ID A0A1J1IG23_9DIPT Unreviewed; 2182 AA.
AC A0A1J1IG23;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=CLUMA_CG012486, isoform C {ECO:0000313|EMBL:CRK99215.1};
GN Name=putative Protein TAPT1 homolog {ECO:0000313|EMBL:CRK99215.1};
GN ORFNames=CLUMA_CG012486 {ECO:0000313|EMBL:CRK99215.1};
OS Clunio marinus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Clunio.
OX NCBI_TaxID=568069 {ECO:0000313|EMBL:CRK99215.1, ECO:0000313|Proteomes:UP000183832};
RN [1] {ECO:0000313|EMBL:CRK99215.1, ECO:0000313|Proteomes:UP000183832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Membrane
CC {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
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DR EMBL; CVRI01000049; CRK99215.1; -; Genomic_DNA.
DR Proteomes; UP000183832; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0061817; P:endoplasmic reticulum-plasma membrane tethering; IEA:InterPro.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR CDD; cd14809; bZIP_AUREO-like; 1.
DR CDD; cd04024; C2A_Synaptotagmin-like; 1.
DR CDD; cd04050; C2B_Synaptotagmin-like; 1.
DR CDD; cd04030; C2C_KIAA1228; 1.
DR CDD; cd21670; SMP_ESyt; 1.
DR Gene3D; 2.60.40.150; C2 domain; 3.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037752; C2C_KIAA1228.
DR InterPro; IPR037749; Ext_Synaptotagmin_C2B.
DR InterPro; IPR031468; SMP_LBD.
DR InterPro; IPR039010; Synaptotagmin_SMP.
DR InterPro; IPR008010; Tatp1.
DR PANTHER; PTHR45761; EXTENDED SYNAPTOTAGMIN-LIKE PROTEIN 2, ISOFORM C; 1.
DR PANTHER; PTHR45761:SF1; EXTENDED SYNAPTOTAGMIN-LIKE PROTEIN 2, ISOFORM C; 1.
DR Pfam; PF00168; C2; 3.
DR Pfam; PF05346; DUF747; 1.
DR Pfam; PF17047; SMP_LBD; 1.
DR SMART; SM00338; BRLZ; 1.
DR SMART; SM00239; C2; 3.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 3.
DR PROSITE; PS00036; BZIP_BASIC; 1.
DR PROSITE; PS50004; C2; 3.
DR PROSITE; PS51847; SMP; 1.
PE 4: Predicted;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 94..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 753..932
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 930..1054
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1076..1197
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1311..1432
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 474..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1224..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1458..1478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1737..1869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1891..1910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1920..1969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1737..1807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1830..1854
