HIP14_DROME
ID HIP14_DROME Reviewed; 637 AA.
AC Q9VUW9;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Palmitoyltransferase Hip14 {ECO:0000303|PubMed:18158335};
DE EC=2.3.1.225 {ECO:0000255|RuleBase:RU079119};
DE AltName: Full=Huntingtin-interacting protein 14 homolog {ECO:0000305};
GN Name=Hip14 {ECO:0000312|FlyBase:FBgn0259824};
GN ORFNames=CG6017 {ECO:0000312|FlyBase:FBgn0259824};
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 {ECO:0000312|Proteomes:UP000000803};
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:AAM11132.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM11132.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM11132.1};
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, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=18158335; DOI=10.1083/jcb.200710061;
RA Ohyama T., Verstreken P., Ly C.V., Rosenmund T., Rajan A., Tien A.C.,
RA Haueter C., Schulze K.L., Bellen H.J.;
RT "Huntingtin-interacting protein 14, a palmitoyl transferase required for
RT exocytosis and targeting of CSP to synaptic vesicles.";
RL J. Cell Biol. 179:1481-1496(2007).
RN [5] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18032660; DOI=10.1523/jneurosci.2464-07.2007;
RA Stowers R.S., Isacoff E.Y.;
RT "Drosophila huntingtin-interacting protein 14 is a presynaptic protein
RT required for photoreceptor synaptic transmission and expression of the
RT palmitoylated proteins synaptosome-associated protein 25 and cysteine
RT string protein.";
RL J. Neurosci. 27:12874-12883(2007).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=18719403; DOI=10.4161/fly.6621;
RA Bannan B.A., Van Etten J., Kohler J.A., Tsoi Y., Hansen N.M., Sigmon S.,
RA Fowler E., Buff H., Williams T.S., Ault J.G., Glaser R.L., Korey C.A.;
RT "The Drosophila protein palmitoylome: characterizing palmitoyl-
RT thioesterases and DHHC palmitoyl-transferases.";
RL Fly 2:198-214(2008).
RN [7]
RP FUNCTION, INTERACTION WITH SOG, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20599894; DOI=10.1016/j.ydbio.2010.06.024;
RA Kang K.H., Bier E.;
RT "dHIP14-dependent palmitoylation promotes secretion of the BMP antagonist
RT Sog.";
RL Dev. Biol. 346:1-10(2010).
CC -!- FUNCTION: Probable palmitoyltransferase which is required for
CC photoreceptor synaptic transmission and for the correct expression and
CC localization of palmitoylated protein Csp and synaptosomal-associated
CC protein Snap25 (PubMed:18158335, PubMed:18032660). Probably
CC palmitoylates Csp (PubMed:18158335). Probably also palmitoylates the
CC dorsal-ventral patterning protein Sog and promotes its secretion and
CC activity and the stabilization of the membrane-bound form
CC (PubMed:20599894). Required for synaptic vesicle exocytosis
CC (PubMed:18158335). {ECO:0000269|PubMed:18032660,
CC ECO:0000269|PubMed:18158335, ECO:0000269|PubMed:20599894}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC EC=2.3.1.225; Evidence={ECO:0000255|RuleBase:RU079119};
CC -!- SUBUNIT: Interacts with dorsal-ventral patterning protein Sog.
CC {ECO:0000269|PubMed:20599894}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:18032660, ECO:0000269|PubMed:18719403,
CC ECO:0000269|PubMed:20599894}; Multi-pass membrane protein
CC {ECO:0000255}. Presynaptic cell membrane {ECO:0000269|PubMed:18032660,
CC ECO:0000269|PubMed:18158335}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to the Golgi apparatus in non-neuronal
CC cells and located primarily in presynaptic terminals in neurons.
CC {ECO:0000269|PubMed:18032660}.
CC -!- TISSUE SPECIFICITY: In stage 13-15 embryos, expressed in the central
CC nervous system. At the third instar larval stage, expressed in the
CC ventral nerve cord and is enriched in the neuropil.
CC {ECO:0000269|PubMed:18158335}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000255|RuleBase:RU079119}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes reduced basal
CC secretion of Sog. {ECO:0000269|PubMed:20599894}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC AKR/ZDHHC17 subfamily. {ECO:0000305}.
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DR EMBL; AE014296; AAF49554.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB94604.1; -; Genomic_DNA.
