ID   BSPRY_RAT               Reviewed;         448 AA.
AC   Q6P6S3; Q4VBG7; Q9JKB6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=B box and SPRY domain-containing protein;
DE   AltName: Full=Zetin-1;
GN   Name=Bspry;
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=Prostate, and Testis;
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   NUCLEOTIDE SEQUENCE [MRNA] OF 146-448, TISSUE SPECIFICITY, SUBCELLULAR
RP   LOCATION, AND INTERACTION WITH YWHAZ.
RC   TISSUE=Brain;
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).
CC   -!- FUNCTION: May regulate epithelial calcium transport by inhibiting TRPV5
CC       activity. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with TRPV5 and TRPV6 (By similarity). Interacts with
CC       YWHAZ/14-3-3 protein zeta. {ECO:0000250, ECO:0000269|PubMed:12615066}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12615066}. Membrane
CC       {ECO:0000269|PubMed:12615066}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:12615066}.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in testis. Expressed in
CC       brain at low levels. {ECO:0000269|PubMed:12615066}.
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DR   EMBL; BC062051; AAH62051.1; -; mRNA.
DR   EMBL; BC095901; AAH95901.1; -; mRNA.
DR   EMBL; CK598656; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; AF245225; AAF72164.1; -; mRNA.
DR   RefSeq; NP_071597.2; NM_022261.2.
DR   AlphaFoldDB; Q6P6S3; -.
DR   SMR; Q6P6S3; -.
DR   MINT; Q6P6S3; -.
DR   STRING; 10116.ENSRNOP00000020366; -.
DR   iPTMnet; Q6P6S3; -.
DR   PhosphoSitePlus; Q6P6S3; -.
DR   PaxDb; Q6P6S3; -.
DR   Ensembl; ENSRNOT00000020366; ENSRNOP00000020366; ENSRNOG00000015105.
DR   GeneID; 64027; -.
DR   KEGG; rno:64027; -.
DR   CTD; 54836; -.
DR   RGD; 708400; Bspry.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000161096; -.
DR   HOGENOM; CLU_050384_0_0_1; -.
DR   InParanoid; Q6P6S3; -.
DR   OMA; SKACADG; -.
DR   OrthoDB; 758185at2759; -.
DR   PhylomeDB; Q6P6S3; -.
DR   TreeFam; TF351014; -.
DR   PRO; PR:Q6P6S3; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000015105; Expressed in testis and 19 other tissues.
DR   ExpressionAtlas; Q6P6S3; baseline and differential.
DR   Genevisible; Q6P6S3; RN.
DR   GO; GO:0031252; C:cell leading edge; IDA:RGD.
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; IDA:RGD.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; ISO:RGD.
DR   GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR   Gene3D; 2.60.120.920; -; 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   InterPro; IPR000315; Znf_B-box.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   PRINTS; PR01407; BUTYPHLNCDUF.
DR   SMART; SM00589; PRY; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
PE   1: Evidence at protein level;
KW   Calcium; Calcium transport; Cytoplasm; Ion transport; Membrane;
KW   Metal-binding; Reference proteome; Transport; Zinc; Zinc-finger.
FT   CHAIN           1..448
FT                   /note="B box and SPRY domain-containing protein"
FT                   /id="PRO_0000244259"
FT   DOMAIN          257..448
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         63..111
FT                   /note="B box-type"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..53
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        310..313
FT                   /note="DDPE -> VTQQ (in Ref. 2; AAF72164)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   448 AA;  49704 MW;  1971FA20FE4019A0 CRC64;
     MSSDVSGTES GSESGPESVP EPVPEPGPEP ESEPGPGPAP GPGPGPAPGP GPGLGREPGQ
     RYQPCQLCPE HGKPLSWFCL SERRPVCATC AGFGGRCHRH RIRRAEEHAE ELRNKIVDHC
     EKLQLQSAGI TKYVAEVLQG KNQKAMIMAN ATREVIIQRL SLVRCLCESE EQRLLEQVHS
     EEERAHQCIL TQRAHWDDKL RKLDSLRTSM VDMLTHLNDL QLIQMEQEIL ERAEEAEGIL
     EPQESEKLSF NEKCAWSPLL TQLWATSVLG SLSGMEDVLI DERTVGPLLN LSEDRKTLTF
     NAKKSKVCSD DPERFDHWPN ALAVNAFQTG LHAWAVNVKH SCAYKVGVAS AQLPRKGSGS
     DCRLGHNAFS WVFSRYDQEF CFSHNGNHEP LALLRCPTQL GLLLDLQAGE LIFYEPASGT
     VLHIHRESFP HRLFPVFAVA DQVISIVC