ID G1PHJ2_MYOLU Unreviewed; 1230 AA.
AC G1PHJ2;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Tight junction protein 2 {ECO:0000313|Ensembl:ENSMLUP00000010147.2};
GN Name=TJP2 {ECO:0000313|Ensembl:ENSMLUP00000010147.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000010147.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000010147.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000010147.2}
RP IDENTIFICATION.
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 EMBL; AAPE02013563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02013564; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02013565; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1PHJ2; -.
DR STRING; 59463.ENSMLUP00000010147; -.
DR Ensembl; ENSMLUT00000011132.2; ENSMLUP00000010147.2; ENSMLUG00000011106.2.
DR eggNOG; KOG3580; Eukaryota.
DR GeneTree; ENSGT00940000158634; -.
DR HOGENOM; CLU_006234_1_0_1; -.
DR InParanoid; G1PHJ2; -.
DR OMA; RQRHSKI; -.
DR TreeFam; TF315957; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
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:UP000001074};
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 349..427
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 551..632
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 646..711
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 734..918
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 202..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 964..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1145..1230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..983
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 998..1023
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1052
FT /note="Basic and acidic 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; 138086 MW; 1FFDBA533EF11A77 CRC64;
MKMAQVLQRL WLQAGRKLGL LKGHKIQDVS CLAKVFPKGT PWLSEGMNEI LKAPGMEEVI
WEQYTVTLQK DSKRGFGIAV SGGRDNPHFE NGETSIVISD VLPGGPADGL LQENDRVVMV
NGTPMEGVLH SFAVQQLRKS GKIAAIVVKR PRKVQLAPLQ SGLPLNEEDR AFEVMDEFDG
RSARSGYSDR YSERSRLHSW ENSLERGHPH DRPHSQERDR ARDRSRGRSL ERGLDRDDYD
RARDRSRGRS LERGLDQDYY DGARDRSRGR SLERGLDHDY GRGRDSSHGR GRSIDQDYDR
AYSPEVEYRH RGQPDARSKM SRSCEHLRLG SPTPEPRGRK DHEGDKPIGV LLTKSKANEE
YGLRLGSQIF IKEMTSTGLA TKDGNLHEGD IILKINGTVT ENMSLTDARK LIEKSRGKLQ
LVVLRDSKQT LIHIPALDDS DSEVLKPDIS EIESNRSFSP EERRQPYSDY DYHSSNEKLK
EKPSLREDIQ NRWSRMGSTP TPFKCAGDIA AATETSQEPK HQEEAPAPQP KALPRTFLRP
SPEDEAIYGP NTKMVKFRKG DSVGLRLAGG NDVGIFVGGI QEGTSADQEG LLEGDQILKV
NTQDFRGMVR EDAVLYLLEI PKGEMVTILA QSRADVYREI LACGRGDSFF IRSHFECEKE
TPQSLAFTRG EIFRVVDTLY DGKLGHWLAV RIGNELEKGL IPNKSRAEQM ASVQNAQRDN
AGDRADFWRM RGQRSGLKKN LRKSREDLTA AVSVSTKFPA YERVLLREAG FKRPVVLFGP
IADIAMEKLA HGLPDLFQIA KSEPKDAGSE KSSGVVRLNT VRQIIEQDKH ALLDVTPKAV
DLLNYTQWFP IVIFFNPDSR QGVKTMRQRL DPTSNKSSRK LYDQANKLKK TCAHLFTATI
DLNAANDSWF GSLKDTIQHQ QGEAVWVSEG KMEGLDDDAE DRMSYLTAMG ADYLSCDSRL
ISDFEDTDGE GGAYTDNELD EPAEEPLVSS ITRSSEPVQH EESVRKPSPE PRAQTRRATS
RDQLRDNSPP PAFKPEPPKA RTQKREDSFD YSRSYEYMPN SPPAVAGNEI PGASAKGPPP
PIAAKPTFCK PILKPSTPVL PPESEEAGEG SEEQDNASKS VLGKVKIFEK MDHKARLQRM
QELQEAQNAR EEIKEKNNPT VALVANKLRD GEGTPWSRPL VPQKGPSALY QDARGSYSSD
VEEEEYRQQL SEHSKRGYYG QPSRYRDTEL
//
