CO4A4_BOVIN
ID CO4A4_BOVIN Reviewed; 453 AA.
AC Q29442;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Collagen alpha-4(IV) chain;
DE Flags: Fragment;
GN Name=COL4A4;
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], AND PROTEIN SEQUENCE OF 317-328.
RC TISSUE=Lens;
RX PubMed=1370461; DOI=10.1016/s0021-9258(18)48422-0;
RA Mariyama M., Kalluri R., Hudson B.G., Reeders S.T.;
RT "The alpha 4(IV) chain of basement membrane collagen. Isolation of cDNAs
RT encoding bovine alpha 4(IV) and comparison with other type IV collagens.";
RL J. Biol. Chem. 267:1253-1258(1992).
RN [2]
RP PROTEIN SEQUENCE OF 217-255; 257-278; 303-314; 391-399 AND 411-434.
RX PubMed=1468209; DOI=10.3109/03008209209015039;
RA Matsukura H., Michael A.F., Fish A.J., Butkowski R.J.;
RT "Partial protein sequence of the globular domain of alpha 4(IV) collagen
RT chain: sites of sequence variability and homology with alpha 2(IV).";
RL Connect. Tissue Res. 28:231-244(1992).
RN [3]
RP PROTEIN SEQUENCE OF 217-246.
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 [4]
RP PROTEIN SEQUENCE OF 217-237.
RX PubMed=1869555; DOI=10.1016/s0021-9258(18)98618-7;
RA Gunwar S., Ballester F., Kalluri R., Timoneda J., Chonko A.M.,
RA Edwards S.J., Noelken M.E., Hudson B.G.;
RT "Glomerular basement membrane. Identification of dimeric subunits of the
RT noncollagenous domain (hexamer) of collagen IV and the Goodpasture
RT antigen.";
RL J. Biol. Chem. 266:15318-15324(1991).
RN [5]
RP PROTEIN SEQUENCE OF 217-233.
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 -!- 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 protomer, respectively. Associates with LAMB2 at
CC the neuromuscular junction and in GBM (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000255|PROSITE-ProRule:PRU00736}.
CC Note=Colocalizes with COL4A4 and COL4A5 in GBM, tubular basement
CC membrane (TBM) and synaptic basal lamina (BL). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Alpha 3 and alpha 4 type IV collagens are
CC colocalized and present only in basement membranes of kidney, eye,
CC cochlea, lung and brain.
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}.
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DR EMBL; M77480; AAA30458.2; ALT_SEQ; mRNA.
DR PIR; S18804; S18804.
DR AlphaFoldDB; Q29442; -.
DR SMR; Q29442; -.
DR STRING; 9913.ENSBTAP00000018302; -.
DR PaxDb; Q29442; -.
DR PRIDE; Q29442; -.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; Q29442; -.
DR OrthoDB; 63831at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0005587; C:collagen type IV trimer; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
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; 2.
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..453
FT /note="Collagen alpha-4(IV) chain"
FT /id="PRO_0000059413"
FT DOMAIN 228..453
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT REGION <1..222
FT /note="Triple-helical region"
FT REGION 1..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..47
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..75
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..149
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 243..332
FT /note="Or C-243 with C-329"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 276..329
FT /note="Or C-276 with C-332"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 288..294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 351..449
FT /note="Or C-351 with C-446"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 385..446
FT /note="Or C-385 with C-449"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 397..404
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT CONFLICT 219
FT /note="I -> P (in Ref. 2; AA sequence, 3; AA sequence and
FT 5; AA sequence)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 453 AA; 46385 MW; F7ED410AE9A65BC1 CRC64;
GPPGPPGAPG KALKGDIPDP GLPGDQGPPG PDGPRGVPGP PGPPGSVDLL KGEPGDCGLP
GPPGLPGPPG PPGHKGFPGC DGKHGQKGPM GFPGPQGPPG SPGPPGDKGL PGPPGRRGPL
GPPGSRGEPG PPADLDACPR IPGLPGVPGP RGPEGTMGLP GMRGPPGPGC KGEPGLDGRR
GEDGLPGSPG PPGHKGDMGE AGCPGAPGPP GPMGDPGPIG FGPGYLSGFL LVLHSQTDGE
PTCPMGMPRL WTGYSLLYLE GQERAHNQDL GLAGSCLPIF STLPFAYCNI HQVCHYARRN
DRSYWLASTA PLPMTPLSED EIRPYISRCA VCEAPAQAVA VHSQDQSIPP CPRAWRSLWI
GYSFLMHTGA GDQGGGQALM SPGSCLEDFR AAPFLECQGR QGTCHFFANK YSFWLTTVRP
DLQFSSAPLP DTLKESHAQR QKISRCQVCV KHS
