ID A0AAQ4S9V0_GASAC Unreviewed; 1492 AA.
AC A0AAQ4S9V0;
DT 02-OCT-2024, integrated into UniProtKB/TrEMBL.
DT 02-OCT-2024, sequence version 1.
DT 28-JAN-2026, entry version 7.
DE RecName: Full=FZ domain-containing protein {ECO:0000259|PROSITE:PS50038};
OS Gasterosteus aculeatus aculeatus (three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=481459 {ECO:0000313|Ensembl:ENSGACP00000071511.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000071511.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lake Benthic {ECO:0000313|Ensembl:ENSGACP00000071511.1,
RC ECO:0000313|Proteomes:UP000007635};
RX PubMed=33598708;
RA Nath S., Shaw D.E., White M.A.;
RT "Improved contiguity of the threespine stickleback genome using long-read
RT sequencing.";
RL G3 (Bethesda) 11:0-0(2021).
RN [2] {ECO:0000313|Ensembl:ENSGACP00000071511.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSGACP00000071511.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR Ensembl; ENSGACT00000056086.1; ENSGACP00000071511.1; ENSGACG00000015036.2.
DR GeneTree; ENSGT00940000165423; -.
DR Proteomes; UP000007635; Chromosome I.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR FunFam; 3.40.1620.70:FF:000003; Collagen type XVIII alpha 1; 1.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF906; COLLAGEN ALPHA-2(IX) CHAIN; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1492
FT /note="FZ domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5042926072"
FT DOMAIN 218..330
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 30..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..1307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..76
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..119
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..633
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..708
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..766
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..802
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..904
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..926
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1026
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1129
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1159
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1167..1182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1200..1219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1234
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1278
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1492
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 233..279
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1492 AA; 150271 MW; D1D5666D0204B1D3 CRC64;
MLRIQVLLPL LVLCARSLDA WWWIPDTTKA PALTTPANGT TPANGTTPAN GTTPSKGTPS
KGTPPNGTTP ANGTTPSKGT PPHGTAPLNC TAPLNGTTSP NGTTSPNGTT PLNGTTPLNA
PLAKDEEDDD LSGLGEEIVN VATGIRKFVE TWDATPAART DDGGMTEEVE RVAANTTGNT
RRFGEERVGG GVEGSDVEVL ALNLTRITVD PLTPPDNSSD QSCHPVPSDW PICSVGRPQF
FALPNFLNHA AAEEVGAVLQ EWAWLAAARC HHSAEWFLCL LLAPGCPQPA GPPPCRSFCQ
VLQDSCWASL EGGRLPVDCH LLPERACASV SNQKEESGVS LLQLIGDPLP EEVTRSYMPN
GESAYVFTSA AVSGQPAVAH VPNPFHRHFS LLFHVKPSTP AAAVLFSITD GPQRIMYIAV
KLGAVRSGRQ RVQLFYTEPD AEASYEAASF EVPSMVGAWN RFSLAVYEEQ VTFYYGCDSV
PQVLKFERSP DPMELDAGAG IFVGQAGGAD GDKFQGEIAD LKLVGNHLAA ERLCDNEDDS
DAASGDWSGS GEGDGTPAVT AVKTSATFSR PLPEPPLISS DGPENKERGS KGDKGDRGAT
GLAGDSGPAG PKGDSGSDSS GSSSGSSGSS SQGGERGQKG EKGAKGNSGF GYSGNKGERG
AQGPPGRTGP PGPSAEVLRL GNGSVVQQGS RLPGPPGPAG SDGAAGPPGE DGEPGDPGED
GKAGPSGPPG FPGTTGASGA KGQKGDLGEG QPGPRGPPGL PGPPGPGTGD NPFIDMEGSG
FPDSYKRGAL GPPGPPGPPG PPGVSVALGP DGPISFGPPG PPGQDGAPGL PGPPGPPGRI
GQPGPAGGKG DSGDLGLPGA AGEKQTSQGS NFFTDLFSYF APSSTGAQGD LGLPGASGQG
GLAGLPGPMG PVGPPGPPGP PGPPPRFGYG YQDGDGTNNG SPGIAGPPGP QGPAGVPGLP
GRPGFPGNHG DKGSEGPAGP RGIPGLDGFP GQPGEKGNSG QQGEPGLPGR DGGLPGPPGP
PGPPGQVPYQ TSDGGIGFPG RPGFPGPSGP KGDKGDVGPS GYATKGQKGE PGIITDSDGR
PQYIGGQAGR PGDRGPAGPE GPRGPPGPSG HKGEIGLPGR PGRPGLNGVR GEKGDSHSGY
GSGIAGPPGP PGPPGPPGGS SPTLSGYDHR FHPGTKGEKG DRGTPGTPGG GSTFGLTSTI
RDELKGVRGD PGFKGEKGEP GGGYYGGSGV GVPGVPGPPG PRGDSIVGPS GPQGPPGQPG
RGYDGPPGPP GPPGPPGESS PGTQRGTQTI NIPGPPGPPG VPGHSSGVTV MRSYDTMTAT
ARRQPEGSLV YVIEQTDLYI RVRDGVRQVQ LGGYIAFPSE DGNEVAAVEP PPVIPYFTDH
HPSNPAHDAV PIPESPVPRY PSNPDPRYPS NPDPRYPSNP DPRYPSNPDP RYPSNPDPRY
PSNPDPQYPS NPDPQYPSNP DPQYPSNPDP RYPSNPDPQY PSNPDPRYPS NP
//