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
//