SPE39_MOUSE
ID SPE39_MOUSE Reviewed; 491 AA.
AC Q8BGQ1; Q8BL55; Q8CIK4; Q91YI3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, Cerebellum, Diencephalon, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21; THR-115; SER-119 AND
RP SER-122, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION, INTERACTION WITH RAB11A, AND KNOCKDOWN.
RX PubMed=20190753; DOI=10.1038/ng.538;
RA Cullinane A.R., Straatman-Iwanowska A., Zaucker A., Wakabayashi Y.,
RA Bruce C.K., Luo G., Rahman F., Gurakan F., Utine E., Ozkan T.B.,
RA Denecke J., Vukovic J., Di Rocco M., Mandel H., Cangul H., Matthews R.P.,
RA Thomas S.G., Rappoport J.Z., Arias I.M., Wolburg H., Knisely A.S.,
RA Kelly D.A., Muller F., Maher E.R., Gissen P.;
RT "Mutations in VIPAR cause an arthrogryposis, renal dysfunction and
RT cholestasis syndrome phenotype with defects in epithelial polarization.";
RL Nat. Genet. 42:303-312(2010).
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 (PubMed:20190753). May
CC play a role in lysosomal trafficking, probably via association with the
CC core HOPS complex in a discrete population of endosomes; the functions
CC seems to be independent of VPS33B (By similarity). May play a role in
CC vesicular trafficking during spermatogenesis (By similarity). May be
CC involved in direct or indirect transcriptional regulation of E-
CC cadherin. {ECO:0000250|UniProtKB:Q23288, ECO:0000250|UniProtKB:Q9H9C1,
CC ECO:0000269|PubMed:20190753}.
CC -!- SUBUNIT: Interacts with VPS33B. Associates with the homotypic fusion
CC and vacuole protein sorting (HOPS) complex; impaired by VPS33B (By
CC similarity). Interacts with RAB11A (PubMed:20190753).
CC {ECO:0000250|UniProtKB:Q9H9C1, ECO:0000269|PubMed:20190753}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BGQ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BGQ1-2; Sequence=VSP_009285;
CC -!- MISCELLANEOUS: Vipar-deficient inner medullary collecting duct cells
CC display abnormal expression of membrane proteins such as Ceacam5,
CC structural and functional tight junction defects and reduced E-cadherin
CC expression.
CC -!- SIMILARITY: Belongs to the SPE39 family. {ECO:0000305}.
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DR EMBL; AK046322; BAC32680.1; -; mRNA.
DR EMBL; AK049643; BAC33854.1; -; mRNA.
DR EMBL; AK079055; BAC37516.1; -; mRNA.
DR EMBL; AK082261; BAC38449.1; -; mRNA.
DR EMBL; BC016646; AAH16646.1; -; mRNA.
DR EMBL; BC023716; AAH23716.1; -; mRNA.
DR CCDS; CCDS26074.1; -. [Q8BGQ1-2]
DR CCDS; CCDS49119.1; -. [Q8BGQ1-1]
DR RefSeq; NP_001136052.1; NM_001142580.1. [Q8BGQ1-1]
DR RefSeq; NP_001136053.1; NM_001142581.1. [Q8BGQ1-2]
DR RefSeq; NP_598805.2; NM_134044.3. [Q8BGQ1-2]
DR RefSeq; XP_006515402.1; XM_006515339.3. [Q8BGQ1-1]
DR RefSeq; XP_011242278.1; XM_011243976.2. [Q8BGQ1-1]
DR AlphaFoldDB; Q8BGQ1; -.
DR SMR; Q8BGQ1; -.
DR BioGRID; 222705; 4.
DR IntAct; Q8BGQ1; 1.
DR MINT; Q8BGQ1; -.
DR STRING; 10090.ENSMUSP00000072527; -.
DR iPTMnet; Q8BGQ1; -.
DR PhosphoSitePlus; Q8BGQ1; -.
DR EPD; Q8BGQ1; -.
DR jPOST; Q8BGQ1; -.
DR MaxQB; Q8BGQ1; -.
DR PaxDb; Q8BGQ1; -.
DR PeptideAtlas; Q8BGQ1; -.
DR PRIDE; Q8BGQ1; -.
