ID H2STS1_TAKRU Unreviewed; 1159 AA.
AC H2STS1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Collagen type IV alpha 1 chain {ECO:0000313|Ensembl:ENSTRUP00000015808.3};
GN Name=COL4A1 {ECO:0000313|Ensembl:ENSTRUP00000015808.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000015808.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000015808.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000015808.3}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; H2STS1; -.
DR STRING; 31033.ENSTRUP00000080847; -.
DR Ensembl; ENSTRUT00000015878.3; ENSTRUP00000015808.3; ENSTRUG00000006458.3.
DR GeneTree; ENSGT00940000157678; -.
DR Proteomes; UP000005226; Chromosome 1.
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:SF854; COLLAGEN ALPHA-1(IV) CHAIN; 1.
DR Pfam; PF01413; C4; 2.
DR Pfam; PF01391; Collagen; 8.
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:UP000005226};
KW Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT DOMAIN 935..1159
FT /note="Collagen IV NC1"
FT /evidence="ECO:0000259|PROSITE:PS51403"
FT REGION 1..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..401
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..924
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1159 AA; 115945 MW; EE60A25C4DB56987 CRC64;
MTRPNALSCV MSGRHLEGAR GERGLKGDQG EKGDMGIEGE SLFGPPGQPG IPGLPGPPGE
PIDPNECDVG TGAPGPPGPP GLQGELGQKG DKGDTCFQCE SSGLPGLPGP QGPKGDHGPP
GSGFPGSPGL LGAPGPVGEP GDIFVAPGLK GDKGLTGVPG SPGMPGIKGE PGRTGIPGIP
GLKGESAKEG IKGERGPSGD PGTIGPPGER GPPGLPGFGR PGEHGDKGSQ GRSGSPGIPG
PPGAKGEPGQ GVGSPGPQGV PGPQGEPGRP GVQGERGLPG DAGIPGFPGQ KGEIGPSGIG
LPGLTGPKGI SGIPGDGEPG QGLPGPKGSQ GIPGLTGFPG EKGSIGLPGI PGQDGHAGPP
GPQGVKGEVG PPGPPGLNGL QGPPGKGTPG LPGPQGPPGE PGPFGREGVK GERGYQGPPG
LDIPGPKGDK GAPGFPGVSG TKGLPGVEGL QGRDGLIGTQ GPKGEMGVIG TPGVPGFPGL
PGQPGSPGWR GDPGVTGPRG AIGESGIKGE RGDPGLQGPA GNMSDVDMEH MKGEKGDIGV
LGEPGFTGQK GTRGMPGDPG QRGTDGEPGL PGQPERRLWF SWRAWQHGTT WTERRSWRDG
ITRSDHTTSK TLHVGKSSVK LLVLVSLCTG TMGPKGTKGN FGTPGFPGLP GEKGVRGFEG
MPGKPGLEGI KGDKGSIGYT GQNSASLSFI LLLYLSQPGR PGEKGVPGLP GPAGERGVDG
QPGKCSQENC LIHTCLSGEA GLQGPPGSPG QKGEAGVDGI PGSSGERGDP GEKGSPGLHG
TPGHPGVPGT KGDKGLPGTP GPRGDLGERG LPGVSLEGPK GDRGETGQPG EIGTLSSCCQ
PAVKFKHLSS IHHYVCLPQT GSQGLPGPPG LQGRDGLKGD KGEQGNPGFQ GELGQKGETG
GNDGPPGPRG YPGPTGPDGV PGQVGPPGPS SMDHGFLVTR HSQTVDVPQC PEGTSLIFDG
YSLLYVQGNE RSHGQDLGTA GSCLRKFSPM PFLFCNINNV CNFASRNDYS YWLTSPEPMP
MSMAPITGHS IKPFISRCAV CEAPAMVIAV HSQTIMIPPC PYGWDSLWIG YSFVMHTSAG
AEGSGQALAS PGSCLEEFRS APFIECHGRG TCNYYANSYS FWLATIEDSD MFTKPVPTTL
KAGNLRTHIS RCQVCMKRT
//
