ID U3JWR5_FICAL Unreviewed; 898 AA.
AC U3JWR5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Collagen type IV alpha 3 chain {ECO:0000313|Ensembl:ENSFALP00000007219.2};
GN Name=COL4A3 {ECO:0000313|Ensembl:ENSFALP00000007219.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000007219.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000007219.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000007219.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00003696}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Secreted, extracellular space, extracellular matrix, basement membrane
CC {ECO:0000256|ARBA:ARBA00004302}.
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DR AlphaFoldDB; U3JWR5; -.
DR STRING; 59894.ENSFALP00000007219; -.
DR Ensembl; ENSFALT00000007251.2; ENSFALP00000007219.2; ENSFALG00000006907.2.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000161675; -.
DR HOGENOM; CLU_002023_0_0_1; -.
DR Proteomes; UP000016665; Chromosome 9.
DR GO; GO:0005587; C:collagen type IV trimer; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0005178; F:integrin binding; IEA:Ensembl.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0072577; P:endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0032836; P:glomerular basement membrane development; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:1905563; P:negative regulation of vascular endothelial cell proliferation; IEA:Ensembl.
DR Gene3D; 2.170.240.10; Collagen IV, non-collagenous; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR001442; Collagen_IV_NC.
DR InterPro; IPR036954; Collagen_IV_NC_sf.
DR InterPro; IPR016187; CTDL_fold.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1077; COLLAGEN ALPHA-3(IV) CHAIN; 1.
DR Pfam; PF01413; C4; 2.
DR Pfam; PF01391; Collagen; 9.
DR SMART; SM00111; C4; 2.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR PROSITE; PS51403; NC1_IV; 1.
PE 4: Predicted;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..898
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032838691"
FT DOMAIN 673..897
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000259|PROSITE:PS51403"
FT REGION 48..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 898 AA; 88753 MW; 75CFCA867818D74A CRC64;
MLTQSLKLNL ALNLLSCLLG DRGSPGLPGD PGFPGRPAEC LIGLPGLPGG QGATGPPGGR
GLQGSKGNLG PPGLSIPGIY GRPGEPGLVG LQGNTGLPGP KGQSGRPGIS GLPGARGDPG
AMGLLGIPGP PGMAGRPGSP GIRGSPGFPG IKGRKGFLGE KGETGDKGFP GPSETLVGIG
DKGERGLKGA QGRMGARGEK GDVGVQGPPG VDGSEGIPGL PGAKGFMGLP GTPGGQGFPG
ALGNQGDMGI PGPKGQKGSP GFPGPSGDPG PPGYGGFPGD KGDPGYPSAG PPGEPGPKGD
PGPPGVFGSK GEKGSEGHPG LTGVPGPHGV RGETGGAGIP GKCGPPGDMG DKARQGRPGQ
PGVPGPPGAV GVPGKHGLVG ERGTQGQDGM PGPPGVKGEP GPPGRGIPGV RGIPGRRGIK
GDMGLPGFPG PPGAKGQQGD QGPIGPPGLV GLPGFQGATG MAVTGQKGNR GIPGAHGRPG
APGFPGLPGL STLSMKGSKG VRGADGIPGP RGPAGDIGPP GPKGIEGRSG YPGARGHPGF
LGFPGVKGEK GNQGPPGPQG AEGPRGPKGQ HGPPGVSGKT FSIPGSKGPP GLPGIPGTPG
DQGVQGIPGL QGPKGVKGLP GRFGHPGHPG LPGPKGDRGF PGQRGQPGLI GFPGLQGLPG
SPGTIVAGPT RKGFIFTRHS QTTKIPSCPH GTSQIYVGYS LLFVQGNERA HGQDLGTAGS
CLQRFSTMPF LFCSPNDVCS FASRNDYSYW LSTTVVMPPD MAPISGRALE PQISRCVVCE
GAAMVIAVHS QTTVVPACPD GWMSLWKGFS FVMYTSAGSE ASGQALASPG SCLEEFRAVP
FIECHGRGTC NYYTNSYSFW LASLNPRRMF RRPVPQTLKA GQLENIISRC QVCMRRPI
//
