GenomeNet

Database: UniProt
Entry: A0A2I3LNW4_PAPAN
LinkDB: A0A2I3LNW4_PAPAN
Original site: A0A2I3LNW4_PAPAN 
ID   A0A2I3LNW4_PAPAN        Unreviewed;      1247 AA.
AC   A0A2I3LNW4;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Tight junction protein 2 {ECO:0000313|Ensembl:ENSPANP00000025112.2};
GN   Name=TJP2 {ECO:0000313|Ensembl:ENSPANP00000025112.2};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000025112.2, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000025112.2, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000025112.2}
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   AlphaFoldDB; A0A2I3LNW4; -.
DR   Ensembl; ENSPANT00000051922.2; ENSPANP00000025112.2; ENSPANG00000025110.3.
DR   GeneTree; ENSGT00940000158634; -.
DR   OMA; RQRHSKI; -.
DR   OrthoDB; 2904077at2759; -.
DR   Proteomes; UP000028761; Chromosome 13.
DR   Bgee; ENSPANG00000025110; Expressed in thyroid gland and 67 other cell types or tissues.
DR   ExpressionAtlas; A0A2I3LNW4; baseline.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0044291; C:cell-cell contact zone; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:1990782; F:protein tyrosine kinase binding; IEA:Ensembl.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:Ensembl.
DR   GO; GO:0090557; P:establishment of endothelial intestinal barrier; IEA:Ensembl.
DR   GO; GO:0034109; P:homotypic cell-cell adhesion; IEA:Ensembl.
DR   GO; GO:0050892; P:intestinal absorption; IEA:Ensembl.
DR   GO; GO:1905605; P:positive regulation of blood-brain barrier permeability; IEA:Ensembl.
DR   GO; GO:0090559; P:regulation of membrane permeability; IEA:Ensembl.
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:UP000028761};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT   DOMAIN          92..179
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          364..442
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          566..647
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          661..726
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          747..933
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          211..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          464..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1007..1138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1162..1247
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..353
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..502
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1013..1027
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1054..1068
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1069..1084
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1214..1229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1247 AA;  140507 MW;  4A7E0D555BABDC03 CRC64;
     MRYKKYIGIL EAAVGITPLN KRELLPESRR HVNLWQQPGV RSTTLPSSPC EWDWYPGCSS
     RRKYSRKHRA VPVHGPRCQA PGMEELIWEQ YTVTLQKDSK RGFGIAVSGG RDNPHFENGE
     TSIVISDVLP GGPADGLLQE NDRVVMVNGT PMEDVLHSFA VQQLRKSGKI AAIVVKRPRK
     VQVAPLQASP PLDQDDRAFE VMDEFDGRSF RSGYSERSRL SSHGGRSRSW EDSPERGRPH
     ERARSRERDL SRDRSRGRSL ERGLDQDHGR ARDRSRGRSL ERGLDHDFGP SRDRDRSRGR
     SIDQDYERAY HQAYDPDYER AYSPEYRRGA RHDARSRGPR SRSREHPRSR SPSPEPRGRP
     GPIGVLLTKS RANEEYGLRL GSQIFIKEMT RTGLATKDGN LHEGDIILKI NGTVTENMSL
     TDARKLIEKS RGKLQLVVLR DSQQTLINIP SLNDSDSEIE DISEIESNRS FSPEERRQQY
     SDYDYHSSSE KLKERPSSRE DTPSRLSRMG ATPTPFKSTG DIAGTVVPET NKEPRYQEDP
     PAPQPKAAPR TFLRPSPEDE AIYGPNTKMV RFKKGDSVGL RLAGGNDVGI FVAGIQEGTS
     AEQEGLQEGD QILKVNTQDF RGLVREDAVL YLLEIPKGEM VTILAQSRAD VYRDILACGR
     GDSFFIRSHF ECEKETPQSL AFTRGEVFRV VDTLYDGKLG HWLAVRIGNE LEKGLIPNKS
     RAEQMASVQN AQRDNAGDRA DFWRMRGQRS GVKKNLRKSR EDLTAVVSVS TKFPAYERVL
     LREAGFKRPV VLFGPIADIA MEKLANELPD WFQTAKTEPK DAGSEKSTGV VRLNTVRQII
     EQDKHALLDV TPKAVDLLNY TQWFPIVIFF NPDSRQGVKT MRQRLNPASN KSSRKLFDQA
     NKLKKTCAHL FTATINLNSA NDSWFGSLKD TIQHQQGEAV WVSEGKMEGM DDDPEDRMSY
     LTAMGADYLS CDSRLISDFE DTDGEGGAYT DNELDEPAEE LLVSSITRSS EPVQHEESIR
     KPSPEPRAQM RRAASSDQLR DNSPPPAFKP EPPKAKTQNK EESYDFSKSY EYKSNPSAVA
     GNETPAASTK GYPPPVAAKP AFGRSILKPS TPIPPQEGEE VGESSEEQDN APKSVLGKVK
     IFEKMDHKAR LQRMQELQEA QNARIEIAQK HPDIYAVPIK SHKPDPSLPQ HTSSRPPEPQ
     KAPSRLYQDT RGSYGSDAEE EEYRQQLSEH SKRGYYGQSA RYRDTEL
//
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