ID A0A315WDJ7_GAMAF Unreviewed; 1566 AA.
AC A0A315WDJ7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 08-OCT-2025, entry version 23.
DE RecName: Full=FZ domain-containing protein {ECO:0000259|PROSITE:PS50038};
GN ORFNames=CCH79_00017225 {ECO:0000313|EMBL:PWA33807.1};
OS Gambusia affinis (Western mosquitofish) (Heterandria affinis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Gambusia.
OX NCBI_TaxID=33528 {ECO:0000313|EMBL:PWA33807.1, ECO:0000313|Proteomes:UP000250572};
RN [1] {ECO:0000313|EMBL:PWA33807.1, ECO:0000313|Proteomes:UP000250572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NE01/NJP1002.9 {ECO:0000313|EMBL:PWA33807.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PWA33807.1};
RX PubMed=29703783;
RA Hoffberg S.L., Troendle N.J., Glenn T.C., Mahmud O., Louha S., Chalopin D.,
RA Bennetzen J.L., Mauricio R.;
RT "A High-Quality Reference Genome for the Invasive Mosquitofish Gambusia
RT affinis Using a Chicago Library.";
RL G3 (Bethesda) 8:1855-1861(2018).
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- SIMILARITY: Belongs to the multiplexin collagen family.
CC {ECO:0000256|ARBA:ARBA00061275}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWA33807.1}.
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DR EMBL; NHOQ01000017; PWA33807.1; -; Genomic_DNA.
DR STRING; 33528.ENSGAFP00000000044; -.
DR Proteomes; UP000250572; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR FunFam; 3.10.100.10:FF:000008; collagen alpha-1(XVIII) chain isoform X1; 1.
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; 1.20.5.320; 6-Phosphogluconate Dehydrogenase, domain 3; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
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:SF1082; COLLAGEN TRIPLE HELIX REPEAT; 1.
DR Pfam; PF01391; Collagen; 1.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 1.
DR Pfam; PF01392; Fz; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR PROSITE; PS50038; FZ; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW Proteoglycan {ECO:0000256|ARBA:ARBA00022974};
KW Reference proteome {ECO:0000313|Proteomes:UP000250572};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1566
FT /note="FZ domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016429440"
FT DOMAIN 133..250
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 300..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1313..1382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..630
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..748
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..788
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..829
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..913
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..982
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..997
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1010
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1045..1054
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1104
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1118
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 138..199
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1566 AA; 167221 MW; 486630340DABD218 CRC64;
MSGIQMWSLL LVLCAGSLEA WWFSNNPQPT TGSTTTEGAT TPSGVLVTQG TKDGKISQVG
EEILKVATGI RQVIDDWDAT TTAWTTSGGL TGTTAKPNIT DEKGRLRGAR VEQGVGEGDR
FWSGSEVSSV DTTSTSPCFP VPSDWPICKQ PNVFSLPNFF NHTSVEEVDA VLREWVWLVR
TRCHRHTERF LCLLLAPRCP IPAAPLPSRG FCHVLQDSCW AFLENGRLPV DCHFLPETEQ
EYQSPGCAAV SSRKEKSGVF LHQLIGDPPP DSIAKGEIGE LRLVRDPQAF QDFCDYDGFP
DESSGDDGNR KADGKQTGKT VSSTSFRPVS KPTTSHQKGA GIKTSEKSGV FLHQLIGDSI
PKVSRPGGTA YKFTSASSSG KLAQDFVPSP FYRDFTIIFH LHASTPAASV LFSITDSAQK
LMYIGVKLSA VQSGRQKIQF FYTEPDSESS YEAASFDVPM LDVNWKPFAL SVHDEQVSFY
SECDGDPEVV KFERSPDPMD LDAGSMIFVG QAGRADPDKF EGEIVELKLV GDTQAFQSFC
DYEDYADEGS GDGGNGEADR RQKENTKTTT FPPLRPVAVP PISSQTETRK GASGGKGEKG
DRGEKGLKGD QGPAGPKGDS GSSSGSSFSS QGRKGVILVL DTLAKRVNVA FRGLLVLLVL
LDLQLRLSDL VTALLCSPWL VQLGHPGHQG RKGLKDLKGL MDSLVIQERM EKLVLLDRRV
FQEFQEQLGE SGEGSPGPRG PPGLPGSPGP GTGDRPTFVD MEGSGFPDLE TFRGPLGPPG
PPGPPGHPGT PGTSVAIGPD GPVAFGPPGP PGQDGVPGLP GPPGPPGLPG RPGLRGEKGD
GGDLGLPGPA GEKQDTTDSN PFNYFFSFFA PSSTGGQGDA GRTGTPGESG LAGLPGPMGP
VGPPGPPGPP GPPYLAGSGS QNEVLNALPG LRGPPGPQGP PGIAGLPGKP GFPGDHGAKG
AEGPRGPPGI PGIDGYPGTP GKQGEKGEKG ETGRPGRDGG PPGPPGPPGQ PGQILYQPSS
RDFNEVYWND LGQGPAGPKG DKGDAGAPGY APKGQKGEPG IIMGPDGRPL YLGGLTGQPG
RPGLNGVKGE KGDSGGGSGY GYPGIPGPPG PPGPPGPPGG YDEYSRYYAV KGEKGDPGPP
GILEIQGLGT GFDFYTLKER KENQAAVIMT PDMEEELAHL DHLDHKVQKE NQLLVHRALR
GLLDPQEQAM MVDLDHQAHR DLQVHLCLGP MEEHRPSVFL DPQDLLELQV FQDSLQQSYD
TMAATATRQP EGSLVYVIDQ MDLYVRVRNG VRQVQLGNYI ALPSELGVAA EASPPVIQPP
SQSNPDSDRP DSRYQIDLVY PQPSNPRYPS YTDRFNQPDN RYLDPRYSVT RPQRPPPPVP
QAPIHRHTSG PALHLIALNS PQRGDMRGIS GVDFLCFSQA QAIGMKGTFR AFLSSKLEDL
NSIVYSSNRE NVPIVNLKDE VLFDNWNRIF SDSRMRDNVS IYSFNGKDVL QDDTWPEKTM
WHGSTSRGQR NIDNYCEAWR VGERALTGMA SPLQSRSLLQ QSSSSCSSSY IVLCVENSYI
RDSRQR
//
