ID I3JA88_ORENI Unreviewed; 1065 AA.
AC I3JA88;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=FZ domain-containing protein {ECO:0000259|PROSITE:PS50038};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000005778.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Ensembl:ENSONIP00000005778.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) 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 AlphaFoldDB; I3JA88; -.
DR Ensembl; ENSONIT00000005782.2; ENSONIP00000005778.2; ENSONIG00000004587.2.
DR eggNOG; KOG3546; Eukaryota.
DR GeneTree; ENSGT00940000165423; -.
DR HOGENOM; CLU_004003_1_0_1; -.
DR InParanoid; I3JA88; -.
DR OMA; GTKQTNI; -.
DR TreeFam; TF315821; -.
DR Proteomes; UP000005207; Unplaced.
DR CDD; cd00247; Endostatin-like; 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; 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:SF533; COLLAGEN ALPHA-6(IV) CHAIN; 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 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1065
FT /note="FZ domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025588238"
FT DOMAIN 124..243
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT REGION 446..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..486
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..516
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..699
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..724
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 139..185
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 176..214
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 1065 AA; 114937 MW; 241A97A997A844BF CRC64;
MVMMRIQFGL VVLLAQWVVC SDAWLWSWTD TTTSAPAVDP EGSGSPAGSG EPLSETIAKI
GEEIIDEGHQ MEKAVQKTGH IPDATQSTIS EKKLNQATLF SQTVAVSEPT TIKQPEAGRP
ALDAESPQCL LLDTALPFCS SMAGQRFVVP NYFNQSSVEE IQALLNEWAW LLNSQCHHSV
EWFFCLLLVP KCGSLAPLPV LPCQSFCEVL RDSCWTLLDE GHLPVECHTL PDEEDDGYQC
LSVSNQKEDS GVSLLQLIGD PPPSEITQIY GPDNTPSFVF GPDANTGQLA RAHLPNPFYR
DFSLIFNLKP TTNQGGVIFS ITDARQSIMH VGVKLSAVQN NNQNVILYYT KPKSARSFEA
ARFLVTSMTD TWTRFSLAVM DNKVLFYFNC DTDPQVVHIE RSTEDMELES GAGVFVGQAG
GADPDKFLGV IGELRVVGDP FAANRHCEED EDDSDMGSAG FGNKGVKGEP GPPGPPGPPG
PPGPAPEHTV GSDGSVSRVP GPRGPPGAPG PQGPPGADGE PVSQLKIICL LENTKHKCAV
TVQPTLLYLS WFACLHKQKD KNHTIFQVQQ KTNKSITFSL QGRPGINGYK GEKGEPGVGS
GLGYPVSINT IINTLNELKG ERGEPGVKGE KGEPGGGYYD PRFGGVQGPP GPPGLPGPKG
DSIIGPPGPS GPTGPPGIGY DGRPGPPGPP GPPGPPGSLS GSYRPNYPVS IPGPAGPPGP
PGAPGLSSGV TVLRSYDTMI ATARRQEEGS LIYIIDRADL YLRVRDGVRQ VMLGEYNPFF
RELENEVAEV QPPPVILYPE SQDQSQNNGA GHYSEGFTLI KPIEPPAPTP ADPRYFPKYE
PRFPDQTHTG HTDGRFATQQ TESRFPVTPQ RQPVPPVLEP AGRFDVHGSG LHLIALNSPH
TGNMRGIRGA DFLCFQQARA VGLKGTFRAF LSSKLQDLYT IVRRSDRDSI PIVNLKNQVL
FSSWDSLFGD NVSTMRENVP IYSFDGRDIL RDSAWPEKMV WHGSSKKGHR QTDQYCETWR
IGDHAVTGLA SSLHSGHLLQ QTPSSCSSSY IVLCIENAFT SPSKK
//
