SPE39_RAT
ID SPE39_RAT Reviewed; 460 AA.
AC Q5PQN6;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Spermatogenesis-defective protein 39 homolog;
DE Short=hSPE-39;
DE AltName: Full=VPS33B-interacting protein in apical-basolateral polarity regulator;
DE AltName: Full=VPS33B-interacting protein in polarity and apical restriction;
GN Name=Vipas39; Synonyms=Spe39, Vipar;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-122, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Proposed to be involved in endosomal maturation implicating
CC in part VPS33B. In epithelial cells, the VPS33B:VIPAS39 complex may
CC play a role in the apical RAB11A-dependent recycling pathway and in the
CC maintenance of the apical-basolateral polarity. May play a role in
CC lysosomal trafficking, probably via association with the core HOPS
CC complex in a discrete population of endosomes; the functions seems to
CC be independent of VPS33B. May play a role in vesicular trafficking
CC during spermatogenesis. May be involved in direct or indirect
CC transcriptional regulation of E-cadherin (By similarity).
CC {ECO:0000250|UniProtKB:Q23288, ECO:0000250|UniProtKB:Q9H9C1}.
CC -!- SUBUNIT: Interacts with VPS33B. Associates with the homotypic fusion
CC and vacuole protein sorting (HOPS) complex; impaired by VPS33B.
CC Interacts with RAB11A (By similarity). {ECO:0000250|UniProtKB:Q8BGQ1,
CC ECO:0000250|UniProtKB:Q9H9C1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle
CC {ECO:0000250}. Early endosome {ECO:0000250|UniProtKB:Q9H9C1}. Recycling
CC endosome {ECO:0000250|UniProtKB:Q9H9C1}. Late endosome
CC {ECO:0000250|UniProtKB:Q9H9C1}. Note=Colocalizes in clusters with
CC VPS33B at cytoplasmic organelles. {ECO:0000250|UniProtKB:Q9H9C1}.
CC -!- SIMILARITY: Belongs to the SPE39 family. {ECO:0000305}.
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DR EMBL; BC087099; AAH87099.1; -; mRNA.
DR RefSeq; NP_001094474.1; NM_001101004.1.
DR AlphaFoldDB; Q5PQN6; -.
DR SMR; Q5PQN6; -.
DR IntAct; Q5PQN6; 3.
DR STRING; 10116.ENSRNOP00000066883; -.
DR iPTMnet; Q5PQN6; -.
DR PhosphoSitePlus; Q5PQN6; -.
DR jPOST; Q5PQN6; -.
DR PaxDb; Q5PQN6; -.
DR PRIDE; Q5PQN6; -.
DR Ensembl; ENSRNOT00000073428; ENSRNOP00000066883; ENSRNOG00000049223.
DR GeneID; 681989; -.
DR KEGG; rno:681989; -.
DR CTD; 63894; -.
DR RGD; 1589291; Vipas39.
DR eggNOG; KOG4677; Eukaryota.
DR GeneTree; ENSGT00390000013955; -.
DR InParanoid; Q5PQN6; -.
DR PhylomeDB; Q5PQN6; -.
DR PRO; PR:Q5PQN6; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000049223; Expressed in heart and 20 other tissues.
DR ExpressionAtlas; Q5PQN6; baseline and differential.
DR Genevisible; Q5PQN6; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005768; C:endosome; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0055037; C:recycling endosome; ISO:RGD.
DR GO; GO:0099023; C:vesicle tethering complex; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR GO; GO:0032963; P:collagen metabolic process; ISO:RGD.
DR GO; GO:0008333; P:endosome to lysosome transport; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; ISO:RGD.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; ISO:RGD.
DR GO; GO:0043687; P:post-translational protein modification; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
DR GO; GO:0007034; P:vacuolar transport; IBA:GO_Central.
DR InterPro; IPR040057; Spe-39.
DR PANTHER; PTHR13364; PTHR13364; 2.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoplasmic vesicle; Differentiation; Endosome; Phosphoprotein;
KW Protein transport; Reference proteome; Spermatogenesis; Transcription;
KW Transcription regulation; Transport.
FT CHAIN 1..460
FT /note="Spermatogenesis-defective protein 39 homolog"
FT /id="PRO_0000395736"
FT REGION 70..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9C1"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGQ1"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9C1"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9C1"
SQ SEQUENCE 460 AA; 53305 MW; 1AC52D2501E78E22 CRC64;
MNRTKGDEEE YWNSSKFKAF TFDDEDDELS QLKESKRAVN SLRDFVDDDD DDDLERVSWT
GEPVGSISWS IKETAGSSGS TSEGREQMKG RNSFYTQLPK PPSTYSLSSF FRGRTRPGSF
QSLSDALSDT PAKTYSPELG RPKGEYRDYS NDWSLSDTVR RLRQGKVLIF LKRTLSKEIL
FRELEVRQVA LRHLIHFLKE IGDQKLLLDL FRFLDRTEEL ALSHYREHLN IQDPEKRKEF
LKTCIGLPFS AEDSAHVQDQ YTLLERQIII EANDRHLESS GQTEIFRKHP RKASILNMPL
VTTLFYACFY HYTESEGTFS SPVNLKKTFK IPDRQYVLTA LAARAKLRAW NDVDALFTTK
NWLGYTKKRA PIGFHRVVEI LHKNSAPVQI LQEYVNLVED VDTKLNLATK FKCHDVVIDT
CRDLKDRQQL LAYRSKVDKG SAEEEKIDVI LSSSQIRWKN
