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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}.
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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
 
 
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