SPE39_CAEEL
ID SPE39_CAEEL Reviewed; 522 AA.
AC Q23288;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Spermatogenesis-defective protein 39;
DE Short=SPE-39;
DE AltName: Full=VPS33B-interacting protein in polarity and apical restriction;
GN Name=spe-39; Synonyms=vipar; ORFNames=ZC404.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=14504223; DOI=10.1093/genetics/165.1.145;
RA Zhu G.D., L'Hernault S.W.;
RT "The Caenorhabditis elegans spe-39 gene is required for intracellular
RT membrane reorganization during spermatogenesis.";
RL Genetics 165:145-157(2003).
RN [3]
RP DISRUPTION PHENOTYPE, FUNCTION, AND INTERACTION WITH VPS-33.1 AND VPS-33.2.
RX PubMed=19109425; DOI=10.1091/mbc.e08-07-0728;
RA Zhu G.D., Salazar G., Zlatic S.A., Fiza B., Doucette M.M., Heilman C.J.,
RA Levey A.I., Faundez V., L'hernault S.W.;
RT "SPE-39 family proteins interact with the HOPS complex and function in
RT lysosomal delivery.";
RL Mol. Biol. Cell 20:1223-1240(2009).
CC -!- FUNCTION: Proposed to be involved in endosomal maturation implicating
CC in part vps-33.2. May play a role in epithelial polarization through
CC stabilization of apical membrane protein content. May play a role in
CC transcriptional regulation (By similarity). Plays a role in lysosomal
CC trafficking, probably via association with the core HOPS complex in a
CC discrete population of endosomes. Essential for vesicular trafficking
CC during spermatogenesis; required during spermiogenesis or sperm
CC activation for the morphogenesis of specialized Golgi-derived fibrous
CC body-membranous organelle (FB-MO) complexes. Required for the
CC processing of internalized proteins in oocytes and coelomocytes.
CC {ECO:0000250|UniProtKB:Q9H9C1, ECO:0000269|PubMed:14504223,
CC ECO:0000269|PubMed:19109425}.
CC -!- SUBUNIT: Interacts with vps-33.1 and vps-33.2 (PubMed:19109425).
CC Associates with the homotypic fusion and vacuole protein sorting (HOPS)
CC complex, impaired by vps-33.2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H9C1, ECO:0000269|PubMed:19109425}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14504223}.
CC Cytoplasmic vesicle {ECO:0000250}. Early endosome
CC {ECO:0000250|UniProtKB:Q9H9C1}. Recycling endosome
CC {ECO:0000250|UniProtKB:Q9H9C1}. Late endosome
CC {ECO:0000250|UniProtKB:Q9H9C1}. Note=Localizes in both residual bodies
CC and budding spermatids (PubMed:14504223).
CC {ECO:0000269|PubMed:14504223}.
CC -!- TISSUE SPECIFICITY: Expressed in spermatocytes and spermatids (at
CC protein level).
CC -!- DEVELOPMENTAL STAGE: Expressed in the embryonic testis.
CC -!- DISRUPTION PHENOTYPE: Mutants produce spermatocytes that complete
CC meiosis but do not usually form functional. Show defective vesicular
CC biogenesis during spermatogenesis with morphogenesis failure of the
CC specialized Golgi-derived fibrous body-membranous organelle (FB-MO)
CC complexes. Show disrupted processing of endocytosed proteins in oocytes
CC and coelomocytes. {ECO:0000269|PubMed:14504223,
CC ECO:0000269|PubMed:19109425}.
CC -!- SIMILARITY: Belongs to the SPE39 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FO081573; CCD72490.1; -; Genomic_DNA.
DR PIR; T29370; T29370.
DR RefSeq; NP_504718.1; NM_072317.4.
DR AlphaFoldDB; Q23288; -.
DR BioGRID; 44116; 3.
DR IntAct; Q23288; 2.
DR STRING; 6239.ZC404.3a; -.
DR EPD; Q23288; -.
DR PaxDb; Q23288; -.
DR EnsemblMetazoa; ZC404.3a.1; ZC404.3a.1; WBGene00004975.
DR GeneID; 179071; -.
DR KEGG; cel:CELE_ZC404.3; -.
DR UCSC; ZC404.3a; c. elegans.
DR CTD; 179071; -.
DR WormBase; ZC404.3a; CE07594; WBGene00004975; spe-39.
DR eggNOG; KOG4677; Eukaryota.
DR GeneTree; ENSGT00390000013955; -.
DR HOGENOM; CLU_491120_0_0_1; -.
DR InParanoid; Q23288; -.
DR OMA; PEMVIEC; -.
DR OrthoDB; 534116at2759; -.
DR PhylomeDB; Q23288; -.
DR PRO; PR:Q23288; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004975; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q23288; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0055037; C:recycling endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0048477; P:oogenesis; IMP:WormBase.
DR GO; GO:0007286; P:spermatid development; IMP:WormBase.
DR GO; GO:0006624; P:vacuolar protein processing; IMP:WormBase.
DR GO; GO:0007034; P:vacuolar transport; IMP:WormBase.
DR InterPro; IPR040057; Spe-39.
DR PANTHER; PTHR13364; PTHR13364; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoplasmic vesicle; Differentiation; Endosome;
KW Protein transport; Reference proteome; Spermatogenesis; Transcription;
KW Transcription regulation; Transport.
FT CHAIN 1..522
FT /note="Spermatogenesis-defective protein 39"
FT /id="PRO_0000395737"
FT REGION 47..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 59507 MW; 16816064C7345E55 CRC64;
MALRRKFTFE LPEDSYWNES DSNSSGLFDD LQSKQLQARA AVDNLFGGDE TPKPYVRPQN
PTPTPTNVPL QIDGRAAAVS DKANIRITDT SPRASGKIVD DFLNMKFAEN VNVAPVIQTA
PSVVSEASAS SLPSEAQRLD LDYNRLRQEH RKLKDQHEVL RHERFQPLTI EASIKRMLQG
HTVTLDYYRS LRDKTQLLKQ AVATYDNNTI FKIVIFLERT LKENIFCKIM DGQKSACRVY
TRHLQITGEW DKMNKFLRSI GQYQHASVIE FEATRKYKRN PDKRVPLLRT MLHGSFSIPE
MKFEARQMEA LMRNYEIQLQ MEKMDAGDKG EHFRKFPKTS SLIGLPALSS LYYSAMYHYD
DSPTSAASLP SVQTLIRFND RLATQTIVSA LTRLSRWPDI DKLLQPKTIT MTFSAAKSVF
KGKKSTSKWG VSINNHNLLT IVKRSHPSPP TDFIYRILKG ESDAQERLRL ALLFDVPEMV
IECLTQKGDR LSLASYAKSL KTNSVESFKA VAALNNPSIK WK