DR ProteomicsDB; 257342; -. [Q8BGQ1-1]
DR ProteomicsDB; 257343; -. [Q8BGQ1-2]
DR Antibodypedia; 26048; 126 antibodies from 22 providers.
DR DNASU; 104799; -.
DR Ensembl; ENSMUST00000021426; ENSMUSP00000021426; ENSMUSG00000021038. [Q8BGQ1-2]
DR Ensembl; ENSMUST00000072744; ENSMUSP00000072527; ENSMUSG00000021038. [Q8BGQ1-1]
DR Ensembl; ENSMUST00000179379; ENSMUSP00000137190; ENSMUSG00000021038. [Q8BGQ1-2]
DR GeneID; 104799; -.
DR KEGG; mmu:104799; -.
DR UCSC; uc007oip.2; mouse. [Q8BGQ1-2]
DR UCSC; uc007oiq.2; mouse. [Q8BGQ1-1]
DR CTD; 63894; -.
DR MGI; MGI:2144805; Vipas39.
DR VEuPathDB; HostDB:ENSMUSG00000021038; -.
DR eggNOG; KOG4677; Eukaryota.
DR GeneTree; ENSGT00390000013955; -.
DR HOGENOM; CLU_029487_0_0_1; -.
DR InParanoid; Q8BGQ1; -.
DR OMA; QIQSTLY; -.
DR OrthoDB; 812306at2759; -.
DR PhylomeDB; Q8BGQ1; -.
DR TreeFam; TF319640; -.
DR BioGRID-ORCS; 104799; 8 hits in 71 CRISPR screens.
DR ChiTaRS; Vipas39; mouse.
DR PRO; PR:Q8BGQ1; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BGQ1; protein.
DR Bgee; ENSMUSG00000021038; Expressed in saccule of membranous labyrinth and 253 other tissues.
DR Genevisible; Q8BGQ1; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005770; C:late endosome; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0099023; C:vesicle tethering complex; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030199; P:collagen fibril organization; IMP:MGI.
DR GO; GO:0032963; P:collagen metabolic process; IMP:MGI.
DR GO; GO:0008333; P:endosome to lysosome transport; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IMP:MGI.
DR GO; GO:0017185; P:peptidyl-lysine hydroxylation; IMP:MGI.
DR GO; GO:0043687; P:post-translational protein modification; IMP:MGI.
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 InterPro; IPR006925; Vps16_C.
DR PANTHER; PTHR13364; PTHR13364; 1.
DR Pfam; PF04840; Vps16_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoplasmic vesicle; Differentiation;
KW Endosome; Phosphoprotein; Protein transport; Reference proteome;
KW Spermatogenesis; Transcription; Transcription regulation; Transport.
FT CHAIN 1..491
FT /note="Spermatogenesis-defective protein 39 homolog"
FT /id="PRO_0000089936"
FT REGION 72..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:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 115
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
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"
FT VAR_SEQ 148..166
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009285"
FT CONFLICT 131
FT /note="P -> R (in Ref. 1; BAC32680)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="I -> V (in Ref. 2; AAH16646)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 56625 MW; 7F143EAA3D009E9A CRC64;
MNRTKGDEEE YWNSSKFKAF TFDDEDDELS QLKESKRAVN SLRDIVDDDD DDDLERVSWT
GEPVGSISWS IKETAGSSGS TPEGREQLKG RNSFYTQLPK PPSTYSLSSF FRGRTRPGSF
QSLSDALSDT PAKSYAPELG RPKGEYRDYS NDWSLSDTVQ RLRRGKVCSL ERFRSLQDKL
QLLEEAVSMH DGNVITAVLI FLKRTLSKEI LFRELEVRQV ALRHLIHFLK EIGDQKLLLD
LFRFLDRAEE LALSHYREHL NIQDPEKRKE FLKTCIGLPF SAEDAAHVQD HYTLLERQII
IEANDRHLES SGQTDIFRKH PRKASILNMP LVTTLFYACF YHYTESEGTF SSPINLKKTF
KIPDKQYVLT ALAARAKLRA WNDVDALFTT KNWLGYTKKR APIGFHRVVE ILHKNSAPVQ
ILQEYVNLVE DVDTKLNLAT KFKCHDVVID TCRDLKDRQQ LLAYRSKVDK GSAEEEKIDA
ILSSSQIRWK N
