CO4A4_RABIT
ID CO4A4_RABIT Reviewed; 623 AA.
AC P55787;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Collagen alpha-4(IV) chain;
DE Flags: Fragment;
GN Name=COL4A4;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Corneal endothelium;
RX PubMed=1429714; DOI=10.1016/s0021-9258(18)35902-7;
RA Kamagata Y., Mattei M.-G., Ninomiya Y.;
RT "Isolation and sequencing of cDNAs and genomic DNAs encoding the alpha 4
RT chain of basement membrane collagen type IV and assignment of the gene to
RT the distal long arm of human chromosome 2.";
RL J. Biol. Chem. 267:23753-23758(1992).
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 promoter, 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 -!- 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; L01477; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A45137; A45137.
DR AlphaFoldDB; P55787; -.
DR SMR; P55787; -.
DR STRING; 9986.ENSOCUP00000026501; -.
DR eggNOG; KOG3544; Eukaryota.
DR InParanoid; P55787; -.
DR Proteomes; UP000001811; 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 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; 4.
DR SMART; SM00111; C4; 2.
DR SUPFAM; SSF56436; SSF56436; 2.
DR PROSITE; PS51403; NC1_IV; 1.
PE 2: Evidence at transcript level;
KW Basement membrane; Cell adhesion; Collagen; Disulfide bond;
KW Extracellular matrix; Hydroxylation; Reference proteome; Repeat; Secreted.
FT CHAIN <1..623
FT /note="Collagen alpha-4(IV) chain"
FT /id="PRO_0000059414"
FT DOMAIN 398..623
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT REGION <1..392
FT /note="Triple-helical region"
FT REGION 1..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..319
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 413..502
FT /note="Or C-413 with C-499"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 446..499
FT /note="Or C-446 with C-502"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 458..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 521..619
FT /note="Or C-521 with C-616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 555..616
FT /note="Or C-555 with C-619"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT DISULFID 567..574
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00736"
FT NON_TER 1
SQ SEQUENCE 623 AA; 62393 MW; CCBC9BB31242FE82 CRC64;
GPKGNKGDAA SQFGPPGPKG EPGSRGYQGH FGGPGEQGFP GVQGHRGPPG RPGSPGSSGP
PGCPGGQGIP GLEGHPGEVG DPGPRGLLGD PGRPGPPGMK GPSGSPGLDG LHGLKGQKGT
KGASGLHEMG PPGPMGIPGI KGDKGEPGSP GISPPGLFGE RGPPGLPGRP GPVGPMGATG
RAPKGDIPDP GPPGDQGLPG PDGPRGAPGP AGPPGSVDLL KGEPGDCGVP GPPGPPGPPG
PPGCQGVPGC DGHDGQKGPM GFPGLQGPHG LPGLPGEKGL PGSPGRKGPT GPPGYRGEPG
PPADEDSCPR IPGLPGVPGP RGPEGAMGFP GQRGPPGQGC KGEPGLDGKR GRDGVPGAPG
PPGHKGDTGE AGRPGAPGPP GPTGDPGPKG LGPGYLSGFL LVLHSQTDQE PACPMGMPRL
WTGYSLLYLE GQEKAHNQDL GLAGSCLPIF STLPFAYCNI HQVCHYAQRN DKSYWLASAG
PLPMMPLSEE EIRPYISRCA VCEAPAQAVA VHSQDQSIPP CPRAWRSLWI GYSFLMHTGA
GDQGGGQALM SPGSCLEDFR AAPFLECQGR QGTCHFFANE YSFWLTTVPP DLQVFSAPSP
DTLKESQAQR QKISRCQVCV KYS
