ID E2AT58_CAMFO Unreviewed; 1227 AA.
AC E2AT58;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Tight junction protein ZO-1 {ECO:0000313|EMBL:EFN63382.1};
GN ORFNames=EAG_08690 {ECO:0000313|EMBL:EFN63382.1};
OS Camponotus floridanus (Florida carpenter ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Camponotus.
OX NCBI_TaxID=104421 {ECO:0000313|Proteomes:UP000000311};
RN [1] {ECO:0000313|EMBL:EFN63382.1, ECO:0000313|Proteomes:UP000000311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C129 {ECO:0000313|Proteomes:UP000000311};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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; GL442513; EFN63382.1; -; Genomic_DNA.
DR AlphaFoldDB; E2AT58; -.
DR STRING; 104421.E2AT58; -.
DR EnsemblMetazoa; XM_020028939.2; XP_019884498.1; LOC105255764.
DR InParanoid; E2AT58; -.
DR OMA; RDSSCCH; -.
DR Proteomes; UP000000311; Unassembled WGS sequence.
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; cd11859; SH3_ZO; 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 PANTHER; PTHR13865:SF28; POLYCHAETOID, ISOFORM O; 1.
DR PANTHER; PTHR13865; TIGHT JUNCTION PROTEIN; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 2.
DR Pfam; PF07653; SH3_2; 1.
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; PS51257; PROKAR_LIPOPROTEIN; 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:UP000000311};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443};
KW Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 84..171
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 188..261
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 374..447
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 641..741
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1123..1204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..342
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..836
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..860
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1227 AA; 134130 MW; C7CBA7C2FCF72938 CRC64;
MDRSDNNVVG VGGGSGSGGS GGGSGGGSGS CHVGNSGSPP NSISSTHGTV HNSTGGLDAQ
VAHPEILGLD IRADTGDRGW EIHHVTVTRV PGYGFGIAVS GGRDNPHFTN GDPAIAISDV
LKAGPAEGKL QVNDRIISAN GVSLEGADYG AAVRVLRDSG STVLLVVKRR SSSNSPGCLG
SVAPQSHRLT LTRNNKKDDF GIVLGCRLYV KEVTRENIGV KTGDVLTRIG SVAADNMSLK
EARKLMDQCK DRLSIVITRD SSCCHVQQQS KGDSGEYLSG ASYSSQNLYV PPPTRQPLDD
KSNLVPRGRS RGPLMDVSLS QLDLPATPTV DPPRPPPPRP EDYYSTRRQL YDEDSVSPRT
KQPMPDPRFI TFQKEGSVGV RLSGGNETGV FVTAVQAGSP ASLQGLQPGD KILKINDMDM
KGVTREEAVL FLLSLQEQID LIVQHRRQEY DQIIASGRGD SFHIKTHFHY EQPQKGEMSF
RSGDVFHVVD TLHNGVVGSW QVFRIGRNNQ EVQKGIIPNK ARAEELATAQ FNATKKEMSA
SESRGSFFRR RRNSHRRSKS LGRDHWDDVV FSDSVSKFPA YERVILRHPG FIRPVVLFGP
VADLAREKLL KDFPDKFTSP QMESQMEDGT GKNTKTSGII RLSAIREVME RSKHALLDIT
PNAVDRLNYA QFYPIVIFLK AETKQVIKEM RAGIPKSAHK SSKKLLEQCQ KLDKIWGHVF
SAVITLNTPE AWYRKLRELI DRQQQGLLWM SQTKPEEALS DDFLFPMTSR LSYASSPESD
LELSPAPVIP GTLGPPSRLK SSSDPSIATQ DDTTAPPPYS TNYQQSFEQQ KRRSQGGMGD
SKYGFSLSGQ MSNQSGSPEY LGGSFEPRSP HHSPPDLPPR VDRNVKPINQ APRGTIGRSA
QERLGVNKID SVLDMGNYIN ATPHKANATS SLERAQPKAG SYDSMSSYDS YNNTNGNANY
GAVNLNASTG RLGPNVPDDL KSNMSVRTHD PPHRFTRSQI QPVTTHDAPT RTDYAKYSRS
TDYKSIPMSQ NKPGGTYKPI PPPKPKNYRP PQASFGQTEN NGNDGNNSYQ HSKSYSIATS
HVHNGVESNV QRNSGQYYYN IPPPGRYNEG NLVNSHHNLN HLATPTHSHS LSHSHAHSHS
SPPVTTAHSH SNSAGQISLG LTHNRNSTNH NGYMHGNNSH GPAGSVYPSA NPGHNREPSG
LDLAGSREQR GSAFELYRKP VHHYNMR
//
