ZDHCS_CAEEL
ID ZDHCS_CAEEL Reviewed; 351 AA.
AC Q5FC64;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Palmitoyltransferase spe-10 {ECO:0000255|RuleBase:RU079119, ECO:0000305};
DE EC=2.3.1.225 {ECO:0000255|RuleBase:RU079119};
DE AltName: Full=Defective spermatogenesis protein 10 {ECO:0000312|WormBase:AC3.10};
GN Name=spe-10 {ECO:0000312|WormBase:AC3.10};
GN ORFNames=AC3.10 {ECO:0000312|WormBase:AC3.10};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF VAL-31; HIS-169; VAL-222 AND GLY-302.
RX PubMed=16143610; DOI=10.1534/genetics.105.047340;
RA Gleason E.J., Lindsey W.C., Kroft T.L., Singson A.W., L'hernault S.W.;
RT "spe-10 encodes a DHHC-CRD zinc-finger membrane protein required for
RT endoplasmic reticulum/Golgi membrane morphogenesis during Caenorhabditis
RT elegans spermatogenesis.";
RL Genetics 172:145-158(2006).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=2744235; DOI=10.1016/0012-1606(89)90103-6;
RA Shakes D.C., Ward S.;
RT "Mutations that disrupt the morphogenesis and localization of a sperm-
RT specific organelle in Caenorhabditis elegans.";
RL Dev. Biol. 134:307-316(1989).
RN [4] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=10638523; DOI=10.1016/s0197-4580(99)00085-8;
RA Cypser J.R., Johnson T.E.;
RT "The spe-10 mutant has longer life and increased stress resistance.";
RL Neurobiol. Aging 20:503-512(1999).
CC -!- FUNCTION: Involved in spermatogenesis, specifically in the
CC morphogenesis of fibrous body-membranous organelles (FB-MO), which are
CC Golgi-derived organelles used for transporting sperm-specific
CC components, in spermatocytes and in their localization into budding
CC spermatids (PubMed:16143610, PubMed:2744235). Required for the proper
CC formation of spermatids and spermatozoa (PubMed:2744235).
CC {ECO:0000269|PubMed:16143610, ECO:0000269|PubMed:2744235}.
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}. Note=Mainly found in fibrous body-membranous
CC organelles. {ECO:0000269|PubMed:16143610}.
CC -!- TISSUE SPECIFICITY: Expressed during spermatogenesis in budding and
CC budded spermatids. {ECO:0000269|PubMed:16143610}.
CC -!- DEVELOPMENTAL STAGE: Only expressed during spermatogenesis in adult
CC males and in hermaphrodites in the larval stage 4.
CC {ECO:0000269|PubMed:16143610}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000255|RuleBase:RU079119}.
CC -!- DISRUPTION PHENOTYPE: Self-sterile phenotype which is slightly
CC temperature sensitive (PubMed:16143610). In hermaphrodites the
CC temperature sensitivity is restricted to the larval stage 4 when
CC spermatogenesis takes place (PubMed:16143610). Premature disassembly of
CC FB-MO before or while spermatids are budding from spermatocytes
CC (PubMed:2744235). FB remain in spermatocytes whereas MO localize to
CC spermatids but often fail to fuse with plasma membrane
CC (PubMed:2744235). Resulting spermatids are usually smaller than normal
CC and contain several or mislocalized nuclei (PubMed:16143610,
CC PubMed:2744235). Fewer spermatozoa are generated and those that are
CC have abnormally short pseudopods and are immotile (PubMed:2744235). The
CC size of spermatocytes is unaffected (PubMed:2744235). Increased life
CC span and resistance to UV and heat but not to oxidative stress induced
CC by paraquat (PubMed:10638523). Normal production of fertile oocytes
CC (PubMed:10638523). {ECO:0000269|PubMed:10638523,
CC ECO:0000269|PubMed:16143610, ECO:0000269|PubMed:2744235}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC {ECO:0000255|RuleBase:RU079119}.
