ID BSPRY_MOUSE Reviewed; 473 AA.
AC Q80YW5; Q3TU74; Q8BZF0; Q99KV7; Q9ER70;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 24-JAN-2024, entry version 140.
DE RecName: Full=B box and SPRY domain-containing protein;
GN Name=Bspry;
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 [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=10978534; DOI=10.1016/s0167-4781(00)00167-6;
RA Schenker T., Trueb B.;
RT "BSPRY, a novel protein of the Ro-Ret family.";
RL Biochim. Biophys. Acta 1493:255-258(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RC TISSUE=Extraembryonic tissue, Placenta, and Urinary bladder;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 145-473 (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary gland;
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 [5]
RP DEVELOPMENTAL STAGE.
RX PubMed=12615066; DOI=10.1016/s0006-291x(03)00182-7;
RA Birkenfeld J., Kartmann B., Anliker B., Ono K., Schloetcke B., Betz H.,
RA Roth D.;
RT "Characterization of zetin 1/rBSPRY, a novel binding partner of 14-3-3
RT proteins.";
RL Biochem. Biophys. Res. Commun. 302:526-533(2003).
RN [6]
RP INTERACTION WITH TRPV5 AND TRPV6, TISSUE SPECIFICITY, FUNCTION, SUBCELLULAR
RP LOCATION, AND INDUCTION.
RX PubMed=16380433; DOI=10.1681/asn.2005101025;
RA van de Graaf S.F.J., van der Kemp A.W.C.M., van den Berg D.,
RA van Oorschot M., Hoenderop J.G.J., Bindels R.J.M.;
RT "Identification of BSPRY as a novel auxiliary protein inhibiting TRPV5
RT activity.";
RL J. Am. Soc. Nephrol. 17:26-30(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: May regulate epithelial calcium transport by inhibiting TRPV5
CC activity. {ECO:0000269|PubMed:16380433}.
CC -!- SUBUNIT: Interacts with YWHAZ/14-3-3 protein zeta (By similarity).
CC Interacts with TRPV5 and TRPV6. {ECO:0000250,
CC ECO:0000269|PubMed:16380433}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16380433}. Membrane
CC {ECO:0000269|PubMed:16380433}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16380433}. Note=Apical domain of kidney distal
CC tubular cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80YW5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80YW5-2; Sequence=VSP_019529;
CC -!- TISSUE SPECIFICITY: According to PubMed:10978534, testis-specific.
CC According to PubMed:16371431, broadly expressed.
CC {ECO:0000269|PubMed:10978534, ECO:0000269|PubMed:16380433}.
CC -!- DEVELOPMENTAL STAGE: Expression starts at 19 dpc in brain.
CC {ECO:0000269|PubMed:12615066}.
CC -!- INDUCTION: Down-regulated by vitamin D. {ECO:0000269|PubMed:16380433}.
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DR EMBL; AJ276690; CAC09325.1; -; mRNA.
DR EMBL; AK035588; BAC29115.1; -; mRNA.
DR EMBL; AK160930; BAE36097.1; -; mRNA.
DR EMBL; AL732594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003992; AAH03992.2; -; mRNA.
DR CCDS; CCDS18241.1; -. [Q80YW5-2]
DR CCDS; CCDS89757.1; -. [Q80YW5-1]
DR RefSeq; NP_619594.1; NM_138653.1. [Q80YW5-2]
DR AlphaFoldDB; Q80YW5; -.
DR SMR; Q80YW5; -.
DR BioGRID; 228643; 1.
DR IntAct; Q80YW5; 1.
DR MINT; Q80YW5; -.
DR STRING; 10090.ENSMUSP00000030088; -.
DR PhosphoSitePlus; Q80YW5; -.
DR SwissPalm; Q80YW5; -.
DR MaxQB; Q80YW5; -.
DR PaxDb; 10090-ENSMUSP00000030088; -.
DR ProteomicsDB; 265247; -. [Q80YW5-1]
DR ProteomicsDB; 265248; -. [Q80YW5-2]
DR Antibodypedia; 29777; 68 antibodies from 12 providers.
DR DNASU; 192120; -.
DR Ensembl; ENSMUST00000030088.12; ENSMUSP00000030088.6; ENSMUSG00000028392.16. [Q80YW5-2]
DR Ensembl; ENSMUST00000107449.4; ENSMUSP00000103073.4; ENSMUSG00000028392.16. [Q80YW5-1]
DR GeneID; 192120; -.
DR KEGG; mmu:192120; -.
DR UCSC; uc008tex.1; mouse. [Q80YW5-1]
DR AGR; MGI:2177191; -.
DR CTD; 54836; -.
DR MGI; MGI:2177191; Bspry.
DR VEuPathDB; HostDB:ENSMUSG00000028392; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000161096; -.
DR HOGENOM; CLU_050384_0_0_1; -.
DR InParanoid; Q80YW5; -.
DR OMA; HESELDW; -.
DR OrthoDB; 5296458at2759; -.
DR TreeFam; TF351014; -.
DR BioGRID-ORCS; 192120; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Bspry; mouse.
DR PRO; PR:Q80YW5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q80YW5; Protein.
DR Bgee; ENSMUSG00000028392; Expressed in spermatid and 130 other cell types or tissues.
DR ExpressionAtlas; Q80YW5; baseline and differential.
DR Genevisible; Q80YW5; MM.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0005499; F:vitamin D binding; IEA:UniProtKB-KW.
DR GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR PANTHER; PTHR24103:SF568; B BOX AND SPRY DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24103; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Calcium transport; Cytoplasm; Ion transport;
KW Membrane; Metal-binding; Reference proteome; Transport; Vitamin D; Zinc;
KW Zinc-finger.
FT CHAIN 1..473
FT /note="B box and SPRY domain-containing protein"
FT /id="PRO_0000244258"
FT DOMAIN 259..455
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 65..113
FT /note="B box-type"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 467..473
FT /note="RSGHASR -> SIRRTTCQDTVGQNVVVGVW (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10978534"
FT /id="VSP_019529"
FT CONFLICT 17
FT /note="E -> F (in Ref. 2; BAC29115)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="A -> D (in Ref. 2; BAE36097)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="C -> S (in Ref. 2; BAE36097)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 52751 MW; 60FBC4A61A8F4A8E CRC64;
MSADVSGTES GSESGPEPEP GPEPGPESRP ESRPKPGPGP EPRPESGPEP GPRSGLRRGP
KQGSERSQLC PEHFEPLSWF CLSERRPVCA TCAGFGGRCH RHRIRRAEEH AEELRNKIVD
QCERLQLQSA GISKYMAEVL QGKNQKAVVM ASAARDLIIQ RLSLVRSLCE SEEQRLLEQV
HGEEERAHQS ILTQRAHWVD AVQKLDTLRT NMVDMITHLD DLQLIQREQE IFERAEEAEG
ILDPQDSEKL SFNEKCAWSP LLTQLWAASV LGSLSGVEEV LIDERTVSPL LHLSEDRRTL
TFIAKKSKVC SDEPERFDHW PNALAATAFQ TGLHAWIVNV KHSCAYKVGV ASDQLPRKGS
GNDCRLGHNA FSWVFSRYDQ EFCFSHNGYH EPLPLLRCPA QLGMLLDLQA GELVFYEPAS
GTVLHIHRAS FPQVLFPVFA VADQLISIVR GPLATVRLDS PPHHPCRSGH ASR
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