ID A0A2K5L5H5_CERAT Unreviewed; 1692 AA.
AC A0A2K5L5H5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Collagen type IV alpha 4 chain {ECO:0000313|Ensembl:ENSCATP00000008198.1};
GN Name=COL4A4 {ECO:0000313|Ensembl:ENSCATP00000008198.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000008198.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000008198.1}
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_011918055.1; XM_012062665.1.
DR RefSeq; XP_011918056.1; XM_012062666.1.
DR RefSeq; XP_011918057.1; XM_012062667.1.
DR STRING; 9531.ENSCATP00000008198; -.
DR Ensembl; ENSCATT00000028384.1; ENSCATP00000008198.1; ENSCATG00000024575.1.
DR GeneID; 105586970; -.
DR KEGG; caty:105586970; -.
DR CTD; 1286; -.
DR GeneTree; ENSGT00940000153991; -.
DR OMA; ISCNVTY; -.
DR OrthoDB; 2882192at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000024575; Expressed in adult mammalian kidney and 3 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:0005201; F:extracellular matrix structural constituent; IEA:Ensembl.
DR GO; GO:0032836; P:glomerular basement membrane development; 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; 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:UP000233060};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 1467..1692
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000259|PROSITE:PS51403"
FT REGION 61..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..369
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..548
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..644
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..911
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1243
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1280
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1314
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1377
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1692 AA; 164336 MW; D144B8247B2B0347 CRC64;
MSSLHVVLMR CSFRLTKSLA TGPWSLILIL FSVQYVYGSG KKYVGPCGGR DCSVCHCVPE
KGSRGPPGPP GPQGPIGPLG APGPTGLSGE KGMTGDRGPP GTAGDKGDKG PTGVPGFPGL
DGIPGHPGPP GPRGKPGKCG YNGSRGDPGF PGGRGALGPG GPPGHPGEKG EKGNSVFILG
AVKGIQGDRG DPGLPGLPGS WGAGGPAGPA GYPGEPGLVG PPGQPGRPGL KGNPGVGVKG
QMGDPGEVGQ RGSPGPTLLV EPPDFCLYKG EKGIKGIPGM IGLPGPPGRK GESGIGAKGE
KGIPGFPGPW GDPGSYGSPG FPGLKGELGL VGDPGLFGFL GPKGDPGDRG HPGPPGVLVT
PPLPLKGPPG DPGFRGRYGE TGDVGPPGPP GLLGRPGEAC AGMIGPPGPQ GFPGLPGLPG
EAGIPGRPDS ATGKPGKPGS PGLPGAPGLQ GLPGSSVTYC SVGNPGPQGI KGKVGPPGGR
GSKGEKGNEG LCACEPGPMG PPGPPGLPGR QGSKGDLGLP GWLGAKGDPG PPGAEGPPGL
PGKPGAPGPP GNKGAKGDVV ISRVKGHKGE RGPDGPPGFP GQPGSHGLDG HAGEKGDPGL
PGDHEDAIPG GKGFPGPLGP PGKAGPVGPP GLGFPGPPGE RGHPGVPGRP GVRGPDGLKG
QKGDTVSCNV TYPGRQGPPG FDGLPGPKGF PGPQGAPGLS GSDGHKGRPG TPGTSEIPGP
PGFRGDIGDP GFGGEKGSSP VGPPGPPGSP GVNGQKGIPG DPAFGHLGPP GKRGLSGVPG
IKGPRGDPGY PGAEGPAGIP GFPGLKGPKG REGHAGFPGV PGPPGHSCER GAPGIPGQPG
LPGDPGSPGA PGGKGQPGDV GPPGPAGMKG LPGLPGRPGA HGPPGLPGIP GPFGDDGLPG
PPGPKGPRGL PGFPGFPGER GKPGAEGCPG TKGEPGEKGM SGYPGDRGVR GAKGALGPPG
DEGEMAIISK KGKPGEPGPP GDDGFPGERG DKGTPGMQGR RGEPGRYGPP GFHRGEPGEK
GQPGPPGPPG PPGSTGLRGF IGFPGLPGDQ GEPGSPGPPG FSGIDGARGP KGNKGDPAPA
SHFGPPGPKG EPGSSGCPGH FGASGEQGLP GVQGPRGSPG RPGPPGSSGP PGCPGDRGMP
GLRGQPGEMG DPGPRGLQGD PGIPGPPGIK GPSGSPGLNG LHGLKGQKGT KGASGLHDVG
PPGPVGMPGL KGERGDPGSP GISPPGPCGE KGLPGPPGRS GPPGPAGATG RAPKDIPDPG
PSGDQGPPGP DGPRGAPGPP GLPGSVDLLR GEPGDCGLPG PPGLPGPPGP PGYKGFPGCD
GKDGQKGPMG FPGPQGPHGF PGPPGEKGLP GPPGRKGPTG LPGPRGEPGP PADADDCPRI
PGLPGVPGLR GPEGAMGLPG MRGPPGPGCK GEPGLDGRRG MDGIPGSPGP PGRKGDTGED
GYPGGPGPPG PTGDPGPKGF GAGYLSGFLL VLHSQTDQEP TCPLGMPRLW TGYSLLYLEG
QEKAHNQDLG LAGSCLPVFS TLPFAYCNIH QVCHYAQRND RSYWLASAAP LPMMPLSEEA
IRPYVSRCAV CEAPAQAVAV HSQDQSIPPC PQTWRSLWIG YSFLMHTGAG DQGGGQALMS
PGSCLEDFRA APFLECQGRQ GTCHFFANEY SFWLTTVKAD LQFSSAPAPD TLKESQAQRQ
KISRCQVCMK YS
//
