ID A0A2Y9DQU3_TRIMA Unreviewed; 918 AA.
AC A0A2Y9DQU3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Tight junction protein ZO-3 {ECO:0000313|RefSeq:XP_004378526.1};
GN Name=LOC101342844 {ECO:0000313|RefSeq:XP_004378526.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004378526.1};
RN [1] {ECO:0000313|RefSeq:XP_004378526.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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_004378526.1; XM_004378469.1.
DR AlphaFoldDB; A0A2Y9DQU3; -.
DR STRING; 127582.A0A2Y9DQU3; -.
DR GeneID; 101342844; -.
DR KEGG; tmu:101342844; -.
DR InParanoid; A0A2Y9DQU3; -.
DR OrthoDB; 2904077at2759; -.
DR Proteomes; UP000248480; 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; IPR005420; ZO-3.
DR PANTHER; PTHR13865; TIGHT JUNCTION PROTEIN; 1.
DR PANTHER; PTHR13865:SF11; TIGHT JUNCTION PROTEIN ZO-3; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR01597; ZONOCCLUDNS.
DR PRINTS; PR01600; ZONOCCLUDNS3.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 3.
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.
PE 4: Predicted;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000248480};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 20..100
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 202..279
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 387..453
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 668..768
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 103..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..137
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 918 AA; 100909 MW; C14BAA8264C6957E CRC64;
MAVRFQVTDM EELTIWEQHT ATLSKDPRRG FGVAISGDRS SGSVVVSDVL PGGPAEGRLQ
IGDHIVMVNG VSMESVTSAF AIQILKTCSK LANITVKRSR KIQLPATKAG PSSPGHQDSD
EEDGPRQLED ADHGRGYEGD SSSGSGRSWG ERSRRPRAGR RSRAGSHGRR SPGGGSEANG
LALVSGFKRL PRQDVLMRPV KSVLVRQRES EEFGVKLGSQ IFIKHITDSG LAARNRGLQE
GDLILQINGV SSENLSLSDT RRLIEKSEGK LTLLVLRDRG QFLVNIPPAV SDSDSSLLED
ISDLGSELSQ APPSHIPPPP QHAQQSADTS RTASPVERSQ LQQERSVDSR SVSEPGEGWA
DSPPESSYDI YRVPSDQSME DHGYSPDVRV VHFTKGASLG LRLAGGNDVG IFVSGVQAGS
PADGQGIQEG DQILQANDTS FQNLTREEAV QFLLGLPPGE EVELVTQRKQ DIFRKMVQSR
VGDSFYIRTH FEMEPSPPSG LGFTRGDVFH VVDTLYPGPG QSHTRRGHWL AARMGRDLRE
QERGVIPNQS RAEQLASLEA AQRAVGAGPG SLANSNARAE FWRLRGLRRG AKRTTHQSRE
DLSALTKQGH YPPYERVVLR EASFKRPVVI LGPVADIAMQ KLTAEMPDQF EIAESMLRTD
TPSKIIKLDT VRVIAEKDKH ALLDVTPSAV ERLNYVQYYP IVVFCAPESR STLKALRQWL
APASRRSSRR LYAQAQKLQK HSSHIFTATI PLHGTSDAWY QELKAIICEQ QTRPIWTAED
QLDSSSDDNL DLPLRALADS SADLSCDSRA NSDYETDGEG YTDGEGGPCT DVDEEPPARA
LARSSEPVLA DEPQNPQDHG RSVAHRGIQV DSWHSKGQWR QDSMRTYERE ALKKKFTRAR
DMESSDEDGY DWGPATDL
//