DR EMBL; AY094779; AAM11132.1; -; mRNA.
DR RefSeq; NP_001261911.1; NM_001274982.1.
DR RefSeq; NP_648824.1; NM_140567.3.
DR AlphaFoldDB; Q9VUW9; -.
DR SMR; Q9VUW9; -.
DR IntAct; Q9VUW9; 2.
DR STRING; 7227.FBpp0305754; -.
DR TCDB; 8.A.114.1.2; the huntington-interacting protein 14 (hip14) family.
DR SwissPalm; Q9VUW9; -.
DR PRIDE; Q9VUW9; -.
DR DNASU; 39747; -.
DR EnsemblMetazoa; FBtr0075518; FBpp0075273; FBgn0259824.
DR EnsemblMetazoa; FBtr0333577; FBpp0305754; FBgn0259824.
DR GeneID; 39747; -.
DR KEGG; dme:Dmel_CG6017; -.
DR UCSC; CG6017-RA; d. melanogaster.
DR CTD; 39747; -.
DR FlyBase; FBgn0259824; Hip14.
DR VEuPathDB; VectorBase:FBgn0259824; -.
DR eggNOG; KOG0509; Eukaryota.
DR GeneTree; ENSGT00530000063074; -.
DR HOGENOM; CLU_012510_3_1_1; -.
DR InParanoid; Q9VUW9; -.
DR OMA; PWMAGIF; -.
DR OrthoDB; 445686at2759; -.
DR PhylomeDB; Q9VUW9; -.
DR SignaLink; Q9VUW9; -.
DR BioGRID-ORCS; 39747; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39747; -.
DR PRO; PR:Q9VUW9; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0259824; Expressed in cleaving embryo and 39 other tissues.
DR ExpressionAtlas; Q9VUW9; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:FlyBase.
DR GO; GO:0008021; C:synaptic vesicle; IDA:FlyBase.
DR GO; GO:0016409; F:palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; ISS:FlyBase.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0050714; P:positive regulation of protein secretion; IMP:FlyBase.
DR GO; GO:0018345; P:protein palmitoylation; ISS:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IMP:FlyBase.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF01529; DHHC; 1.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; ANK repeat; Cell membrane; Cell projection;
KW Golgi apparatus; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Repeat; Synapse; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..637
FT /note="Palmitoyltransferase Hip14"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436308"
FT TOPO_DOM 1..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 296..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..318
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 319..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..373
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..520
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 521..541
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..637
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 77..106
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 111..140
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 144..173
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 177..207
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 212..242
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT DOMAIN 430..480
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT ACT_SITE 460
FT /note="S-palmitoyl cysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q8IUH5"
SQ SEQUENCE 637 AA; 71299 MW; 0985078D5D091710 CRC64;
MYQSACQAAT TGSCVPGTGQ QPDNERQSAL IAQQPPTAPV EPDYSGFDIV KATQYGAIAR
VRELVESGWD VNQPDSETVT LLHWAAINNR RDIIRYFLEK GATVDAVGGE LNATPLHWAT
RQGHLGAVVL LMAAGADPRI RDAEGCSCIH IAAQFAHTAL VAYFIAKGVD PDLQDRGGMT
ALMWAAWKVC ALDPVRLLLT LGANPAMVDY THGNTALHWA ILARNATAIS TLVLKSKASL
DVPNLRGETP LSMLESQTGA IWIGAKVMDR VKEAALTSQQ RRSLLSKLRH DKRLRWWSMV
ACPFTAFYLA GIVFTVNTLY IIKFFLLGCL YSIFHTIGKA LFDEHLMALL PLSVYLATKA
WFYVTWLMYI DDAVSFTATV CFLISSLLLW VCFLKSWKGD PGIIRPTREQ RFKTIIELSE
RGGIGFEPAS FCSGCLVRRP IRSKHCSVCD RCVARFDHHC PWVGNCIGLK NHSYFMGFLW
MLLIMCAWML YGGSKYYVNQ CNVRFDDFLG AMRAIGNCDA WVGWVMGNAL LHMSWVILLT
ICQTYQVICL GMTTNERMNR GRYRHFQAKG GHSPFTRGPI QNLVDFLECS CFGLVQPKRV
DWMNYYDYDA QTHQTIEKEP LLSVDCPDGM AGDHQYV
