Q8BGQ1 (SPE39_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Spermatogenesis-defective protein 39 homolog
Short name=hSPE-39

Alternative name(s):
VPS33B-interacting protein in apical-basolateral polarity regulator
VPS33B-interacting protein in polarity and apical restriction

Gene names

Name:	Vipas39
Synonyms:	Spe39, Vipar

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	491 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Plays a role in lysosomal trafficking, probably via association with the core HOPS complex in a discrete population of endosomes. May play a role in vesicular trafficking during spermatogenesis By similarity. May play a role in epithelial polarization through stabilization of apical membrane protein content, possibly via the RAB11A-dependent apical recycling pathway. Also involved in direct or indirect transcriptional regulation of E-cadherin. Ref.6
Subunit structure	Associates with the homotypic fusion and vacuole protein sorting (HOPS) complex By similarity. Interacts with VPS33A and VPS33B By similarity. Interacts with RAB11A. Ref.6
Subcellular location	Cytoplasm By similarity. Cytoplasmic vesicle By similarity. Early endosome By similarity. Recycling endosome By similarity. Late endosome By similarity. Note: Colocalizes in clusters with VPS33B at cytoplasmic organelles By similarity.
Miscellaneous	Vipar-deficient inner medullary collecting duct cells display abnormal expression of membrane proteins such as Ceacam5, structural and functional tight junction defects and reduced E-cadherin expression.
Sequence similarities	Belongs to the SPE39 family.

