ID   F6RIS8_MOUSE            Unreviewed;       197 AA.
AC   F6RIS8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   02-SEP-2026, entry version 88.
DE   SubName: Full=Collagen, type IV, alpha 3 {ECO:0000313|Ensembl:ENSMUSP00000119094.2};
DE   Flags: Fragment;
GN   Name=Col4a3 {ECO:0000313|Ensembl:ENSMUSP00000119094.2,
GN   ECO:0000313|MGI:MGI:104688};
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 {ECO:0000313|Ensembl:ENSMUSP00000119094.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000119094.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000119094.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RG   Mouse Genome Sequencing Consortium;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0000313|Ensembl:ENSMUSP00000119094.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000119094.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=21750661;
RA   Church D.M., Schneider V.A., Graves T., Auger K., Cunningham F., Bouk N.,
RA   Chen H.C., Agarwala R., McLaren W.M., Ritchie G.R., Albracht D.,
RA   Kremitzki M., Rock S., Kotkiewicz H., Kremitzki C., Wollam A., Trani L.,
RA   Fulton L., Fulton R., Matthews L., Whitehead S., Chow W., Torrance J.,
RA   Dunn M., Harden G., Threadgold G., Wood J., Collins J., Heath P.,
RA   Griffiths G., Pelan S., Grafham D., Eichler E.E., Weinstock G.,
RA   Mardis E.R., Wilson R.K., Howe K., Flicek P., Hubbard T.;
RT   "Modernizing reference genome assemblies.";
RL   PLoS Biol. 9:e1001091-e1001091(2011).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000119094.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000119094.2};
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302,
CC       ECO:0000256|PROSITE-ProRule:PRU00736}.
CC   -!- DOMAIN: Alpha chains of type IV collagen have a non-collagenous domain
CC       (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats
CC       in the long central triple-helical domain (which may cause flexibility
CC       in the triple helix), and a short N-terminal triple-helical 7S domain.
CC       {ECO:0000256|PROSITE-ProRule:PRU00736}.
CC   -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC       (G-X-Y) are hydroxylated in some or all of the chains.
CC       {ECO:0000256|PROSITE-ProRule:PRU00736}.
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:0000256|PROSITE-ProRule:PRU00736}.
CC   -!- SIMILARITY: Belongs to the type IV collagen family.
CC       {ECO:0000256|PROSITE-ProRule:PRU00736}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00736}.
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DR   AlphaFoldDB; F6RIS8; -.
DR   SMR; F6RIS8; -.
DR   PeptideAtlas; F6RIS8; -.
DR   ProteomicsDB; 308203; -.
DR   Antibodypedia; 34379; 291 antibodies from 32 providers.
DR   Ensembl; ENSMUST00000152664.2; ENSMUSP00000119094.2; ENSMUSG00000079465.9.
DR   AGR; MGI:104688; -.
DR   MGI; MGI:104688; Col4a3.
DR   VEuPathDB; HostDB:ENSMUSG00000079465; -.
DR   GeneTree; ENSGT00940000161675; -.
DR   HOGENOM; CLU_1387085_0_0_1; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000079465; Expressed in epithelium of lens and 101 other cell types or tissues.
DR   ExpressionAtlas; F6RIS8; baseline and differential.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005581; C:collagen trimer; IEA:InterPro.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR   Gene3D; 2.170.240.10; Collagen IV, non-collagenous; 1.
DR   InterPro; IPR001442; Collagen_IV_NC.
DR   InterPro; IPR036954; Collagen_IV_NC_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF01413; C4; 2.
DR   SMART; SM00111; C4; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 2.
DR   PROSITE; PS51403; NC1_IV; 1.
PE   1: Evidence at protein level;
KW   Basement membrane {ECO:0000256|ARBA:ARBA00022869, ECO:0000256|PROSITE-
KW   ProRule:PRU00736};
KW   Collagen {ECO:0000256|ARBA:ARBA00023119, ECO:0000256|PROSITE-
KW   ProRule:PRU00736};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00736};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530, ECO:0000256|PROSITE-
KW   ProRule:PRU00736};
KW   Proteomics identification {ECO:0007829|ProteomicsDB:F6RIS8};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|PROSITE-
KW   ProRule:PRU00736}.
FT   DOMAIN          8..150
FT                   /note="Collagen IV NC1"
FT                   /evidence="ECO:0000259|PROSITE:PS51403"
FT   DISULFID        68..74
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00736"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|Ensembl:ENSMUSP00000119094.2"
SQ   SEQUENCE   197 AA;  22381 MW;  0EEA01E6BA6E5AAC CRC64;
     ATGTRMRGFI FTRHSQTTAI PSCPEGTQPL YSGFSLLFVQ GNKRAHGQDL GTLGSCLQRF
     TTMPFLFCNI NNVCNFASRN DYSYWLSTPA LMPMDMAPIS GRALEPYISR CTVCEGPAMA
     IAVHSQTTAI PPCPQDWVSL WKGFSFIMKT YSINCESWRL RENHKPLSGV HEEKTLTKSK
     KPEPFFFFFF FFLFLLK
//