SNN_HUMAN
ID SNN_HUMAN Reviewed; 88 AA.
AC O75324; D3DUG4; Q6FGI0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Stannin;
DE AltName: Full=AG8_1;
GN Name=SNN;
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].
RC TISSUE=Brain;
RX PubMed=9657854; DOI=10.1007/s003359900818;
RA Dejneka N.S., Polavarapu R., Deng X., Martin-Deleon P.A., Billingsley M.L.;
RT "Chromosomal localization and characterization of the stannin (Snn) gene.";
RL Mamm. Genome 9:556-564(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Endothelial cell;
RX PubMed=10233894;
RA Horrevoets A.J.G., Fontijn R.D., van Zonneveld A.J., de Vries C.J.M.,
RA ten Cate J.W., Pannekoek H.;
RT "Vascular endothelial genes that are responsive to tumor necrosis factor-
RT alpha in vitro are expressed in atherosclerotic lesions, including
RT inhibitor of apoptosis protein-1, stannin, and two novel genes.";
RL Blood 93:3418-3431(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-17 AND SER-88.
RG NIEHS SNPs program;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, 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 [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15269288; DOI=10.1124/mol.104.001719;
RA Davidson C.E., Reese B.E., Billingsley M.L., Yun J.K.;
RT "Stannin, a protein that localizes to the mitochondria and sensitizes NIH-
RT 3T3 cells to trimethyltin and dimethyltin toxicity.";
RL Mol. Pharmacol. 66:855-863(2004).
RN [9]
RP FUNCTION.
RX PubMed=27015288; DOI=10.1371/journal.pbio.1002395;
RA Pueyo J.I., Magny E.G., Sampson C.J., Amin U., Evans I.R., Bishop S.A.,
RA Couso J.P.;
RT "Hemotin, a regulator of phagocytosis encoded by a small ORF and conserved
RT across metazoans.";
RL PLoS Biol. 14:E1002395-E1002395(2016).
RN [10]
RP STRUCTURE BY NMR, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=16246365; DOI=10.1016/j.jmb.2005.09.038;
RA Buck-Koehntop B.A., Mascioni A., Buffy J.J., Veglia G.;
RT "Structure, dynamics, and membrane topology of stannin: a mediator of
RT neuronal cell apoptosis induced by trimethyltin chloride.";
RL J. Mol. Biol. 354:652-665(2005).
CC -!- FUNCTION: Plays a role in the toxic effects of organotins
CC (PubMed:15269288). Plays a role in endosomal maturation
CC (PubMed:27015288). {ECO:0000269|PubMed:15269288,
CC ECO:0000269|PubMed:27015288}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16246365}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:15269288, ECO:0000269|PubMed:16246365}; Single-pass
CC membrane protein {ECO:0000269|PubMed:16246365}.
CC -!- SIMILARITY: Belongs to the stannin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/snn/";
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DR EMBL; AF030196; AAC28427.1; -; mRNA.
DR EMBL; AF070673; AAC83231.1; -; mRNA.
DR EMBL; AL161976; CAB82314.1; -; mRNA.
DR EMBL; AY325800; AAP78484.1; -; Genomic_DNA.
DR EMBL; CR542127; CAG46924.1; -; mRNA.
DR EMBL; CR542138; CAG46935.1; -; mRNA.
DR EMBL; CH471112; EAW85146.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85147.1; -; Genomic_DNA.
DR EMBL; BC036100; AAH36100.1; -; mRNA.
DR EMBL; BC036443; AAH36443.1; -; mRNA.
DR CCDS; CCDS10549.1; -.
DR PIR; T47139; T47139.
DR RefSeq; NP_003489.1; NM_003498.5.
DR RefSeq; XP_016879231.1; XM_017023742.1.
DR PDB; 1ZZA; NMR; -; A=1-88.
DR PDBsum; 1ZZA; -.
DR AlphaFoldDB; O75324; -.
