CO4A3_BOVIN
ID CO4A3_BOVIN Reviewed; 471 AA.
AC Q28084;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=Collagen alpha-3(IV) chain;
DE Flags: Fragment;
GN Name=COL4A3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens;
RX PubMed=1985905; DOI=10.1016/s0021-9258(18)52397-8;
RA Morrison K.E., Germino G.G., Reeders S.T.;
RT "Use of the polymerase chain reaction to clone and sequence a cDNA encoding
RT the bovine alpha 3 chain of type IV collagen.";
RL J. Biol. Chem. 266:34-39(1991).
RN [2]
RP PROTEIN SEQUENCE OF 227-258.
RC TISSUE=Kidney;
RX PubMed=2318822; DOI=10.1016/s0021-9258(19)39384-6;
RA Gunwar S., Saus J., Noelken M.E., Hudson B.G.;
RT "Glomerular basement membrane. Identification of a fourth chain, alpha 4,
RT of type IV collagen.";
RL J. Biol. Chem. 265:5466-5469(1990).
RN [3]
RP PROTEIN SEQUENCE OF 227-254, AND HYDROXYLATION AT PRO-232 AND PRO-238.
RX PubMed=3417661; DOI=10.1016/s0021-9258(18)37714-7;
RA Saus J., Wieslander J., Langeveld J.P.M., Quinones S., Hudson B.G.;
RT "Identification of the Goodpasture antigen as the alpha 3(IV) chain of
RT collagen IV.";
RL J. Biol. Chem. 263:13374-13380(1988).
RN [4]
RP PROTEIN SEQUENCE OF 227-244.
RX PubMed=2438283; DOI=10.1016/s0021-9258(18)47648-x;
RA Butkowski R.J., Langeveld J.P.M., Wieslander J., Hamilton J., Hudson B.G.;
RT "Localization of the Goodpasture epitope to a novel chain of basement
RT membrane collagen.";
RL J. Biol. Chem. 262:7874-7877(1987).
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:Q01955, ECO:0000250|UniProtKB:Q9QZS0}.
CC -!- SUBUNIT: There are six type IV collagen isoforms, alpha 1(IV)-alpha
CC 6(IV), each of which can form a triple helix structure with 2 other
CC chains to generate type IV collagen network. The alpha 3(IV) chain
CC forms a triple helical protomer with alpha 4(IV) and alpha 5(IV); this
CC triple helical structure dimerizes through NC1-NC1 domain interactions
CC such that the alpha 3(IV), alpha 4(IV) and alpha 5(IV) chains of one
CC protomer connect with the alpha 5(IV), alpha 4(IV) and alpha 3(IV)
CC chains of the opposite promoter, respectively (By similarity).
CC Interacts with ITGB3 (By similarity). Associates with LAMB2 at the
CC neuromuscular junction and in GBM (By similarity).
CC {ECO:0000250|UniProtKB:Q01955, ECO:0000250|UniProtKB:Q9QZS0}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane.
CC -!- DOMAIN: Alpha chains of type IV collagen have a non-collagenous domain
CC (NC1) at their C-terminus, frequent interruptions of the G-X-Y repeats
CC in the long central triple-helical domain (which may cause flexibility
CC in the triple helix), and a short N-terminal triple-helical 7S domain.
CC -!- PTM: Prolines at the third position of the tripeptide repeating unit
CC (G-X-Y) are hydroxylated in some or all of the chains.
CC {ECO:0000255|PROSITE-ProRule:PRU00736, ECO:0000269|PubMed:3417661}.
CC -!- PTM: Type IV collagens contain numerous cysteine residues which are
CC involved in inter- and intramolecular disulfide bonding. 12 of these,
CC located in the NC1 domain, are conserved in all known type IV
CC collagens.
CC -!- PTM: The trimeric structure of the NC1 domains is stabilized by
CC covalent bonds between Lys and Met residues. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Thought to be phosphorylated by CERT, but CERT
CC does not have kinase activity. {ECO:0000250|UniProtKB:Q01955}.
CC -!- SIMILARITY: Belongs to the type IV collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00736}.
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DR EMBL; M63139; AAA62708.1; -; mRNA.
DR PIR; A39024; A39024.
DR AlphaFoldDB; Q28084; -.
DR SMR; Q28084; -.
DR STRING; 9913.ENSBTAP00000028418; -.
DR PaxDb; Q28084; -.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; Q28084; -.
DR OrthoDB; 63831at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
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; 4.
DR SMART; SM00111; C4; 2.
DR SUPFAM; SSF56436; SSF56436; 2.
DR PROSITE; PS51403; NC1_IV; 1.
PE 1: Evidence at protein level;
KW Basement membrane; Cell adhesion; Collagen; Direct protein sequencing;
KW Disulfide bond; Extracellular matrix; Hydroxylation; Reference proteome;
KW Repeat; Secreted.
FT CHAIN <1..471
FT /note="Collagen alpha-3(IV) chain"
FT /id="PRO_0000059412"
FT DOMAIN 246..470
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT REGION <1..238
FT /note="Triple-helical region"
FT REGION 1..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 106..108
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 48..62
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..200
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 232
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2438283,
FT ECO:0000269|PubMed:3417661"
FT MOD_RES 238
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2438283,
FT ECO:0000269|PubMed:3417661"
FT DISULFID 261..352
FT /note="Or C-261 with C-349"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 294..349
FT /note="Or C-294 with C-352"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 306..312
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 371..466
FT /note="Or C-371 with C-463"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 405..463
FT /note="Or C-405 with C-466"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 417..423
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT CROSSLNK 334
FT /note="S-Lysyl-methionine sulfilimine (Met-Lys) (interchain
FT with K-452)"
FT /evidence="ECO:0000250"
FT CROSSLNK 452
FT /note="S-Lysyl-methionine sulfilimine (Lys-Met) (interchain
FT with M-334)"
FT /evidence="ECO:0000250"
FT CONFLICT 253
FT /note="S -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 471 AA; 47585 MW; C03B66F14E7008DE CRC64;
GLPGRKGPVG DAGPPGQLGV TGPQGAPGFP GVTIPGQKGD RGPPGSRGNP GMPGPPGPPG
SPVEGIKGDK GLMGEPGQRG PPGAIGDMGS PGHPGAPGVP GQPGARGDPG FYGFPGMKGK
KGNSGFPGPP GPPGQSGPKG PPGVRGEPGT VKIISLPGSP GPPGSAGEPG MQGEPGPPGP
PGDPGPCGPK GKPGEDGPPG TPGPTGEKGN KGCKGEQGPP GSDGLPGLKG KPGDTGPPAA
GAVMRGFVFT RHSQTTAIPS CPEGTEPLYS GFSLLFVQGN EQAHGQDLGT LGSCLQRFTT
MPFLFCNIND VCNFASRNDY SYWLSTPAMI PMDMAPITGR ALEPYISRCT VCEGPAIAIA
VHSQTTDIPP CPAGWISLWK GFSFIMFTSA GSEGAGQALA SPGSCLEEFR ASPFIECHGR
GTCNYYSNSY SFWLASLDPK RMFRKPIPST VKAGELENII SRCQVCMKMR P
