ID A0A2K5CMJ4_AOTNA Unreviewed; 1587 AA.
AC A0A2K5CMJ4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Collagen type IV alpha 3 chain {ECO:0000313|Ensembl:ENSANAP00000009923.1};
GN Name=COL4A3 {ECO:0000313|Ensembl:ENSANAP00000009923.1};
OS Aotus nancymaae (Ma's night monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC Aotus.
OX NCBI_TaxID=37293 {ECO:0000313|Ensembl:ENSANAP00000009923.1, ECO:0000313|Proteomes:UP000233020};
RN [1] {ECO:0000313|Ensembl:ENSANAP00000009923.1}
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 STRING; 37293.ENSANAP00000009923; -.
DR Ensembl; ENSANAT00000027718.1; ENSANAP00000009923.1; ENSANAG00000022940.1.
DR GeneTree; ENSGT00940000161675; -.
DR Proteomes; UP000233020; Unplaced.
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:SF1019; COLLAGEN; 1.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR Pfam; PF01413; C4; 2.
DR Pfam; PF01391; Collagen; 12.
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 Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Reference proteome {ECO:0000313|Proteomes:UP000233020};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 1362..1586
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000259|PROSITE:PS51403"
FT REGION 26..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 243..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..318
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..376
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..556
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..626
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1304
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1587 AA; 154618 MW; F9F9A807370CC04D CRC64;
LTATSTSQGC ICKEKGQCFC DGAKGQKGEK GFPGPPGSPG QKGFTGPEGL PGPQGPKGSP
GLPGLTGAKG VRGITGLPGF SGSPGLPGTP GNTGPYGLAG VPGCNGSKGE QGFPGLPGTP
GYPGIPGSAG LKGQKGAPAK GEDIELDAKG DPGLPGAPGP QGVKGLTGPP GPPGTVIVTL
TGPDNRTNLK GEKGDKGAMG EPGPPGPSGL PGESYGSEKG LAIFIKFHVF DLFLLDGVPG
FPGSEGVKGN RGFPGLTGED GIKGQKGDIG PPGFRGPTEY YDTYQEKGDK GIPGPPGPKG
ARGPQGPSGP PGVPGSPGPS RPGLRGVPGW PGLKGSKGER GPPGKDAMGT PGSPGCPGSP
GPTGSPGPPG PPGDIVFRKG PPGDRGLPGY LGSPGILGVD GPKGEPGLLC TQCPYIPGPP
GLPGLPGLHG VKGIPGRQGA PGLKGSPGSP GNTGLPGFPG FPGAQGDPGL KGEKGETLQP
KGQVGAPGDP GLRGQPGRKG LDGIPGTPGV KGLPGPKGEL ALSGEKGDQG PPGDPGSPGF
PGPAGPAGPP GYGPQGKPGP KGTQGVPGAP GPPGEAGWLV FFPVLFSDGV GIPGSMGKYG
DPGLPGPDGE PGIPGIGFPG PPGPKGDQGF PGTKGSLGCP GKMGEPGLPG KPGLPGAKGE
PALAMPGGPG APGFPGERGN SGEHGEIGLP GLPGLPGTPG NEGLDGPRGD PGQPGPPGEQ
GPQGRCIEGP RGAQGLPGLN GLKGQQGRRG KTGPKGDPGI PGLDRSGFPG ETGSPGRPGH
QGETGPPGQK GYPGNPGILG PPGEDGMVGM MGFPGAIGSP GPPGNPGMPG QRGSLGIPGV
KGQRGTPGAK GEQGDKGNPG PSQISHLIGD KGEPGLKGFA GNVGEKGNRG VPGLPGLKGL
QGLPGPPGPP GPRGDLGSIG HPGEPGPRGV PGSMGNMGMP GSKGRRGTLG FPGRAGRPGL
PGIHGLQGDK GEPGYSEGTR PGPPGPTGDP GLPGDTGKKG EMGQPGPPGH SGPAGPEGVI
GSPGSPGLPG KPGPHGDLGF KGIKGFLGPP GIKGPPGLPG FPGSPGPMGI RGDQGHDGIP
GPAGEKGETG LLGAPPGPRG NPGAQGAKGD RGSPGLPGLP GRKGAMGDAG PRGPTGIEGF
PGPPGLPGAI IPGQKGNRGP PGSRGRPGDP GPLGPPGSHV KGIKGDKGSM GHPGPKGPPG
TVGDMGPPGH LGAPGTPGLP GLRGDPGFRG FPGVKGEKGN PGFLGSIGPP GPIGPKGPPG
IRGDPGTLQI ISLPGSPGPP GTPGEPGMRG EPGPPGPPGN LGPCGPRGKP GKDGKPGIPG
PVGEKGNKGS KGEQGPPGSD GLPGLKGKPG DIGSPATWTT RGFVFTRHSQ TTAIPSCPEG
TVPLYSGFSF LYVQGNQRAH GQDLGTLGSC LQRFTTMPFL FCNINDVCNF ASRNDYSYWL
STPALMPMNM APITGRALEP YISRCTVCEG PAIAIAVHSQ TTDIPPCPHG WISLWKGFSF
IMFTSAGSEG AGQALASPGS CLEEFRASPF LECHGRGTCN YYSNSYSFWL ASLNPERMFR
KPIPSTMKAG ELEKIVSRCQ VCMKKRQ
//
