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   27-MAR-2024, entry version 205.
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   GlyCosmos; P02463; 1 site, No reported glycans.
DR   GlyGen; P02463; 1 site.
DR   iPTMnet; P02463; -.
DR   PhosphoSitePlus; P02463; -.
DR   EPD; P02463; -.
DR   MaxQB; P02463; -.
DR   PaxDb; 10090-ENSMUSP00000033898; -.
DR   PeptideAtlas; P02463; -.
DR   ProteomicsDB; 279129; -.
DR   Pumba; P02463; -.
DR   Antibodypedia; 3436; 967 antibodies from 39 providers.
DR   DNASU; 12826; -.
DR   Ensembl; ENSMUST00000033898.10; ENSMUSP00000033898.10; ENSMUSG00000031502.12.
DR   GeneID; 12826; -.
DR   KEGG; mmu:12826; -.
DR   UCSC; uc009kvb.2; mouse.
DR   AGR; MGI:88454; -.
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; PYHVIKG; -.
DR   OrthoDB; 2882192at2759; -.
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-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   BioGRID-ORCS; 12826; 3 hits in 80 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 294 other cell types or tissues.
DR   ExpressionAtlas; P02463; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR   GO; GO:0005587; C:collagen type IV trimer; IDA:MGI.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
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; Collagen IV, non-collagenous; 1.
DR   InterPro; IPR008160; Collagen.
DR   InterPro; IPR001442; Collagen_IV_NC.
DR   InterPro; IPR036954; Collagen_IV_NC_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   PANTHER; PTHR24023:SF1100; FIBRILLAR COLLAGEN NC1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01413; C4; 2.
DR   Pfam; PF01391; Collagen; 16.
DR   SMART; SM00111; C4; 2.
DR   SUPFAM; SSF56436; C-type lectin-like; 2.
DR   PROSITE; PS51403; NC1_IV; 1.
DR   Genevisible; P02463; MM.
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
//