ID V9K9L4_CALMI Unreviewed; 1019 AA.
AC V9K9L4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Tight junction protein ZO-2-like protein {ECO:0000313|EMBL:AFO94552.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO94552.1};
RN [1] {ECO:0000313|EMBL:AFO94552.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Intestine {ECO:0000313|EMBL:AFO94552.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
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; JW862035; AFO94552.1; -; mRNA.
DR AlphaFoldDB; V9K9L4; -.
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 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 2: Evidence at transcript level;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Tight junction {ECO:0000256|ARBA:ARBA00022427}.
FT DOMAIN 21..108
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 319..396
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 503..584
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 598..666
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 776..876
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 121..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1019
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1007
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1019 AA; 115416 MW; 28E2A3AD734314BD CRC64;
MSVRFLDQST VMEEIIWEPF TVTLHKDPRI GFGIAISGGR DKPNPANGDP AILVTDVVPQ
GPAFGKMMIN DKIIMVNGVS MENVTSFFSI QTLKSCGKAV NIIIKRSRKV VVNRELPANS
YYSSQSFHSD PPRSDDASDE DEDYDPNRNL RRAQNQNLYA DHPNHRPDYN HHNHSREPSS
DGSYDRDRSS TRSYERGRSP TRSYGRGHSP TRSYDRGRSP SWSDDQGRSP PRSYDQGINR
AKSYDQLSSN RGYDEELSPM RRAKSHDRGL SPRRSDDRGH SSSREYTGDR ERYPKRSHHD
ELDQNNSHSD LTFNKPIQSV LVKQNPNEEY GLRLGSQVYI KHMSPSGLAT KDGVLQEGDI
ILKINGIVTE NISLEDTRTL IEKSEGKLAL LVLRDKEQFL VNIPELADSD EHSSGLEDIS
DLEPDPLDSP DERRRKPVER NPERETKNNE RLKTNKADVV DKPTAIEPLP GLSSVSEDPI
YSLPVKPSFT KLKDEYNAGY SPDMKMARFT KDDSVGLQLA GGNDVGIFVS GVQDGSPAGK
QGIQKGDQIL KVNNVNFQNL TREEAILFLL DIPRGEQMEI LAQSKQDIYT KMMQSNVGDS
FHIRAHFEHE ADEPRGLTFS RGEVFRVVDT MFKGKLGTWL AVRIGHDLKE QDRGTIPNKS
RAEQIVRVGM TQKIASSNSS TGPRAEFWKM RGLRGAKKNL RKSRDDLSNL TIQSRFPPYE
HVALREASFK RPIVILGPIS DVAIQTLADD LPIKFELAQT VRRNPDADYS SSIIKLETVK
FIAQKDKHGL LDITPPAIER LNYVKWYPIV VFFNPENRQE VKAVRQRLCP ESKKSSKRLY
TQAVKLRKHW SHLFTATINL NSAPATWFSN LASVIKEQQS HPVWFSEEKT EEGGNEELEI
LKPSISMDYL SCDDSRMTSD YEDTDAEGGG YTDNELDDYM GVPAISRSSE PVRNEAHHSP
VPHTRVSTEN LLAQVQPRGQ YKNPQYPRSD KWDHRTHHNH GRTNYSSDED DWNGPATEL
//
