ID A0A3Q0G6G7_ALLSI Unreviewed; 1860 AA.
AC A0A3Q0G6G7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Tight junction protein ZO-1 isoform X3 {ECO:0000313|RefSeq:XP_025055256.1};
GN Name=TJP1 {ECO:0000313|RefSeq:XP_025055256.1};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_025055256.1};
RN [1] {ECO:0000313|RefSeq:XP_025055256.1}
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_025055256.1; XM_025199471.1.
DR Proteomes; UP000189705; 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; cd12026; SH3_ZO-1; 1.
DR Gene3D; 2.30.42.10; -; 3.
DR Gene3D; 2.60.220.30; -; 1.
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; IPR005418; ZO-1.
DR InterPro; IPR035597; ZO-1_SH3.
DR InterPro; IPR000906; ZU5_dom.
DR PANTHER; PTHR13865:SF28; POLYCHAETOID, ISOFORM O; 1.
DR PANTHER; PTHR13865; TIGHT JUNCTION PROTEIN; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 3.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF00791; ZU5; 1.
DR PRINTS; PR01597; ZONOCCLUDNS.
DR PRINTS; PR01598; ZONOCCLUDNS1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 3.
DR SMART; SM00218; ZU5; 1.
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.
DR PROSITE; PS51145; ZU5; 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:UP000189705};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 107..194
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 271..349
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 506..587
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 601..669
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 775..876
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT DOMAIN 1726..1860
FT /note="ZU5"
FT /evidence="ECO:0000259|PROSITE:PS51145"
FT REGION 18..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1127..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1456..1679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..949
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1128..1151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1316..1341
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1528
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1545..1562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1575..1624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1642..1669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1860 AA; 208424 MW; 867B1A7D8DB198AB CRC64;
MQRSFPDLSE ETKMMAVSEM ELHETCETND QEGNPSAEDP VNQSFNKYRV TPPSENPNGA
SCSVSQGKPS LRRIKGRIHR SKSLDSIDFC EFSSTTMEET AIWEQHTVTL HRAPGFGFGI
AISGGRDNPH FQSGETSIVI SDVLKGGPAE GLLQENDRVA MVNGVSMDNV EHAFAVQQLR
KSGKNAKITI RRMKKVQIPV ARPEPEPVSE NEEDSFDEEI QDPRSARGGP GANRKHEKSW
VRDRSASRER SLSPRSDRRS IASSQPAKPT KVTLVKSRKN EEYGLRLASH IFVKEISQDS
LAARDGNIQE GDVVLKINGT VTENMSLADA KTLIERSKGK LKMVVQRDER ATLLNVPDLS
DSIHSANASE RDDISEIQSL ASDHSNRSHD RPRRSRSRSP DQRSEPSDHS RHSPQQPSNG
SLRSREDERV SKPGAISTPV KNADDIPLSK TMEEVVVERN EKQTPPLPEP KPVYAQAGQP
DVDLPVSPSD GPLPSSTHED GMLRPSMKLV KFKKGDSVGL RLAGGNDVGI FVAGVLEDSP
AAKEGLEEGD QILRVNNVDF TNIIREEAVL FLLDLPKGEE VTILAQKKKD VYRRIVESDV
GDSFYIRTHF EYEKESPYGL SFNKGEVFRV VDTLYNGKLG SWLAIRIGKN HKEVERGIIP
NKNRAEQLAS VQYTLPKTAG GDRADFWRFR GLRSSKRNLR KSREDLSAQP VQTKFPAYER
VVLREAGFLR PVTIFGPIAD VAREKLAREE PDIFQIAKSE PRDAGTDQRS SGIIRLHTIK
QIIDRDKHAL LDVTPNAVDR LNYAQWYPIV VFLNPDSKQG VKTMRTRLCP ESRKSARKLY
ERAHKLRKNN HHLFTTTINL NSMNDGWYGA LKEAIQQQQN QLVWVSEGKA DGATSDDLDL
HDDRLSYLSA PGSEYSMYST DSRHTSDYED TDTEGGAYTD QELDETLNDE VGTPPESAIT
RSSEPVREDS SGMHHEAQAY PYVSQAQPQP NLRMDSPGFK ITASQPKAEA SPAVPYLSPS
PETNPAISST SVVNPNVNLT NVRLEEPTPP PYNSYQPQAG PLRTSSTEGA HIMLRDQEPS
SLSPHIDPTK VYRKDPYINE EAAPRQNYIL KQPAVNHPVH RQERESNLIY ESQTQYTEKQ
PSREYEQSTY RYDSANYSDQ FARSYDPHLH YEDRVPSYED QWSYYDEKQP YQPRPPYDNQ
PPKDFDPRQN AEESTERSYY PAQPRFEEPP PMTYDSRPRY EHAPKNFIPQ VRYEDQPTTA
YDIHGRYKPE AQTYPPVISR SPEPKQYFEP HTRGYEPGPP QGFNAKVGQY EPSHTTANVP
PPPPPSQTKP EILPSNSKPL PTPPTLTEEE EDPAMKPQSV LTRVKMFENK RSLSVEKIKD
SNDTPAVKPP ELAPKPTLAT VAKPASQYEH DKTTYRAPEP QRPQAKPPED IVRSNHYDPE
EDEEYYRKQL SYFDRRSFEN KPSAQIPASH HPEPAKPVHP QLNFTNYSSK GKPTDTEPMD
RPVGEKRYEP VPQVTSAVPP PPPVQYTQPQ SINNPALSLQ AHHKPALSEV NSVSVDFQNS
TVSKPDPPPP QNKPAILRSS NREDTVQSTF YPQKSFPDKG PLNGSEQTQK PVTPAYNRFT
TKPYTSAARP FERKFESPKF NHNLLPNETQ HKPELPSKSP NSPQPILKAH GSLQPSEFDS
GMDTFSIQAD KPKYQPNNVN AVPKAIPVSP SALEDDEEED GHTVVATARG VFNSNGGVLS
SIETGVSIII PQGAIPEGIE QEIYFKVCRD NSILPPLDKE KGETLLSPLV MCGPHGLKFL
KPVELRLPHC ASMTPDGWSF ALKSSDSSSG DPKTWQNKSL PGDPNYLVGA NCVSVLIDHF
//
