005201; F:extracellular matrix structural constituent; ISO:MGI.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; ISO:MGI.
DR GO; GO:0048407; F:platelet-derived growth factor binding; ISO:MGI.
DR GO; GO:0071711; P:basement membrane organization; ISO:MGI.
DR GO; GO:0048514; P:blood vessel morphogenesis; ISO:MGI.
DR GO; GO:0007420; P:brain development; ISO:MGI.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISO:MGI.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IGI:MGI.
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; IMP:MGI.
DR GO; GO:0061333; P:renal tubule morphogenesis; ISO:MGI.
DR GO; GO:0061304; P:retinal blood vessel morphogenesis; ISO:MGI.
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; 17.
DR SMART; SM00111; C4; 2.
DR SUPFAM; SSF56436; SSF56436; 2.
DR PROSITE; PS51403; NC1_IV; 1.
PE 1: Evidence at protein level;
KW Angiogenesis; Basement membrane; Collagen; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydroxylation; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT PROPEP 28..172
FT /note="N-terminal propeptide (7S domain)"
FT /id="PRO_0000005750"
FT CHAIN 173..1669
FT /note="Collagen alpha-1(IV) chain"
FT /id="PRO_0000005751"
FT CHAIN 1445..1669
FT /note="Arresten"
FT /id="PRO_0000390483"
FT DOMAIN 1445..1669
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT REGION 47..1443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..1440
FT /note="Triple-helical region"
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 191..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 363..380
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 409..425
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..817
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1245..1259
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1434
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:0000269|PubMed:25645914"
FT MOD_RES 603
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25645914"
FT MOD_RES 605
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25645914"
FT MOD_RES 606
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25645914"
FT MOD_RES 623
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25645914"
FT MOD_RES 626
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25645914"
FT MOD_RES 629
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25645914"
FT MOD_RES 632
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:25645914"
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 /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:0000269|PubMed:22842973"
FT CROSSLNK 1651
FT /note="S-Lysyl-methionine sulfilimine (Lys-Met) (interchain
FT with M-1533)"
FT /evidence="ECO:0000269|PubMed:22842973"
FT CONFLICT 26
FT /note="A -> P (in Ref. 4; CAA29946)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="S -> L (in Ref. 4; CAA29946)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="Q -> S (in Ref. 4; CAA29946)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="Q -> L (in Ref. 4; CAA29946)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="L -> F (in Ref. 4; CAA29946)"
FT /evidence="ECO:0000305"
FT CONFLICT 481
FT /note="P -> L (in Ref. 4; CAA29946)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="Q -> H (in Ref. 4; CAA29946)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="G -> S (in Ref. 2; BAE27208)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="S -> I (in Ref. 4; CAA29946)"
FT /evidence="ECO:0000305"
FT CONFLICT 813
FT /note="Q -> E (in Ref. 1; AAA50292)"
FT /evidence="ECO:0000305"
FT CONFLICT 982
FT /note="Q -> H (in Ref. 4; CAA29946)"
FT /evidence="ECO:0000305"
FT CONFLICT 1397
FT /note="V -> S (in Ref. 10; AAA37342)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1669 AA; 160679 MW; EFEEC72AF301E5CF CRC64;
MGPRLSVWLL LLFAALLLHE ERSRAAAKGD CGGSGCGKCD CHGVKGQKGE RGLPGLQGVI
GFPGMQGPEG PHGPPGQKGD AGEPGLPGTK GTRGPPGAAG YPGNPGLPGI PGQDGPPGPP
GIPGCNGTKG ERGPLGPPGL PGFSGNPGPP GLPGMKGDPG EILGHVPGTL LKGERGFPGI
PGMPGSPGLP GLQGPVGPPG FTGPPGPPGP PGPPGEKGQM GSSFQGPKGD KGEQGVSGPP
GVPGQAQVKE KGDFAPTGEK GQKGEPGFPG VPGYGEKGEP GKQGPRGKPG KDGEKGERGS
PGIPGDSGYP GLPGRQGPQG EKGEAGLPGP PGTVIGTMPL GEKGDRGYPG APGLRGEPGP
KGFPGTPGQP GPPGFPTPGQ AGAPGFPGER GEKGDQGFPG VSLPGPSGRD GAPGPPGPPG
PPGQPGHTNG IVECQPGPPG DQGPPGTPGQ PGLTGEVGQK GQKGESCLAC DTEGLRGPPG
PQGPPGEIGF PGQPGAKGDR GLPGRDGLEG LPGPQGSPGL IGQPGAKGEP GEIFFDMRLK
GDKGDPGFPG QPGMPGRAGT PGRDGHPGLP GPKGSPGSIG LKGERGPPGG VGFPGSRGDI
GPPGPPGVGP IGPVGEKGQA GFPGGPGSPG LPGPKGEAGK VVPLPGPPGA AGLPGSPGFP
GPQGDRGFPG TPGRPGIPGE KGAVGQPGIG FPGLPGPKGV DGLPGEIGRP GSPGRPGFNG
LPGNPGPQGQ KGEPGIGLPG LKGQPGLPGI PGTPGEKGSI GGPGVPGEQG LTGPPGLQGI
RGDPGPPGVQ GPAGPPGVPG IGPPGAMGPP GGQGPPGSSG PPGIKGEKGF PGFPGLDMPG
PKGDKGSQGL PGLTGQSGLP GLPGQQGTPG VPGFPGSKGE MGVMGTPGQP GSPGPAGTPG
LPGEKGDHGL PGSSGPRGDP GFKGDKGDVG LPGMPGSMEH VDMGSMKGQK GDQGEKGQIG
PTGDKGSRGD PGTPGVPGKD GQAGHPGQPG PKGDPGLSGT PGSPGLPGPK GSVGGMGLPG
SPGEKGVPGI PGSQGVPGSP GEKGAKGEKG QSGLPGIGIP GRPGDKGDQG LAGFPGSPGE
KGEKGSAGTP GMPGSPGPRG SPGNIGHPGS PGLPGEKGDK GLPGLDGVPG VKGEAGLPGT
PGPTGPAGQK GEPGSDGIPG SAGEKGEQGV PGRGFPGFPG SKGDKGSKGE VGFPGLAGSP
GIPGVKGEQG FMGPPGPQGQ PGLPGTPGHP VEGPKGDRGP QGQPGLPGHP GPMGPPGFPG
INGPKGDKGN QGWPGAPGVP GPKGDPGFQG MPGIGGSPGI TGSKGDMGLP GVPGFQGQKG
LPGLQGVKGD QGDQGVPGPK GLQGPPGPPG PYDVIKGEPG LPGPEGPPGL KGLQGPPGPK
GQQGVTGSVG LPGPPGVPGF DGAPGQKGET GPFGPPGPRG FPGPPGPDGL PGSMGPPGTP
SVDHGFLVTR HSQTTDDPLC PPGTKILYHG YSLLYVQGNE RAHGQDLGTA GSCLRKFSTM
PFLFCNINNV CNFASRNDYS YWLSTPEPMP MSMAPISGDN IRPFISRCAV CEAPAMVMAV
HSQTIQIPQC PNGWSSLWIG YSFVMHTSAG AEGSGQALAS PGSCLEEFRS APFIECHGRG
TCNYYANAYS FWLATIERSE MFKKPTPSTL KAGELRTHVS RCQVCMRRT
