ID F1MBN2_BOVIN Unreviewed; 1174 AA.
AC F1MBN2;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Tight junction protein 2 {ECO:0000313|Ensembl:ENSBTAP00000015635.6};
GN Name=TJP2 {ECO:0000313|Ensembl:ENSBTAP00000015635.6,
GN ECO:0000313|VGNC:VGNC:35882};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000015635.6, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000015635.6, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000015635.6,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000015635.6}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000015635.6};
RG Ensembl;
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 AlphaFoldDB; F1MBN2; -.
DR iPTMnet; F1MBN2; -.
DR Ensembl; ENSBTAT00000015635.6; ENSBTAP00000015635.6; ENSBTAG00000011770.6.
DR VEuPathDB; HostDB:ENSBTAG00000011770; -.
DR VGNC; VGNC:35882; TJP2.
DR eggNOG; KOG3580; Eukaryota.
DR GeneTree; ENSGT00940000158634; -.
DR TreeFam; TF315957; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000011770; Expressed in retina and 102 other cell types or tissues.
DR ExpressionAtlas; F1MBN2; baseline and differential.
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 1: Evidence at protein level;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Proteomics identification {ECO:0007829|PeptideAtlas:F1MBN2};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
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 291..369
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 493..574
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 588..653
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 758..860
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 145..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1089..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..429
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..479
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..925
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..995
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1174 AA; 131610 MW; 3D9F059139D7A16C CRC64;
MPVRGDRGFP SRREMSGWLP APGMEELIWE QYTVTLQKDS KRGFGIAVSG GRDNPHFENG
ETSIVISDVL PGGPADGLLQ ENDRVVMVNG TPMEDVLHSF AVQQLRKSGK IAAIVVKRPR
KVQLAPLQDS PPVHEDDRAF EVMDEFDGRS ARSGYSERSR PSSRGGRSRS WEESPERGRP
HDRVRSRDRG RSLERGLDHD DDYGRAREHS RGRSLERGLD QDDYRRARES SRGRSIDPVY
DRAYTPEGEY GHRAQPDARY GASQSRSREH LHSRSPSPEP RGRPDSDKPI GVLLMKSKAN
EEYGLRLGSQ IFIKEMTRTG LATKDGNLHE GDIILKINGT VTENMSLTDA RKLIEKSRGK
LQLVVLRDSK QTLINIPSLN DSDSEIEDIS EIESNRSFSP EERQQQYSDY DYHSSNEKLK
ERPNSREDMQ SRWSRMGATP TPFKSTGDMA AAGSVEPSKE PKYQEEAPVP PPKPAPRAVL
RPSPEDLAIY GPNTKMVRFK KGDSVGLRLA GGNDVGIFVA GIQEGTSAEQ EGLQEGDQIL
KVNTQDFRGL VREDAVLYLL EIPKGETVTI LAQSRADVYR DILACGRGDS FFIRSHFECE
KETPQSLAFT RGEVFRVVDT LYDGKLGHWL AVRIGNELEK GLIPNKSRAE QMASVQNAQR
DTTGDRADFW RMRGQRSGVK KNLRKSREDL TAAVTVSTKF PAYERVLLRE AGFKRPVVLF
GPIADIALEK LANDLPDLFQ TAKTEPRDAG SEKSTGVVRL NTVRQIIEQD KHALLDVTPK
AVDLLNYTQW FPIVIFFNPD SRQGVKTMRQ RLNPSSNKSS RKLFDQANKL KKTCAHLFTA
TINLNSANDS WFGSLKDTIQ HQQGEAVWVS EGKMEGMDDD PEDRMSYLTA MGADYLSCDS
RLISDFEDTD GEGGAYTDNE LDEPAEEPLV SSITRSSEPV QHEESIRKPS PEPRAQMRRA
ASRDQLRDNS PPPTFKPEPP KAKTQNREES FDFSRSYEYK SNPSAAAGNE IPGASTKGCP
PPIAAKPTFG RPVLKPSTPV PPPESEETGE GSEEQHNAPK SVLGKVKIFE KMDHKAKLQR
MQELQEAQNA RIEIAQKHPD IYAVPIKTHK PDPGPPQYTS SRPPEPQKGP ARLYQDPRGS
YGSDAEEEEY RQQLSEHSRH GYYGQPSRYR DTEL
//
