ID A0A3Q7T5J7_VULVU Unreviewed; 1712 AA.
AC A0A3Q7T5J7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Collagen alpha-2(IV) chain {ECO:0000313|RefSeq:XP_025864648.1};
GN Name=COL4A2 {ECO:0000313|RefSeq:XP_025864648.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025864648.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025864648.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025864648.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025864648.1};
RG RefSeq;
RL Submitted (NOV-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_025864648.1; XM_026008863.1.
DR STRING; 9627.ENSVVUP00000028014; -.
DR KEGG; vvp:112927466; -.
DR OrthoDB; 2882192at2759; -.
DR Proteomes; UP000286640; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
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:SF533; COLLAGEN ALPHA-6(IV) CHAIN; 1.
DR Pfam; PF01413; C4; 2.
DR Pfam; PF01391; Collagen; 17.
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 ECO:0000313|RefSeq:XP_025864648.1};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1712
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018597355"
FT DOMAIN 1489..1712
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000259|PROSITE:PS51403"
FT REGION 60..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..226
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..443
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..656
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..768
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..842
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1712 AA; 167575 MW; 41B736D2A149171D CRC64;
MDRPRCSASS PALRRWLLLG AVTVGLLAQS VLAGVKKFDV PCGGRDCSGG CQCYPEKGGR
GQPGPVGPQG YTGPPGLQGF PGLQGRKGDK GERGSPGITG PKGDVGARGV SGFPGADGIP
GHPGQGGPRG PPGYDGCNGT RGDVGRQGPE GPAGFLGPPG PQGPKGQKGE PYALSSVDRD
KYRGEPGEPG LVGFQGPPGR PGPIGQMGPV GAPGRPGPPG PPGPKGQPGN RGLGFYGEKG
EKGDMGLPGP NGIPSDTHHA IIGPMKEMFH PDQYKGEKGS EGEPGRKGIS LKGEEGIMGF
SGTRGAPGYD GEKGSPGQKG SKGLDGYQGP DGPPGPKGEA GDRGPPGAPA YFPHPSQVKG
ARGDPGFPGT HGDPGSRGEP GDPGPPGLPG PSIRDEDGKR GLPGEMGPKG FIGEPGIPAL
YPGPPGTDGK PGLRGPPGAA GPPGPDGFLF GLKGTEGSAG FPGPSGFPGA RGQKGWKGDA
GDCKCAEGDQ FIGGLPGLPG PKGFPGINGE PGRKGSQGDP GQHGIPGFPG FKGAPGTIGP
PGPKGMKGDS RAITTKGERG QPGVPGVPGL KGDDGVPGRD GLDGFPGLPG PPGDGIKGPP
GDSGYPGAPG TKGAPGERGP PGLGLPGPKG ERGFPGDAGL PGPPGFPGPP GPPGTPGQID
CDTGVKRPIG GDGQEAVQPD CVRGPMGSPG LPGPPGPTGA KGLQGIPGLS GADGTPGLRG
LPGDPGREGF PGPPGFVGPR GSKGAVGLPG PDGHPGPTGL PGPVGPPGDR GLPGEVLGAQ
PGPRGDAGLP GHPGLKGPPG ERGPPGFRGS QGMPGMPGLK GQPGFPGPSG QPGLPGPPGQ
HGFPGAPGRE GPLGLPGASG HGGLPGDRGD PGDTGVPGPV GMKGLSGDRG DPGLLGERGP
PGSPGFKGMS GMPGIPGQKG GRGSPGMDGF QGMVGLKGRP GLPGNKGEAG FFGIPGLKGL
AGEPGVKGSR GDPGPPGPPP IIQPGMKDIK GEKGDEGPMG LKGYLGLKGL PGMPGIPGLS
GVPGLPGKPG HIKGVKGDIG VPGMPGLPGF PGVPGPPGII GFPGFTGSRG DKGAPGRAGL
YGEVGPTGDF GDSGDIINLP GSPGLKGERG IAGAPGLKGF FGEKGTEGEV GFPGITGVPG
VQGPPGPKGQ TGFPGLTGLQ GPQGDPGRAG VPGDKGDYGW PGIPGSPGFP GIRGISGLHG
LPGTKGLPGS PGADIHGDPG FPGPAGDRGD PGEANIRPGP IGAPGQKGER GDPGGRGPTG
SPGLQGFPGI TPPSNVSGLP GDKGAPGIFG LEGYRGPPGP PGPAALPGSK GDEGNPGAPG
TPGTKGWGGD PGPQGRPGVF GLPGEKGPRG EPGFMGNTGA TGSVGDRGPK GPKGDRGLPG
APGSVGSPGI AGIPQKITIQ PGPVGPQGRR GPPGMQGEMG PQGPPGDPGF RGAPGKAGPQ
GRGGVSAVPG FRGDQGPMGH QGPVGQEGEP GRPGTPGLPG MPGRSVSIGY LLVKHSQTDQ
EPMCPVGMNK LWSGYSLLYF EGQEKAHNQD LGLAGSCLAR FSTMPFLYCN PGDVCYYASR
NDKSYWLSTT APLPMMPVAE DDIKPYISRC SVCEAPAVAI AVHSQDVSIP HCPAGWRSLW
IGYSFLMHTA AGDEGGGQSL VSPGSCLEDF RATPFIECNG GRGTCHYYAN KYSFWLTTIP
EQSFQGSPSA DTLKAGLIRT HISRCQVCMK NL
//