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TTD14_DROME
ID   TTD14_DROME             Reviewed;         475 AA.
AC   Q7K556; A8DYI1;
DT   13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=TRPL translocation defect protein 14 {ECO:0000303|PubMed:26509977};
GN   Name=Ttd14 {ECO:0000303|PubMed:26509977, ECO:0000312|FlyBase:FBgn0284257};
GN   ORFNames=CG30118 {ECO:0000312|FlyBase:FBgn0284257};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1] {ECO:0000312|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000312|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [3] {ECO:0000312|EMBL:AAK92870.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAK92870.1};
RC   TISSUE=Head {ECO:0000312|EMBL:AAK92870.1};
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [4] {ECO:0000305}
RP   FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP   PRO-75.
RX   PubMed=26509977; DOI=10.1371/journal.pgen.1005578;
RA   Cerny A.C., Altendorfer A., Schopf K., Baltner K., Maag N., Sehn E.,
RA   Wolfrum U., Huber A.;
RT   "The GTP- and phospholipid-binding protein TTD14 regulates trafficking of
RT   the TRPL ion channel in Drosophila photoreceptor cells.";
RL   PLoS Genet. 11:E1005578-E1005578(2015).
CC   -!- FUNCTION: GTP-binding protein which is required for the light-dependent
CC       internalization of the TRPL ion channel from the rhabdomere on the
CC       apical surface of photoreceptor cells to the cell body and for the
CC       recycling of TRPL back to the rhabdomere in the dark. Binds to 3-
CC       phosphoinositide (PtdIns(3)P) and phosphatic acid and so may interact
CC       with membranes, particularly the early endosome membrane where
CC       PtdIns(3)P is predominantly localized. Plays a role in preventing
CC       photoreceptor degeneration. {ECO:0000269|PubMed:26509977}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26509977}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A {ECO:0000312|FlyBase:FBgn0284257};
CC         IsoId=Q7K556-1; Sequence=Displayed;
CC       Name=B {ECO:0000312|FlyBase:FBgn0284257};
CC         IsoId=Q7K556-2; Sequence=VSP_058208;
CC   -!- TISSUE SPECIFICITY: Isoform A: Expressed in the head. Isoform B:
CC       Expressed in the head. {ECO:0000269|PubMed:26509977}.
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DR   EMBL; AE013599; AAF57688.2; -; Genomic_DNA.
DR   EMBL; AE013599; ABV53842.1; -; Genomic_DNA.
DR   EMBL; AY051446; AAK92870.1; -; mRNA.
DR   RefSeq; NP_001097365.1; NM_001103895.2. [Q7K556-2]
DR   RefSeq; NP_611333.1; NM_137489.4. [Q7K556-1]
DR   AlphaFoldDB; Q7K556; -.
DR   IntAct; Q7K556; 2.
DR   STRING; 7227.FBpp0112273; -.
DR   PRIDE; Q7K556; -.
DR   DNASU; 37119; -.
DR   EnsemblMetazoa; FBtr0086724; FBpp0085903; FBgn0284257. [Q7K556-1]
DR   EnsemblMetazoa; FBtr0113360; FBpp0112272; FBgn0284257. [Q7K556-2]
DR   GeneID; 37119; -.
DR   KEGG; dme:Dmel_CG30118; -.
DR   UCSC; CG30118-RA; d. melanogaster. [Q7K556-1]
DR   UCSC; CG30118-RB; d. melanogaster.
DR   CTD; 37119; -.
DR   FlyBase; FBgn0284257; Ttd14.
DR   VEuPathDB; VectorBase:FBgn0284257; -.
DR   eggNOG; ENOG502QVQD; Eukaryota.
DR   GeneTree; ENSGT00520000060563; -.
DR   HOGENOM; CLU_037796_0_1_1; -.
DR   GenomeRNAi; 37119; -.
DR   PRO; PR:Q7K556; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0284257; Expressed in anlage in statu nascendi and 74 other tissues.
DR   ExpressionAtlas; Q7K556; baseline and differential.
DR   Genevisible; A8DYI1; DM.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR   GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
DR   GO; GO:0045494; P:photoreceptor cell maintenance; IMP:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR033469; CYTH-like_dom_sf.
DR   InterPro; IPR038727; NadR/Ttd14_AAA_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF13521; AAA_28; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF55154; SSF55154; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; GTP-binding; Lipid-binding;
KW   Nucleotide-binding; Protein transport; Reference proteome; Transport.
FT   CHAIN           1..475
FT                   /note="TRPL translocation defect protein 14"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000436009"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         454..475
FT                   /note="GKQEEQSPVPAKQYHPYDENSD -> VKGAANGVSSTPLLLNGQ (in
FT                   isoform B)"
FT                   /id="VSP_058208"
FT   MUTAGEN         75
FT                   /note="P->L: Lack of GTP-binding, defective light-induced
FT                   internalization of TRPL, late-onset light-dependent
FT                   photoreceptor degeneration and larval lethality."
FT                   /evidence="ECO:0000269|PubMed:26509977"
SQ   SEQUENCE   475 AA;  54337 MW;  261D57E316B51697 CRC64;
     MATLLSNGQQ SVMASTSNGQ EQQRHQDEPE QQQQVEIRKS SSPKPGAMPS LKLNRMGSVS
     PKDKRVYKIV LTGGPCGGKT TGQSRLCTFF ENLGWKVFRV PETATVLLSG GVKFSDLTEK
     EAYKFQENLI RTMVQIENTY FELGNSSNRN CLIICDRGVM DASAYISKDK WEKMMAGNNW
     NPVEMRDNRY NQILHLVSAA NGAEDFYSTE DHACRSEGVD LARELDYKSA AAWVGHPYFD
     VIDNSTNFET KMNRMIESVC QKLGIDIGDR LQATSRKLKY LVALLPPDSE FPPFQDFDVV
     HHYLQSAGPK VQARLRKRGQ KNHWSYIHTQ RRPNVHGQAR IEVKTQLTHR DYMNLLAQRD
     DAHFTIYKKR RCFLINNQYF QLDIYKEPGH PRCKGLVLLE TYSSLTGDAL KNCMPKFLNI
     VKEVTGDPDY SMFNLSLKED WSTTKKFCRS ATHGKQEEQS PVPAKQYHPY DENSD
 
 
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