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DR EMBL; Z71177; CAI46554.1; -; Genomic_DNA.
DR RefSeq; NP_001021339.1; NM_001026168.3.
DR AlphaFoldDB; Q5FC64; -.
DR SMR; Q5FC64; -.
DR BioGRID; 532832; 8.
DR STRING; 6239.AC3.10; -.
DR PaxDb; Q5FC64; -.
DR EnsemblMetazoa; AC3.10.1; AC3.10.1; WBGene00004964.
DR EnsemblMetazoa; AC3.10.2; AC3.10.2; WBGene00004964.
DR GeneID; 3565514; -.
DR KEGG; cel:CELE_AC3.10; -.
DR UCSC; AC3.10; c. elegans.
DR CTD; 3565514; -.
DR WormBase; AC3.10; CE37870; WBGene00004964; spe-10.
DR eggNOG; KOG1315; Eukaryota.
DR HOGENOM; CLU_027721_1_0_1; -.
DR InParanoid; Q5FC64; -.
DR OMA; RYCKTCW; -.
DR OrthoDB; 1491968at2759; -.
DR PhylomeDB; Q5FC64; -.
DR PRO; PR:Q5FC64; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004964; Expressed in larva and 2 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043227; C:membrane-bounded organelle; IDA:WormBase.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0097723; P:amoeboid sperm motility; IMP:WormBase.
DR GO; GO:0051179; P:localization; IMP:WormBase.
DR GO; GO:0061025; P:membrane fusion; IMP:WormBase.
DR GO; GO:0007097; P:nuclear migration; IMP:WormBase.
DR GO; GO:0006996; P:organelle organization; IMP:WormBase.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IBA:GO_Central.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:WormBase.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR GO; GO:0031268; P:pseudopodium organization; IMP:WormBase.
DR GO; GO:0007286; P:spermatid development; IMP:WormBase.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Differentiation; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Spermatogenesis; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..351
FT /note="Palmitoyltransferase spe-10"
FT /id="PRO_0000431241"
FT TRANSMEM 21..43
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT DOMAIN 154..204
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT MUTAGEN 31
FT /note="V->E: In eb106; defect in spermatogenesis.
FT Temperature sensitive fertility defect."
FT /evidence="ECO:0000269|PubMed:16143610,
FT ECO:0000303|PubMed:16143610"
FT MUTAGEN 169
FT /note="H->Y: In eb64; defect in spermatogenesis. Slightly
FT temperature sensitive fertility defect. Does not affect
FT spe-10 localization."
FT /evidence="ECO:0000269|PubMed:16143610,
FT ECO:0000303|PubMed:16143610"
FT MUTAGEN 222
FT /note="V->D: In eb105; defect in spermatogenesis.
FT Temperature sensitive fertility defect."
FT /evidence="ECO:0000269|PubMed:16143610"
FT MUTAGEN 302
FT /note="G->E: In eb118; defect in spermatogenesis.
FT Temperature sensitive fertility defect."
FT /evidence="ECO:0000269|PubMed:16143610"
SQ SEQUENCE 351 AA; 41431 MW; 59E5B1D5440A2F56 CRC64;
MSWYSKIYVA VREYRAKHKI TGWILTRCLN VLLFIQLILL WWSLYMYVTV TIGYYVQSTI
QATIYLIVGS FLFVMSMWSL AKTLFTRVGR VPERYRPSKE LEDRLKAVTP MEKNRYVVEK
STPEQLAQQN TILEEMCTYC KVVVAECDQV GRLKYCYECG HIKPDRARHC SSCGKCCIKY
DHHCPWINMC VTHVNYKYFL LYIIYTSFLV YWYLLTSLEG AVRYFINQQW TDELGKFLFY
LFSFIVGGVF GYYPLGELII FHYQLISLNE TTVEQTKPAL LRFDNAADYN MGKYNNFQSV
FGWGLWLCPI DSSTQDGLHF DIRYVNTQQR NRFVRIEEEP SSTQSSQSSI Q