DR BMRB; O75324; -.
DR SMR; O75324; -.
DR BioGRID; 113904; 13.
DR IntAct; O75324; 4.
DR STRING; 9606.ENSP00000329287; -.
DR iPTMnet; O75324; -.
DR PhosphoSitePlus; O75324; -.
DR BioMuta; SNN; -.
DR jPOST; O75324; -.
DR MassIVE; O75324; -.
DR PaxDb; O75324; -.
DR PeptideAtlas; O75324; -.
DR PRIDE; O75324; -.
DR ProteomicsDB; 49894; -.
DR Antibodypedia; 2691; 9 antibodies from 8 providers.
DR DNASU; 8303; -.
DR Ensembl; ENST00000329565.6; ENSP00000329287.5; ENSG00000184602.6.
DR GeneID; 8303; -.
DR KEGG; hsa:8303; -.
DR MANE-Select; ENST00000329565.6; ENSP00000329287.5; NM_003498.6; NP_003489.1.
DR UCSC; uc002dbf.5; human.
DR CTD; 8303; -.
DR GeneCards; SNN; -.
DR HGNC; HGNC:11149; SNN.
DR HPA; ENSG00000184602; Tissue enhanced (brain, skeletal muscle).
DR MIM; 603032; gene.
DR neXtProt; NX_O75324; -.
DR OpenTargets; ENSG00000184602; -.
DR PharmGKB; PA35991; -.
DR VEuPathDB; HostDB:ENSG00000184602; -.
DR eggNOG; ENOG502S14Z; Eukaryota.
DR GeneTree; ENSGT00390000009447; -.
DR HOGENOM; CLU_2711160_0_0_1; -.
DR InParanoid; O75324; -.
DR OMA; FGCWCYL; -.
DR OrthoDB; 1594644at2759; -.
DR PhylomeDB; O75324; -.
DR TreeFam; TF336244; -.
DR PathwayCommons; O75324; -.
DR SignaLink; O75324; -.
DR BioGRID-ORCS; 8303; 8 hits in 1078 CRISPR screens.
DR ChiTaRS; SNN; human.
DR EvolutionaryTrace; O75324; -.
DR GeneWiki; SNN_(gene); -.
DR GenomeRNAi; 8303; -.
DR Pharos; O75324; Tdark.
DR PRO; PR:O75324; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O75324; protein.
DR Bgee; ENSG00000184602; Expressed in middle temporal gyrus and 205 other tissues.
DR Genevisible; O75324; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0016021; C:integral component of membrane; IDA:CAFA.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IDA:CAFA.
DR GO; GO:0009636; P:response to toxic substance; TAS:CAFA.
DR CDD; cd20257; Stannin; 1.
DR DisProt; DP00162; -.
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 3D-structure; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..88
FT /note="Stannin"
FT /id="PRO_0000072014"
FT TOPO_DOM 1..10
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:16246365"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..88
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16246365"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61807"
FT VARIANT 17
FT /note="V -> I (in dbSNP:rs8191328)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_018842"
FT VARIANT 88
FT /note="G -> S (in dbSNP:rs8191329)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_018843"
FT TURN 5..8
FT /evidence="ECO:0007829|PDB:1ZZA"
FT HELIX 9..33
FT /evidence="ECO:0007829|PDB:1ZZA"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:1ZZA"
FT TURN 48..54
FT /evidence="ECO:0007829|PDB:1ZZA"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1ZZA"
FT HELIX 60..79
FT /evidence="ECO:0007829|PDB:1ZZA"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:1ZZA"
SQ SEQUENCE 88 AA; 9497 MW; 1E8DA73323C5D6DF CRC64;
MSIMDHSPTT GVVTVIVILI AIAALGALIL GCWCYLRLQR ISQSEDEESI VGDGETKEPF
LLVQYSAKGP CVERKAKLMT PNGPEVHG
