SNG3_HUMAN
ID SNG3_HUMAN Reviewed; 229 AA.
AC O43761; B2R9S0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Synaptogyrin-3 {ECO:0000305};
GN Name=SYNGR3 {ECO:0000312|HGNC:HGNC:11501};
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], AND TISSUE SPECIFICITY.
RX PubMed=9760194; DOI=10.1007/s004390050795;
RA Kedra D., Pan H.-Q., