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Database: UniProt
Entry: A0A3B4BSF4_PYGNA
LinkDB: A0A3B4BSF4_PYGNA
Original site: A0A3B4BSF4_PYGNA 
ID   A0A3B4BSF4_PYGNA        Unreviewed;      1457 AA.
AC   A0A3B4BSF4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Collagen type IV alpha 1 chain {ECO:0000313|Ensembl:ENSPNAP00000002578.1};
GN   Name=COL4A1 {ECO:0000313|Ensembl:ENSPNAP00000002578.1};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000002578.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000002578.1}
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; 42514.ENSPNAP00000002578; -.
DR   Ensembl; ENSPNAT00000010184.1; ENSPNAP00000002578.1; ENSPNAG00000009000.1.
DR   GeneTree; ENSGT00940000157678; -.
DR   OMA; MIPPCPQ; -.
DR   Proteomes; UP000261440; 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:SF1019; COLLAGEN; 1.
DR   PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR   Pfam; PF01413; C4; 2.
DR   Pfam; PF01391; Collagen; 9.
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   Secreted {ECO:0000256|ARBA:ARBA00022530}.
FT   DOMAIN          1234..1457
FT                   /note="Collagen IV NC1"
FT                   /evidence="ECO:0000259|PROSITE:PS51403"
FT   REGION          1..1101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1183..1229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..157
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..261
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..309
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..464
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        541..555
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        639..662
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        776..792
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1200..1223
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1457 AA;  142013 MW;  B70901A40749E73E CRC64;
     RGFPGLQGNM GFPGMQGHEG PPGPMGPKGD LGEPGAPGIK GARGPPGAAG FPGNPGLPGL
     PGQDGPPGPS GIPGCNGTKG ERGIDGISGL PGLQGPPGDP GGFIGGILPQ KGEKGFQGQP
     GLPGSPGNPG PQGLLGPPGP PGLKGYAGPP GPPGPPGTLM FMGAKGDKCS VYDAGIKGEP
     GPPGPPGKAG KDGQDGAEGG KGDPGFPGHN GLKGDKGERG PPGYGDGAPG PPGPPGFPGP
     QGERYPGQPG DPGPPRHLEG PPGERGFPGE IGQKGDKGVD GEPLRGPPGA DGAAGPPGPP
     GPLPPGPPGL QGEIGQKDQG DTCTQCSAFG PPGLPGAPGP KGQQFPGPAG SKGEKGQPGP
     VGVPGDPGSD GSPGLMGAPG AQGAPGDIYL APHLKGEKGL SGLPGSRGLP GINGLPGKDG
     RPGQPGPKGE PARVGIKGER GPDGDPGTPG PPGERGPPGL PGIGRPGEPG EKGSPGQPGV
     PGRQGIPPKG DPGKGVSSPG PQGPPGPRGE SGIPGLQERG PPGDQGLPGF PGLKGDPGLP
     GIGLPGPPGP KYSGIPGAPG LPGEPGRPGQ DGIPGIPGTA GQKGEPAIGL RGPKGSIGQP
     GVPGFPGEKG NVGMPGVPGT EGHTGPPGAQ ERGPPGAHGL AGPPGPPGPG EPGLPGPMGP
     TGKPGPFQIG EKGEKGLPGL PGPAMPGPKG EKGTPGLPGF PGPKGLPGET GHPGQDGMPG
     ERPKGEMGIM GAPGSPGFQD PGFTGPRGEF GEPGPKGERG EQGERGPPGN MTEVDMENMK
     GEKGDTGDRD PGPTGDRGYP GADGDPGMPG KDGMPGTPGQ PVGGPKGSKG TSGTPGHHGF
     KGTEGPKGDK GVAGLPGIGI PGLPGEKGEI GQPGFPGESG QKGVKGAMGI PGSPGSPGPK
     GDIGPISPGV PGEKGVVGLP GSPGESGFPG RPEPGLQGPP GPHGEKGDPG IDGIPGSSGE
     RGDPVPGRGF PGTPGQLGIK DRGNPGLPGT PGIPGIPGTK GEKGLPGLEG IQGQPGERGL
     PGPSMQGPKG DRGAPGEPGE PQIGAPGPTG VPGSPGVKGE RGNQGFTGPQ GTQGLKGDKG
     FTGLPGEPGL PGYNGPKGEM GIQGVPGFPI KGELGHVGVK GEAGDRGFPG VKNEGPPGTP
     GTNTFIKGDI GFPGPQGPAG LPGAQGYPGA KGQQLMGIQG IKGEDGEPGY NGLPGAKGEP
     GPVGPAPRGY PGPPGPDGIP GQVGPPGPSS MDHGFLVTRH SQSVDVPLCP QGTTLIYDGY
     SLLYVQGNER SHGQDLTAGS CLRKFSPMPF LFCNINNVCN FASRNDYSYW LTSPEPMPMS
     MAPVTGDSIK PFISCAVCEA PAMVIAVHSQ TVAIPPCPHG WISLWIGYSF VMQHTSAGAE
     GSGQALASPG SCLEEFRSAP FIECHGRGTC NYYANSYSFW LATIEDEEMF RKPVPTTLKA
     GNLRTHISRC QVCMKRT
//
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