ID A0A3B4D254_PYGNA Unreviewed; 1225 AA.
AC A0A3B4D254;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Tight junction protein ZO-2-like {ECO:0000313|Ensembl:ENSPNAP00000017156.1};
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:ENSPNAP00000017156.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000017156.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000256|ARBA:ARBA00004435}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004413}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
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DR RefSeq; XP_017571617.1; XM_017716128.1.
DR AlphaFoldDB; A0A3B4D254; -.
DR STRING; 42514.ENSPNAP00000017156; -.
DR Ensembl; ENSPNAT00000025890.1; ENSPNAP00000017156.1; ENSPNAG00000023382.1.
DR GeneTree; ENSGT00940000158634; -.
DR OMA; MPNSNRS; -.
DR OrthoDB; 2904077at2759; -.
DR Proteomes; UP000261440; Unplaced.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR CDD; cd00992; PDZ_signaling; 3.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR005417; ZO.
DR InterPro; IPR005419; ZO-2.
DR PANTHER; PTHR13865; TIGHT JUNCTION PROTEIN; 1.
DR PANTHER; PTHR13865:SF26; TIGHT JUNCTION PROTEIN ZO-2; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR01597; ZONOCCLUDNS.
DR PRINTS; PR01599; ZONOCCLUDNS2.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 3.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 3.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 3.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 32..119
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 307..385
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 504..585
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 599..667
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 771..873
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 121..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1155..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1057
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1186
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1225 AA; 137027 MW; BC759D8020FFA319 CRC64;
MPVRGGGRAA YASKLGSAGS SGMEETVWEQ YTVTLQRDAK MGFGIAVSGG RDNPNVDTGE
TSIIVSDVLQ GGPADGLLYE NDRVIQVNTI PMENVPHSFA VQQLRKCGKV AKITVKRPRK
VAVLKRPPSP DRDSRDYNLS SYYPEDNRST HSDPDSDYPR GNGGLGYPRE RDRSQDKGRM
GYLEPDYRRP DYDPGRRERS RGRSLERSPS PDRGYRRDGS RGRTLERGAS PDSHYHRQRS
RGGAESPAGS YGRDPGPGFD SRKYETRSDD RMMRSHSRDR LQEHSPSPSR GRGKDWGHLE
PLDTPINVLL VKNRPNEEYG LRLGSQIFIK EMTSSGLASR DGNLQEGDII LKINGTVTEN
LSLSDAGKLI EKSRGKLQLV VQRDNRQILV RIPALADSDS EPDDVSEMES YHSYSPQEDQ
RSRQSDLSSH SSNEVPRENV REDPQSRLPK MAATSSPYRL TEELAEAQED HTEPRPEEPP
AAVKTTPKIL LRPSPEDEQM YGPNTMMVSF QKGESVGLRL AGGNDAGIFV AGVQEGSPAE
EEGLRVGDQI MKVNNVDFRG IVREEAVLFL LELPRGENIT ILAQSKPDVY EDVLVSGRGD
SFFIRTHFDY EKEQPQCLAF SRGDIFKVVD TLYDGKLGNW LAIRVGKENQ LLEKGIIPNK
SRADQMTNVQ HTHKGSSGDR ADFWRLRGQR ASKKKDLRKN REDLSTGLVS TRFPAYERVV
LREAGFRRPV VLFGPIADAA IEKLATELPE EFVVAKTEPK DAGSEKSSGV VRLNTIRQII
EQDKHALLDV TPKAVDTLNY TQWYPIVIFF NPDSKHGVKN MRQRVMPNSN RSARKLYDQA
IKLRKSCSHL FTAVIDLNAA NDAWYGSVKE CIRQQQTQAV WVSEGKLDGT EGDLDLHDDR
MSYLSAMSAD YLSMDSRVTS DYDDTADEGG AYTDNELDEP LERQRVSAIS RSSEPVMPEE
ILRKSSPENR FHSHVGAVNR ELLSEGSPPV MSTFLPDPSK VKLLAQSEAS RGRYDPSRVY
DPHSMNPTSN PAMKPSSNPA IILTSNLPSN PVSHEPLRTH DSPSKPMPPP IALKPSSVSR
VSRGQADSPP LRDHEPPGNS PEDPSQKSFL GKVRAFEKMD HFARAQRMLE LQEAQNARLE
IAQKHPDIYA VPIKAQKLDH SRPQPIGSSS RPEPQTPPPK PPYLESYSPC PDKEEGAEEE
YRQRLADQTK RGYYPDAHKY QDTEL
//