Ontologies

Keywords
Biological process	Differentiation Protein transport Spermatogenesis Transcription Transcription regulation Transport
Cellular component	Cytoplasm Cytoplasmic vesicle Endosome
Coding sequence diversity	Alternative splicing
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW endosome to lysosome transport Inferred from electronic annotation. Source: Compara intracellular protein transport Inferred from electronic annotation. Source: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW spermatogenesis Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	HOPS complex Inferred from electronic annotation. Source: Compara cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell early endosome Inferred from electronic annotation. Source: UniProtKB-SubCell late endosome Inferred from electronic annotation. Source: UniProtKB-SubCell recycling endosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8BGQ1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q8BGQ1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     148-166: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 491	491	Spermatogenesis-defective protein 39 homolog		PRO_0000089936
Amino acid modifications
	Modified residue	21	1	Phosphothreonine Ref.3
	Modified residue	119	1	Phosphoserine Ref.4 Ref.5
	Modified residue	122	1	Phosphoserine Ref.4
	Modified residue	130	1	Phosphothreonine By similarity
Natural variations
	Alternative sequence	148 – 166	19	Missing in isoform 2.		VSP_009285
Experimental info
	Sequence conflict	131	1	P → R in BAC32680. Ref.1
	Sequence conflict	316	1	I → V in AAH16646. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 7F143EAA3D009E9A	FASTA	491	56,625
	10 20 30 40 50 60 MNRTKGDEEE YWNSSKFKAF TFDDEDDELS QLKESKRAVN SLRDIVDDDD DDDLERVSWT 70 80 90 100 110 120 GEPVGSISWS IKETAGSSGS TPEGREQLKG RNSFYTQLPK PPSTYSLSSF FRGRTRPGSF 130 140 150 160 170 180 QSLSDALSDT PAKSYAPELG RPKGEYRDYS NDWSLSDTVQ RLRRGKVCSL ERFRSLQDKL 190 200 210 220 230 240 QLLEEAVSMH DGNVITAVLI FLKRTLSKEI LFRELEVRQV ALRHLIHFLK EIGDQKLLLD 250 260 270 280 290 300 LFRFLDRAEE LALSHYREHL NIQDPEKRKE FLKTCIGLPF SAEDAAHVQD HYTLLERQII 310 320 330 340 350 360 IEANDRHLES SGQTDIFRKH PRKASILNMP LVTTLFYACF YHYTESEGTF SSPINLKKTF 370 380 390 400 410 420 KIPDKQYVLT ALAARAKLRA WNDVDALFTT KNWLGYTKKR APIGFHRVVE ILHKNSAPVQ 430 440 450 460 470 480 ILQEYVNLVE DVDTKLNLAT KFKCHDVVID TCRDLKDRQQ LLAYRSKVDK GSAEEEKIDA 490 ILSSSQIRWK N
	Isoform 2 [UniParc]. Checksum: 206D86D3E1C5781E	FASTA	472	54,347
	10 20 30 40 50 60 MNRTKGDEEE YWNSSKFKAF TFDDEDDELS QLKESKRAVN SLRDIVDDDD DDDLERVSWT 70 80 90 100 110 120 GEPVGSISWS IKETAGSSGS TPEGREQLKG RNSFYTQLPK PPSTYSLSSF FRGRTRPGSF 130 140 150 160 170 180 QSLSDALSDT PAKSYAPELG RPKGEYRVCS LERFRSLQDK LQLLEEAVSM HDGNVITAVL 190 200 210 220 230 240 IFLKRTLSKE ILFRELEVRQ VALRHLIHFL KEIGDQKLLL DLFRFLDRAE ELALSHYREH 250 260 270 280 290 300 LNIQDPEKRK EFLKTCIGLP FSAEDAAHVQ DHYTLLERQI IIEANDRHLE SSGQTDIFRK 310 320 330 340 350 360 HPRKASILNM PLVTTLFYAC FYHYTESEGT FSSPINLKKT FKIPDKQYVL TALAARAKLR 370 380 390 400 410 420 AWNDVDALFT TKNWLGYTKK RAPIGFHRVV EILHKNSAPV QILQEYVNLV EDVDTKLNLA 430 440 450 460 470 TKFKCHDVVI DTCRDLKDRQ QLLAYRSKVD KGSAEEEKID AILSSSQIRW KN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Brain, Cerebellum, Diencephalon and Spinal cord.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: FVB/N. Tissue: Mammary tumor.
[3]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-21, MASS SPECTROMETRY. Tissue: Embryonic brain.
[4]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119 AND SER-122, MASS SPECTROMETRY. Tissue: Liver.
[5]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, MASS SPECTROMETRY. Tissue: Melanoma.
[6]	"Mutations in VIPAR cause an arthrogryposis, renal dysfunction and cholestasis syndrome phenotype with defects in epithelial polarization." Cullinane A.R., Straatman-Iwanowska A., Zaucker A., Wakabayashi Y., Bruce C.K., Luo G., Rahman F., Gurakan F., Utine E., Ozkan T.B., Denecke J., Vukovic J., Di Rocco M., Mandel H., Cangul H., Matthews R.P., Thomas S.G., Rappoport J.Z. , Arias I.M., Wolburg H., Knisely A.S., Kelly D.A., Muller F., Maher E.R., Gissen P. Nat. Genet. 42:303-312(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH RAB11A, KNOCKDOWN.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK046322 mRNA. Translation: BAC32680.1. AK049643 mRNA. Translation: BAC33854.1. AK079055 mRNA. Translation: BAC37516.1. AK082261 mRNA. Translation: BAC38449.1. BC016646 mRNA. Translation: AAH16646.1. BC023716 mRNA. Translation: AAH23716.1.
IPI	IPI00229865. IPI00400395.
RefSeq	NP_001136052.1. NM_001142580.1. NP_001136053.1. NM_001142581.1. NP_598805.2. NM_134044.3.
UniGene	Mm.208750.
3D structure databases
ProteinModelPortal	Q8BGQ1.
ModBase	Search...
PTM databases
PhosphoSite	Q8BGQ1.
Proteomic databases
PaxDb	Q8BGQ1.
PRIDE	Q8BGQ1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000021426; ENSMUSP00000021426; ENSMUSG00000021038. ENSMUST00000072744; ENSMUSP00000072527; ENSMUSG00000021038. ENSMUST00000179379; ENSMUSP00000137190; ENSMUSG00000021038.
GeneID	104799.
KEGG	mmu:104799.
UCSC	uc007oip.2. mouse. uc007oiq.2. mouse.
Organism-specific databases
CTD	63894.
MGI	MGI:2144805. Vipas39.
Phylogenomic databases
eggNOG	NOG147553.
GeneTree	ENSGT00390000013955.
HOGENOM	HOG000070044.
HOVERGEN	HBG051031.
InParanoid	Q8BGQ1.
OMA	CFYHYTE.
OrthoDB	EOG4FXR7Q.
Gene expression databases
Bgee	Q8BGQ1.
CleanEx	MM_AI413782.
Genevestigator	Q8BGQ1.
GermOnline	ENSMUSG00000021038. Mus musculus.
Family and domain databases
InterPro	IPR019177. Golgin_subfamily_A_member_5. [Graphical view]
Pfam	PF09787. Golgin_A5. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	357292.
SOURCE	Search...

Entry information

Entry name

SPE39_MOUSE

Accession

Primary (citable) accession number: Q8BGQ1
Secondary accession number(s): Q8BL55, Q8CIK4, Q91YI3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	March 1, 2003
Last modified:	April 3, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program