ID   BSPRY_HUMAN             Reviewed;         402 AA.
AC   Q5W0U4; B3KS19; Q96DJ2; Q9H4E4; Q9NXN0;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   24-JAN-2024, entry version 150.
DE   RecName: Full=B box and SPRY domain-containing protein;
GN   Name=BSPRY;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-374.
RC   TISSUE=Placenta;
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 GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Colon;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-374.
RC   TISSUE=Colon, and Prostate;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
CC   -!- FUNCTION: May regulate epithelial calcium transport by inhibiting TRPV5
CC       activity. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with TRPV5 and TRPV6. Interacts with YWHAZ/14-3-3
CC       protein zeta (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5W0U4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5W0U4-2; Sequence=VSP_019527, VSP_019528;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA90980.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ276691; CAC09324.1; -; mRNA.
DR   EMBL; AL137066; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471090; EAW87374.1; -; Genomic_DNA.
DR   EMBL; BC001477; AAH01477.1; -; mRNA.
DR   EMBL; AK000157; BAA90980.1; ALT_INIT; mRNA.
DR   EMBL; AK092607; BAG52581.1; -; mRNA.
DR   CCDS; CCDS43868.1; -. [Q5W0U4-1]
DR   RefSeq; NP_001304872.1; NM_001317943.1.
DR   RefSeq; NP_001304873.1; NM_001317944.1. [Q5W0U4-2]
DR   RefSeq; NP_060158.2; NM_017688.2. [Q5W0U4-1]
DR   AlphaFoldDB; Q5W0U4; -.
DR   SMR; Q5W0U4; -.
DR   BioGRID; 120188; 36.
DR   IntAct; Q5W0U4; 27.
DR   MINT; Q5W0U4; -.
DR   STRING; 9606.ENSP00000363298; -.
DR   iPTMnet; Q5W0U4; -.
DR   PhosphoSitePlus; Q5W0U4; -.
DR   BioMuta; BSPRY; -.
DR   DMDM; 74747982; -.
DR   EPD; Q5W0U4; -.
DR   jPOST; Q5W0U4; -.
DR   MassIVE; Q5W0U4; -.
DR   MaxQB; Q5W0U4; -.
DR   PaxDb; 9606-ENSP00000363298; -.
DR   PeptideAtlas; Q5W0U4; -.
DR   ProteomicsDB; 65776; -. [Q5W0U4-1]
DR   ProteomicsDB; 65777; -. [Q5W0U4-2]
DR   Pumba; Q5W0U4; -.
DR   Antibodypedia; 29777; 68 antibodies from 12 providers.
DR   DNASU; 54836; -.
DR   Ensembl; ENST00000374183.5; ENSP00000363298.4; ENSG00000119411.11. [Q5W0U4-1]
DR   GeneID; 54836; -.
DR   KEGG; hsa:54836; -.
DR   MANE-Select; ENST00000374183.5; ENSP00000363298.4; NM_017688.3; NP_060158.2.
DR   UCSC; uc004bhg.5; human. [Q5W0U4-1]
DR   AGR; HGNC:18232; -.
DR   CTD; 54836; -.
DR   GeneCards; BSPRY; -.
DR   HGNC; HGNC:18232; BSPRY.
DR   HPA; ENSG00000119411; Tissue enriched (parathyroid).
DR   MIM; 619683; gene.
DR   neXtProt; NX_Q5W0U4; -.
DR   OpenTargets; ENSG00000119411; -.
DR   PharmGKB; PA134979106; -.
DR   VEuPathDB; HostDB:ENSG00000119411; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000161096; -.
DR   HOGENOM; CLU_050384_0_0_1; -.
DR   InParanoid; Q5W0U4; -.
DR   OMA; HESELDW; -.
DR   OrthoDB; 5296458at2759; -.
DR   PhylomeDB; Q5W0U4; -.
DR   TreeFam; TF351014; -.
DR   PathwayCommons; Q5W0U4; -.
DR   SignaLink; Q5W0U4; -.
DR   BioGRID-ORCS; 54836; 19 hits in 1145 CRISPR screens.
DR   ChiTaRS; BSPRY; human.
DR   GenomeRNAi; 54836; -.
DR   Pharos; Q5W0U4; Tdark.
DR   PRO; PR:Q5W0U4; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q5W0U4; Protein.
DR   Bgee; ENSG00000119411; Expressed in parotid gland and 155 other cell types or tissues.
DR   GO; GO:0031252; C:cell leading edge; IEA:Ensembl.
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; IEA:Ensembl.
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:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   CDD; cd19834; Bbox2_BSPRY; 1.
DR   CDD; cd12904; SPRY_BSPRY; 1.
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.
DR   Genevisible; Q5W0U4; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Calcium transport; Cytoplasm; Ion transport;
KW   Membrane; Metal-binding; Reference proteome; Transport; Zinc; Zinc-finger.
FT   CHAIN           1..402
FT                   /note="B box and SPRY domain-containing protein"
FT                   /id="PRO_0000244257"
FT   DOMAIN          212..402
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         17..65
FT                   /note="B box-type"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         187..193
FT                   /note="TEEAEGI -> HRGHTDR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_019527"
FT   VAR_SEQ         194..402
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_019528"
FT   VARIANT         261
FT                   /note="A -> P (in dbSNP:rs34089316)"
FT                   /id="VAR_048397"
FT   VARIANT         293
FT                   /note="Q -> H (in dbSNP:rs818711)"
FT                   /id="VAR_026882"
FT   VARIANT         374
FT                   /note="T -> I (in dbSNP:rs3088235)"
FT                   /evidence="ECO:0000269|PubMed:10978534,
FT                   ECO:0000269|PubMed:14702039"
FT                   /id="VAR_026883"
FT   CONFLICT        100
FT                   /note="V -> E (in Ref. 5; BAA90980)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   402 AA;  44381 MW;  EEBBB95B0A9863F4 CRC64;
     MSAEGAEPGP GSGSGPGPGP LCPEHGQALS WFCGSERRPV CAACAGLGGR CRGHRIRRAE
     ERAEELRNKI VDQCERLQLQ SAAITKYVAD VLPGKNQRAV SMASAARELV IQRLSLVRSL
     CESEEQRLLE QVHGEEERAH QSILTQRVHW AEALQKLDTI RTGLVGMLTH LDDLQLIQKE
     QEIFERTEEA EGILDPQESE MLNFNEKCTR SPLLTQLWAT AVLGSLSGTE DIRIDERTVS
     PFLQLSDDRK TLTFSTKKSK ACADGPERFD HWPNALAATS FQNGLHAWMV NVQNSCAYKV
     GVASGHLPRK GSGSDCRLGH NAFSWVFSRY DQEFRFSHNG QHEPLGLLRG PAQLGVVLDL
     QVQELLFYEP ASGTVLCAHH VSFPGPLFPV FAVADQTISI VR
//