ID A0A2K6AYU6_MACNE Unreviewed; 1683 AA.
AC A0A2K6AYU6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Collagen type IV alpha 2 chain {ECO:0000313|Ensembl:ENSMNEP00000004318.1};
GN Name=COL4A2 {ECO:0000313|Ensembl:ENSMNEP00000004318.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000004318.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000004318.1}
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 RefSeq; XP_011745895.1; XM_011747593.1.
DR STRING; 9545.ENSMNEP00000004318; -.
DR Ensembl; ENSMNET00000022021.1; ENSMNEP00000004318.1; ENSMNEG00000020056.1.
DR GeneID; 105485298; -.
DR KEGG; mni:105485298; -.
DR CTD; 1284; -.
DR GeneTree; ENSGT00940000157234; -.
DR OMA; ATEPIWS; -.
DR OrthoDB; 2882192at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000020056; Expressed in lung and 12 other cell types or tissues.
DR GO; GO:0005587; C:collagen type IV trimer; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; 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:SF714; COLLAGEN ALPHA-4(IV) CHAIN; 1.
DR Pfam; PF01413; C4; 2.
DR Pfam; PF01391; Collagen; 18.
DR SMART; SM00111; C4; 1.
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 Lectin {ECO:0000256|ARBA:ARBA00022734};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1683
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014409399"
FT DOMAIN 1489..1627
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000259|PROSITE:PS51403"
FT REGION 60..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..444
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..654
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..768
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1683 AA; 164134 MW; 6C8AA35E328BB4A7 CRC64;
MERDQRAVAG PALRRWLLLG TVTVGFLAQG VLAGVKKFDV PCGGRDCSGG CQCYPEKGGR
GQPGPVGPQG YNGPPGLQGF PGLQGRKGDK GERGAPGITG PKGDVGARGV SGFPGADGIP
GHPGQGGPRG RPGYDGCNGT QGDSGPQGPP GSEGFTGPPG PQGPKGQKGE PYALPREERD
RYRGEPGEPG LVGFQGPPGR PGPVGQMGPV GAPGRPGPPG PPGPKGQQGN RGLGFYGVKG
EKGDVGQPGP NGIPSDTLHP IVAPTGVTFH PDQYKGEKGS EGEPGIRGIS LKGEEGIMGF
PGPRGPPGLS GEKGSPGQKG SRGLDGYQGP DGPRGPKGEA GDLGPPGLPA YSPHPSLAKG
ARGDPGFPGA QGEPGSQGEP GDPGPRGPPG LSIGDEDQRR GLPGEMGPKG FIGDPGIPAL
YPGPPGPDGK PGPPGPPGLP GPPGPDGFLF GRKGAKGTPG FPGLSGSPGA RGPKGWKGDA
GDCRCAEGDE AVRGLPGLPG PKGFAGINGE PGRKGDKGDP GQHGLPGFPG LKGVPGNVGA
PGPKGAKGDS RTITTKGERG QPGVPGVPGM KGDDGSPGRN GLDGFPGLPG PPGDGIKGPP
GDAGYPGIPG TKGTPGEMGP PGLGLPGFKG QRGFPGDAGL PGPPGFPGPP GPAGTPGQID
CDTDVKRPIG GDRQEAVQPG CIGGPKGLPG LPGPPGPSGA KGLRGIPGFS GADGGPGPKG
LPGDPGREGF PGPPGFIGPR GSKGAVGLPG PDGPPGPIGL PGPDGPPGDR GLPGEVLGAQ
PGPRGDAGVP GQPGFKGLPG DRGPPGFRGS QGMPGMPGLK GQPGLPGPSG QPGLSGPPGQ
HGFPGAPGQE GPLGLPGIPG LEGLPGDRGD PGDIGAPGPV GMKGVSGDRG DAGLAGERGH
PGSPGFKGID GMPGTPGLKG ERGSPGMDGF QGMPGLKGRP GFPGSKGEAG FFGIPGLKGL
AGEPGFKGSR GDPGPPGPPP IILPGMKDIK GEKGDEGPMG LKGYLGAKGI QGMPGIPGLS
GIPGLPGRPG HIKGVKGDIG APGIPGLPGF PGVAGPPGIT GFPGFIGSRG DKGAPGRAGL
YGEIGPTGDF GDIGDTINLP GRPGLKGEQG TAGIPGLKGF FGEKGTEGDI GFPGITGVTG
VQGPPGLKGQ TGFPGLTGPP GSQGEPGRIG LPGGKGDDGW PGIPGLPGFP GLRGIRGLHG
LPGTKGFPGS PGADIHGDPG FPGPPGDRGD PGDANTLPGP VGVPGQKGEQ GAPGERGPPG
SPGLQGFPGI TPPSNISGAP GDKGAPGIFG LKGYRGPPGP PGSAALPGSK GDAGNPGAPG
TPGTKGWAGD SGPQGRPGVF GLPGEKGPRG EQGFMGNTGP AGAVGDRGPK GPKGDPGFPG
APGIVGAPGI AGIPQKIAIP PGTVGPQGRR GPPGAPGEMG PQGPPGEPGF RGAPGKAGPQ
GRGGVSAVPG FRGDEGPVGH QGPIGQEGAP GRPGSPGLPG MPGRSVSIGY LLVKHSQTDQ
EPMCPVGMNK LWSGYSLLYF EGQEKAHNQD LGLAGSCLAR FSTMPFLYCN PGDVCYYASR
NDKSYWLSTT APLPMMPVAE DEIKPYISRC SVCEAPAVAI AVHSQDVSIP HCPAGWRSLW
IGYSFLMVRG IYPVPLPSHT LAGDTARTPA FVRVIGQGSS GCALHEGTWP RERERAGIQL
TLC
//
