TM163_RAT
ID TM163_RAT Reviewed; 288 AA.
AC A9CMA6;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Transmembrane protein 163;
DE AltName: Full=Synaptic vesicle membrane protein of 31 kDa;
GN Name=Tmem163; Synonyms=Sv31;
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 [GENOMIC DNA].
RC STRAIN=Buffalo/Mna, and Wistar Kyoto/Ncrj;
RX PubMed=18064521; DOI=10.1007/s00335-007-9078-5;
RA Akiyama K., Morita H., Suetsugu S., Kuraba S., Numata Y., Yamamoto Y.,
RA Inui K., Ideura T., Wakisaka N., Nakano K., Oniki H., Takenawa T.,
RA Matsuyama M., Yoshimura A.;
RT "Actin-related protein 3 (Arp3) is mutated in proteinuric BUF/Mna rats.";
RL Mamm. Genome 19:41-50(2008).
RN [2]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND TISSUE SPECIFICITY.
RX PubMed=17623043; DOI=10.1111/j.1471-4159.2007.04758.x;
RA Burre J., Zimmermann H., Volknandt W.;
RT "Identification and characterization of SV31, a novel synaptic vesicle
RT membrane protein and potential transporter.";
RL J. Neurochem. 103:276-287(2007).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=20053882; DOI=10.1523/jneurosci.4074-09.2010;
RA Groenborg M., Pavlos N.J., Brunk I., Chua J.J., Muenster-Wandowski A.,
RA Riedel D., Ahnert-Hilger G., Urlaub H., Jahn R.;
RT "Quantitative comparison of glutamatergic and GABAergic synaptic vesicles
RT unveils selectivity for few proteins including MAL2, a novel synaptic
RT vesicle protein.";
RL J. Neurosci. 30:2-12(2010).
RN [4]
RP FUNCTION IN ZINC-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=21668449; DOI=10.1111/j.1471-4159.2011.07344.x;
RA Barth J., Zimmermann H., Volknandt W.;
RT "SV31 is a Zn2+-binding synaptic vesicle protein.";
RL J. Neurochem. 118:558-570(2011).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-60, AND
RP IDENTIFICATION BY 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: May bind zinc and other divalent cations and recruit them to
CC vesicular organelles. {ECO:0000269|PubMed:21668449}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane; Multi-pass membrane protein. Early endosome membrane.
CC Note=Glutamatergic synaptic vesicles.
CC -!- TISSUE SPECIFICITY: Strongly expressed in brain. Also detected in lung,
CC liver, kidney and spleen. Mainly expressed in the glutaminergic neuron
CC subpopulations. {ECO:0000269|PubMed:17623043,
CC ECO:0000269|PubMed:20053882}.
CC -!- SIMILARITY: Belongs to the TMEM163 family. {ECO:0000305}.
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DR EMBL; AB294577; BAF94224.1; -; Genomic_DNA.
DR EMBL; AB294578; BAF94244.1; -; Genomic_DNA.
DR RefSeq; NP_001104233.2; NM_001110763.2.
DR AlphaFoldDB; A9CMA6; -.
DR SMR; A9CMA6; -.
DR STRING; 10116.ENSRNOP00000005006; -.
DR iPTMnet; A9CMA6; -.
DR PhosphoSitePlus; A9CMA6; -.
DR PaxDb; A9CMA6; -.
DR PRIDE; A9CMA6; -.
DR Ensembl; ENSRNOT00000005006; ENSRNOP00000005006; ENSRNOG00000003769.
DR GeneID; 360839; -.
DR KEGG; rno:360839; -.
DR UCSC; RGD:1306212; rat.
DR CTD; 81615; -.
DR RGD; 1306212; Tmem163.
DR eggNOG; ENOG502QW7B; Eukaryota.
DR GeneTree; ENSGT00390000001170; -.
DR HOGENOM; CLU_081161_0_0_1; -.
DR InParanoid; A9CMA6; -.
DR OMA; WQGVRAW; -.
DR OrthoDB; 1547703at2759; -.
DR PhylomeDB; A9CMA6; -.
DR TreeFam; TF330782; -.
DR PRO; PR:A9CMA6; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000003769; Expressed in cerebellum and 12 other tissues.
DR Genevisible; A9CMA6; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0031901; C:early endosome membrane; IDA:UniProtKB.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:UniProtKB.
DR GO; GO:0097708; C:intracellular vesicle; ISO:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0099180; P:zinc ion import into synaptic vesicle; IDA:SynGO.
DR Gene3D; 1.20.1510.10; -; 1.
DR InterPro; IPR027469; Cation_efflux_TMD_sf.
DR InterPro; IPR026765; Tmem163.
DR PANTHER; PTHR31937; PTHR31937; 1.
DR SUPFAM; SSF161111; SSF161111; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endosome; Membrane; Phosphoprotein;
KW Reference proteome; Synapse; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..288
FT /note="Transmembrane protein 163"
FT /id="PRO_0000416586"
FT TOPO_DOM 1..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..186
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..254
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 54
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C996"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C996"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 288 AA; 31344 MW; 5C0577453233F89D CRC64;
MERAPGSERR SPPGPGVPRP PPRGHAPSTA APAPNPAPLS SSMQPDEERQ PRISESGQFS
DGFEDRGLLE SSTRLKPHEA QNYRKKALWV SWLSIIVTLA LAVAAFTVSV MRYSASAFGF
AFDAILDVLS SAIVLWRYSN AAAVHSAHRE YIACVILGVI FLLSSICIVV KAIHDLSTRL
LPEVDDFLFS VSILSGILCS VLAVLKFMLG KVLTSRALIT DGFNSLVGGV MGFSILLSAE
VFKHNAAVWY LDGSIGVLIG LTIFAYGVKL LIDMVPRVRQ TRHYEMFE
