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Database: UniProt
Entry: G1PGM9_MYOLU
LinkDB: G1PGM9_MYOLU
Original site: G1PGM9_MYOLU 
ID   G1PGM9_MYOLU            Unreviewed;       926 AA.
AC   G1PGM9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Tight junction protein 3 {ECO:0000313|Ensembl:ENSMLUP00000009801.2};
GN   Name=TJP3 {ECO:0000313|Ensembl:ENSMLUP00000009801.2};
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:ENSMLUP00000009801.2, ECO:0000313|Proteomes:UP000001074};
RN   [1] {ECO:0000313|Ensembl:ENSMLUP00000009801.2, 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:ENSMLUP00000009801.2}
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; AAPE02052842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G1PGM9; -.
DR   STRING; 59463.ENSMLUP00000009801; -.
DR   Ensembl; ENSMLUT00000010751.2; ENSMLUP00000009801.2; ENSMLUG00000010732.2.
DR   eggNOG; KOG3580; Eukaryota.
DR   GeneTree; ENSGT00940000160036; -.
DR   HOGENOM; CLU_006234_0_0_1; -.
DR   InParanoid; G1PGM9; -.
DR   OMA; MEEVTIW; -.
DR   TreeFam; TF315606; -.
DR   Proteomes; UP000001074; Unassembled WGS sequence.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   CDD; cd00992; PDZ_signaling; 3.
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; IPR005420; ZO-3.
DR   PANTHER; PTHR13865; TIGHT JUNCTION PROTEIN; 1.
DR   PANTHER; PTHR13865:SF11; TIGHT JUNCTION PROTEIN ZO-3; 1.
DR   Pfam; PF00625; Guanylate_kin; 1.
DR   Pfam; PF00595; PDZ; 3.
DR   Pfam; PF07653; SH3_2; 1.
DR   PRINTS; PR01597; ZONOCCLUDNS.
DR   PRINTS; PR01600; ZONOCCLUDNS3.
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          20..102
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          203..280
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          388..455
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          484..558
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          670..770
FT                   /note="Guanylate kinase-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50052"
FT   REGION          104..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..385
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          795..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          906..926
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        121..137
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        344..358
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        359..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        873..891
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   926 AA;  102575 MW;  6D37B35418AD202B CRC64;
     LFPLCQVLDM EELTIWEQHT VTVCKDPRRG FGIAISGGHD RPGGPVFVSD VVPGGPAEGR
     LQTGDQIVMV NGVSMENVNS TFAIHILKTC TKLANITVKR PRKIQLPSTK ASPCGPGHQD
     SDEDGPWRLE DANHGRGYEG DTSSGSGRSL GERSHRPRAG RRSRAGNHGS RSPGGGSEVR
     GLALMSGFKR LPRQDVQMRP LKSVLVRRRE SEEFGVKLGS QIFIKHITDS GLAAQNGGLQ
     EGDLVLQING VSSENLSLSD TRQLIEKSEG KLTLLVLRDR EQFLVNIPPA VSDSDSSLLE
     DISDLCSELS QAPPSHVPPP PQHRQRSPDT DRTNSPVESP QLRRRSSVDS RTTLEPGTRR
     VDTPRQSSYD IYRVPSRQSM EDRGYSPDSR VVRFYKGTSI GMKLAGGNDV GIFVSGVQEG
     SPAEEQGIQE GDQILQQVND VPFRNLTREE AVQVLLGLPL GEEVELVTQR KQDIFRKMVQ
     SRVGDSFYIR THFELEPSPP YGLGFTRGDV FHVLDTLYPG PGQGHARGGQ WLAVRMGRDL
     REQERGIIPN QKRAEQLASL EAAQRALGPG PGASAGSGGR AEFWRLRGFR RGAKKTSHRS
     REDLSDLTRQ GHYPPYERVV LREANFKRPV VILGPVADIA MQKLTAEMPD QFEIAESVLR
     TDRPSKIIKL DTVRVIAEQD KHALLDVTPS AVERLNYVQY YPIVVFCAPE SRSALKALRQ
     WLAPASRRST RRLYAQAQKL WKHSDHLFTA TVHLQGTSDG WYQELKAIIR EQQMRPIWTA
     EDQLDGSLED NLDLPHRGLN DSSADLSCDS RVNSDYETDG EGYTDGEGYT DGEGGPHTDV
     DEGPPAPALV RSSEPVLVEK PESLRDHGRS SGHQGAQVDS CHPQGQWRQE SIRTYAREAV
     RKKFTQARHV ESSDEDGYDW GPATDI
//
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