ID I2CXW8_MACMU Unreviewed; 1188 AA.
AC I2CXW8;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Tight junction protein ZO-2 isoform 1 {ECO:0000313|EMBL:AFJ71803.1};
GN Name=TJP2 {ECO:0000313|EMBL:AFJ71803.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFJ71803.1};
RN [1] {ECO:0000313|EMBL:AFJ71803.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Orbital {ECO:0000313|EMBL:AFJ71803.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
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 EMBL; JV636463; AFJ71803.1; -; mRNA.
DR AlphaFoldDB; I2CXW8; -.
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 CDD; cd12027; SH3_ZO-2; 1.
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 InterPro; IPR035598; ZO-2_SH3.
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 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 2: Evidence at transcript level;
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 33..120
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 305..383
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 507..588
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 602..667
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 688..874
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 152..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 405..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..939
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1009
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1010..1025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1155..1170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1188 AA; 133671 MW; B61950743F19E79B CRC64;
MPVRGDRGFP PRRELSGWLR APGMEELIWE QYTVTLQKDS KRGFGIAVSG GRDNPHFENG
ETSIVISDVL PGGPADGLLQ ENDRVVMVNG TPMEDVLHSF AVQQLRKSGK IAAIVVKRPR
KVQVAPLQAS PPLDQDDRAF EVMDEFDGRS FRSGYSERSR LSSHGGRSRS WEDSPERGRP
HERARSRERD LSRDRSRGRS LERGLDQDHG RARDRSRGRS LERGLDHDFG PSRDRDRSRG
RSIDQDYERA YHQAYDPDYE RAYSPEYRRG ARHDARSRGP RSRSREHPRS RSPSPEPRGR
PGPIGVLLTK SRANEEYGLR LGSQIFIKEM TRTGLATKDG NLHEGDIILK INGTVTENMS
LTDARKLIEK SRGKLQLVVL RDSQQTLINI PSLNDSDSEI EDISEIESNR SFSPEERRQQ
YSDYDYHSSS EKLKERPSSR EDTPSRLSRM GATPTPFKST GDIAGTIVPE TNKEPRYQED
PPAPQPKAAP RTFLRPSPED EAIYGPNTKM VRFKKGDSVG LRLAGGNDVG IFVAGIQEGT
SAEQEGLQEG DQILKVNTQD FRGLVREDAV LYLLEIPKGE MVTILAQSRA DVYRDILACG
RGDSFFIRSH FECEKETPQS LAFTRGEVFR VVDTLYDGKL GHWLAVRIGN ELEKGLIPNK
SRAEQMASVQ NAQRDNAGDR ADFWRMRGQR SGVKKNLRKS REDLTAVVSV STKFPAYERV
LLREAGFKRP VVLFGPIADI AMEKLANELP DWFQTAKTEP KDAGSEKSTG VVRLNTVRQI
IEQDKHALLD VTPKAVDLLN YTQWFPIVIF FNPDSRQGVK TMRQRLNPAS NKSSRKLFDQ
ANKLKKTCAH LFTATINLNS ANDSWFGSLK DTIQHQQGEA VWVSEGKMEG MDDDPEDRMS
YLTAMGADYL SCDSRLISDF EDTDGEGGAY TDNELDEPAE EPLVSSITRS SEPVQHEESI
RKPSPEPRAQ MRRAASSDQL RDNSPPPAFK PEPPKAKTQN KEESYDFSKS YEYKSNPSAI
AGNETPAAST KGYPPPVAAK PAFGRSILKP STPIPPQEGE EVGESSEEQD NAPKSVLGKV
KIFEKMDHKA RLQRMQELQE AQNARIEIAQ KHPDIYAVPI KSHKPDPSLP QHTSSRPPEP
QKAPSRLYQD TRGSYGSDAE EEEYRQQLSE HSKRGYYGQS ARYRDTEL
//