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1896..1910
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1920..1941
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1951..1969
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2182 AA; 244647 MW; ABCD4A39611CDEB7 CRC64;
MEFSSTPVKR IRFRGDSFQA ENEFLLDNDN TEDFHTFKNG EIPKENEQAN FGLLDFLRVE
LNRGYCLNHD EERYTARREK IYSFMKIPRE LEKFLAYGCM QCADSFLYIF TFLPVRYIMA
LWALLTRPVI RCLRNRRDYQ RLLSPAETCD LLKGTLWFVV SFALLYADTN MLYHLIKSQS
IIKLYMFYNM LEIGDRLLSA FGQDIIDALF WTATEPKTPH KRHLSVFAHF LFAIIYVLLH
SILVMFQATA LNVAINSSNK GLLTIMMSNN FVELKGSVFK KFDKNNLFQL TCSDVRERFH
LSILLVIVMI QTMREYNWKS EQFFVMLPDC FWVMFTEFIV DWIKHAFITR FNEIPIDVYK
EYTISLAYDV TQTRQKHAFS DHSDLVARRM GFIPFPLGVV LVKALYHSLS FTNFGSAVLF
LAAYSCLFSC RVLNTICTLG KACDIMQKHE DDKIAEKFSN QTPACSIIKS KNVSNGKVDS
STSPLHRTSL INSPDQSPVI SSTTPSPIRI INVQSPSSPS PDDKRLKLDS SLGATALFSN
SDVDLEDMGI LNSKVIEQTV EDKIQSIDDS LRAGSEPDLA NIPVESSLEE DELQPTLNRR
RSHKRSEKKD QDEVCLLKDE TDDLLSGKEL KSNLDSEIAE ASANIVTDKM SNSKELSKEK
ADLNEKVNDG SMFSIIYSTV KKVAIVGVVY FVGYMNWSFA WLLCPLVFSV VREQYRSQHE
IRRAVAKASA TSSDKEVILA RLNDLPAWVF FPDIERCEWL NRILKQVWPN ANHYTRSLIK
DKIEPNVQKA LAGYKLNGFK FDRIILGTIP PRIGGVKVYD KNISRNEVIM DLDLFYAGDC
DINFVLGGMR GGIKDFQVHG TLRIVMKPLI SQIPLFGGMQ IFFLNNPNID FNLVGVVDLL
DMPGLSDLLR KIIVDQIAAF MVLPNKLPII LSEEIEALSL KMPEPEGVLR VHVVEAKNLM
KMDIGMLGKG KSDPYAIVTV GAQQFRTQII DNNVNPKWDY WCEAEINETL VQELLITLWD
YDGFFPGVQG DDFLGRATVE ISTVVRKSEV DTWLTLEQAK HGMVHLRLTW MQLSTDKSDL
KAALAETQML RVTDMSTALL TVFIDSAKNL PHARQQSNPD PYIVLSVGKK TEQTAVQMRT
DAPVWEQGYT FLVANPENDT LQMKVVDNKT QNEIGKLSYI IATLLDKKNM EIINQPFQIQ
KSGPESKLIM TLQLRILKRS EPIPDDEDEE MIGDVVAKED PSKSPLKKQD SRVSRSTVND
AVIEEPIESS SVSANLSAAP PSPTASKTSD LSTSSFERNP SIKSFDGEAG SLGAINLTVQ
YSVQRQRLIV IVHKIRNIPL KDPNNIPDPY VKLYLLPGRS KDSKRKTNVI KDNCNPVFDQ
TFEYLISTAE LYSSSLEVTV ATQKVIGSPI LGMLKIELKD PEIQGVGKNF WWNLLPEFKS
TEFFLKFEAS SPLFELSPPS SGALSPPTPL ASNSNSISDK MDSSINNPLL TTASMPIPTR
NVTSNCNMSN NNNRTTNDFS DVIFEFENSK SPLSTISENP KQNNQTPMVI NYTDGSTFGF
QQNSFSGGSG SNLMWDGVSP MMNTASDTNT MGGLSDKSGP FHMDEDDIFQ VDKSDLIQGP
TLAELNGDNL YVDLLNIDDI LAVDSNQYLQ QSNMQNLTQL TAVNFQSLQN AINESSQAEQ
LSPNQYQNIT IPQTPHNTPI PSFQTNGGQL IFYDDPSSNN SSFNVYSPPN TLSISNHLRN
APTSTTTTMT AFSPGSQSHS STSTSSIALN SSLSPPHSQK SFTTSRVRQS RSGRSSGLVQ
HNPKYSTLHS LLMKKDPTSA EKSMMGKIQH AVASSPSQLV THTSAVSPSG LPTRRLNMQG
GGFVSRLSSS APTHLGLEQI WQRREPRPHL LSTGSLAEGH GSTSSLSGEI LSPENIDFSQ
DEAYSDDDDS DHYEDFSSDS DGDDNKDQLR SMSSNDSNNN QKSSNFSSSK KNARFFWQYN
VQAKGPKGQR LVIKTQAEDP HHLNEVTDPV FSPNCSVRGI KSIQIKHSGK ARKGDGNDLT
PNPKKLNAIG KELDKLGRVI NDMTPVSELP FNVRPKTRKE KNKLASRACR LKKKAQHEAN
KIKLFGLEKE HKSLLNGIHQ MKQLLALKCS SSHDTQEEIN QRMEQVVVES TTVKIAENST
EYVNRVLDRM KAGNPTGGLE EY
//
