ID   SNN_RAT                 Reviewed;          88 AA.
AC   P61808; O88369; Q498Q9;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Stannin;
GN   Name=Snn;
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 [MRNA], FUNCTION, AND INDUCTION BY TMT.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=1635553;
RA   Toggas S.M., Krady J.K., Billingsley M.L.;
RT   "Molecular neurotoxicology of trimethyltin: identification of stannin, a
RT   novel protein expressed in trimethyltin-sensitive cells.";
RL   Mol. Pharmacol. 42:44-56(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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   TISSUE SPECIFICITY.
RX   PubMed=9413842; DOI=10.1016/s0197-0186(97)00034-x;
RA   Dejneka N.S., Patanow C.M., Polavarapu R., Toggas S.M., Krady J.K.,
RA   Billingsley M.L.;
RT   "Localization and characterization of stannin: relationship to cellular
RT   sensitivity to organotin compounds.";
RL   Neurochem. Int. 31:801-815(1997).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Plays a role in the toxic effects of organotins
CC       (PubMed:1635553). Plays a role in endosomal maturation (By similarity).
CC       {ECO:0000250|UniProtKB:O75324, ECO:0000269|PubMed:1635553}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O75324}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: High level of expression in spleen, followed by
CC       brain and kidney. {ECO:0000269|PubMed:9413842}.
CC   -!- INDUCTION: By trimethyltin (TMT), a trialkyltin compound which is a
CC       potent neurotoxic agent that selectively damages specific brain
CC       regions. {ECO:0000269|PubMed:1635553}.
CC   -!- SIMILARITY: Belongs to the stannin family. {ECO:0000305}.
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DR   EMBL; M81639; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC100111; AAI00112.1; -; mRNA.
DR   RefSeq; NP_001029255.1; NM_001034083.1.
DR   AlphaFoldDB; P61808; -.
DR   BMRB; P61808; -.
DR   SMR; P61808; -.
DR   STRING; 10116.ENSRNOP00000003333; -.
DR   iPTMnet; P61808; -.
DR   PhosphoSitePlus; P61808; -.
DR   PaxDb; P61808; -.
DR   Ensembl; ENSRNOT00000088279; ENSRNOP00000074283; ENSRNOG00000058739.
DR   Ensembl; ENSRNOT00000116003; ENSRNOP00000080199; ENSRNOG00000058739.
DR   GeneID; 29140; -.
DR   KEGG; rno:29140; -.
DR   UCSC; RGD:3730; rat.
DR   CTD; 8303; -.
DR   RGD; 3730; Snn.
DR   eggNOG; ENOG502S14Z; Eukaryota.
DR   GeneTree; ENSGT00390000009447; -.
DR   HOGENOM; CLU_2711160_0_0_1; -.
DR   InParanoid; P61808; -.
DR   OMA; FGCWCYL; -.
DR   OrthoDB; 1594644at2759; -.
DR   PhylomeDB; P61808; -.
DR   TreeFam; TF336244; -.
DR   PRO; PR:P61808; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000058739; Expressed in thymus and 19 other tissues.
DR   Genevisible; P61808; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; ISO:RGD.
DR   CDD; cd20257; Stannin; 1.
DR   Gene3D; 4.10.280.20; -; 1.
DR   InterPro; IPR015137; SNN_cytoplasm.
DR   InterPro; IPR015136; SNN_linker.
DR   InterPro; IPR015135; SNN_transmemb.
DR   InterPro; IPR038747; Stannin.
DR   InterPro; IPR027435; Stannin_sf.
DR   PANTHER; PTHR28564; PTHR28564; 1.
DR   Pfam; PF09051; SNN_cytoplasm; 1.
DR   Pfam; PF09050; SNN_linker; 1.
DR   Pfam; PF09049; SNN_transmemb; 1.
PE   1: Evidence at protein level;
KW   Membrane; Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..88
FT                   /note="Stannin"
FT                   /id="PRO_0000072016"
FT   TOPO_DOM        1..10
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..88
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         49
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P61807"
FT   MOD_RES         83
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   88 AA;  9501 MW;  EB8DA73323D816C5 CRC64;
     MSIMDHSPTT GVVTVIVILI AIAALGALIL GCWCYLRLQR ISQSEDEESI VGDGETKEPF
     LLVQYSAKGP CVERKAKLMT ANSPEVHG