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Database: UniProt
Entry: A0A2U3VQU3_ODORO
LinkDB: A0A2U3VQU3_ODORO
Original site: A0A2U3VQU3_ODORO 
ID   A0A2U3VQU3_ODORO        Unreviewed;      1230 AA.
AC   A0A2U3VQU3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Tight junction protein ZO-2 isoform X2 {ECO:0000313|RefSeq:XP_004397587.1};
GN   Name=TJP2 {ECO:0000313|RefSeq:XP_004397587.1};
OS   Odobenus rosmarus divergens (Pacific walrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC   Odobenus.
OX   NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004397587.1};
RN   [1] {ECO:0000313|RefSeq:XP_004397587.1}
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_004397587.1; XM_004397530.1.
DR   AlphaFoldDB; A0A2U3VQU3; -.
DR   GeneID; 101372161; -.
DR   CTD; 9414; -.
DR   OrthoDB; 2904077at2759; -.
DR   Proteomes; UP000245340; 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   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   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:UP000245340};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT   DOMAIN          65..152
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          347..425
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          549..630
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          644..709
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          814..916
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          177..346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          447..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          512..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          960..1124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1156..1230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..304
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..340
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        967..981
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        996..1021
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1037..1052
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1053..1069
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1197..1212
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1230 AA;  138019 MW;  AB0B7335375F519E CRC64;
     MKTAQVLQRM WIQAVKKLGR LKGHVSPSAS SPPFLSQLFF WCEGQGEKTT LSAPGMEELI
     WEQYTVTLQK DSKRGFGIAV SGGRDNPHFE NGETSIVISD VLPGGPADGL LQENDRVVMV
     NGTPMEDVLH SFAVQQLRKS GKIAAIVVKR PRKVQLAPPQ DSPPVDEDDR AFEVMDEFDG
     RSARSGYSER SGRGSHGGRS RSWADSPERG RPHERAQSRE RERSRGRSLE RGLDADNYGR
     ARERSRGRSL ERGLDHDDCG RARERSRGRS TDRAYDQYDQ AYDRGYDDAY DRTYSPEAEY
     GHRAQPDARY SAPRSRSREH LHSRSPSPEL RRRPDHAGPP DSDRPIGVLL MKSKANEEYG
     LRLGSQIFIK EMTRTGLATK DGNLHEGDII LKINGTVTEN MSLTDARKLI EKSRGKLQLV
     VLRDSKQTLI NIPSLDDSDS EIEDISEIES NRSFSPEERR QQYSDYDYHS SNEKLKERPN
     SREDMQNRWS RMGATPTPFK STGDIAAAVG TENSKEPRYQ EEPPAPQPKA ASRTFLRPSP
     EDEAIYGPNT KMVRFKKGDS VGLRLAGGND VGIFVAGIQE GTSAEQEGLQ EGDQILKVNT
     QDFRGLVRED AVLYLLEIPK GEMVTILAQS RADVYRDILA CGRGDSFFIR SHFECEKETP
     QSLAFTRGEV FRVVDTLYDG KLGHWLAVRI GNELEKGLIP NKSRAEQMAS VQNAQRDNAG
     DRADFWRMRG QRSGVKKNLR KSREDLTAVV SVSTKFPAYE RVLLREAGFK RPVVLFGPIA
     DIALEKLANE LPDLFQTAKT EPKDAGSEKS SGVVRLNTVR QIIEQDKHAL LDVTPKAVDL
     LNYTQWFPIV IFFNPDSRQG VKTLRQRLNP TSNKSSRKLY DQANKLKKTC AHLFTATINL
     NSANDSWFGS LKDIIQHQQG EAVWVSEGKM EGMDDDPEDR MSYLTAMGAD YLSCDSRLIS
     DFEDTDGEGG AYTDNELDEP AEEPLVSSIT RSSEPVQHEE SIRKPSPEPR AQMRRAASRD
     QLRDSSPPPA FKPEPPKAKT QNREDSFDFS RSHEYKSNPS ATAGNEVSGA STKGYPPPVA
     AKPAFGRSIL KPSTPVPPPE SEEVGEGSEE QEGTPKSVLG KVKIFEKMDH KARLQRMQEL
     QEAQNARIEI AQKHPDIYAV PIKTHKPDPG LSQHTSSRPP EPQKGPSRLY QDPRGSYSSD
     AEEEEYRQQL SEHSKRGYYS QPSRYRDTEL
//
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