CO4A2_BOVIN
ID CO4A2_BOVIN Reviewed; 227 AA.
AC Q7SIB3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Collagen alpha-2(IV) chain;
DE Flags: Fragment;
GN Name=COL4A2;
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 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND DISULFIDE BONDS.
RX PubMed=11970952; DOI=10.1074/jbc.m201740200;
RA Sundaramoorthy M., Meiyappan M., Todd P., Hudson B.G.;
RT "Crystal structure of NC1 domains. Structural basis for type IV collagen
RT assembly in basement membranes.";
RL J. Biol. Chem. 277:31142-31153(2002).
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. Potently
CC inhibits angiogenesis and tumor growth (By similarity). {ECO:0000250}.
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:P08122}.
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 -!- 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 -!- SIMILARITY: Belongs to the type IV collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00736}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PDB; 1M3D; X-ray; 2.00 A; C/F/I/L=1-227.
DR PDB; 1T60; X-ray; 1.50 A; C/F/I/L/O/R/U/X=1-227.
DR PDB; 1T61; X-ray; 1.50 A; C/F=1-227.
DR PDBsum; 1M3D; -.
DR PDBsum; 1T60; -.
DR PDBsum; 1T61; -.
DR AlphaFoldDB; Q7SIB3; -.
DR SMR; Q7SIB3; -.
DR ComplexPortal; CPX-3107; Collagen type IV trimer variant 1.
DR STRING; 9913.ENSBTAP00000005916; -.
DR GlyConnect; 109; 20 N-Linked glycans.
DR PaxDb; Q7SIB3; -.
DR PRIDE; Q7SIB3; -.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; Q7SIB3; -.
DR OrthoDB; 63831at2759; -.
DR EvolutionaryTrace; Q7SIB3; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR Gene3D; 2.170.240.10; -; 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; 2.
DR SUPFAM; SSF56436; SSF56436; 2.
DR PROSITE; PS51403; NC1_IV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Basement membrane; Collagen; Disulfide bond;
KW Extracellular matrix; Hydroxylation; Reference proteome; Repeat; Secreted.
FT CHAIN <1..227
FT /note="Collagen alpha-2(IV) chain"
FT /id="PRO_0000059411"
FT DOMAIN 4..227
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 19..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736,
FT ECO:0000269|PubMed:11970952"
FT DISULFID 52..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736,
FT ECO:0000269|PubMed:11970952"
FT DISULFID 64..70
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736,
FT ECO:0000269|PubMed:11970952"
FT DISULFID 127..223
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736,
FT ECO:0000269|PubMed:11970952"
FT DISULFID 161..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736,
FT ECO:0000269|PubMed:11970952"
FT DISULFID 173..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736,
FT ECO:0000269|PubMed:11970952"
FT NON_TER 1
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 24..37
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:1T60"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1T60"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:1T60"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1T60"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 132..144
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:1T60"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:1T60"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:1T60"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:1T60"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:1T60"
FT STRAND 219..224
FT /evidence="ECO:0007829|PDB:1T60"
SQ SEQUENCE 227 AA; 25061 MW; BC81FF77053BEBD4 CRC64;
ISIGYLLVKH SQTDQEPMCP VGMNKLWSGY SLLYFEGQEK AHNQDLGLAG SCLARFSTMP
FLYCNPGDVC YYASRNDKSY WLSTTAPLPM MPVAEEDIRP YISRCSVCEA PAVAIAVHSQ
DVSIPHCPAG WRSLWIGYSF LMHTAAGDEG GGQSLVSPGS CLEDFRATPF IECNGARGTC
HYYANKYSFW LTTIPEQSFQ GTPSADTLKA GLIRTHISRC QVCMKNL
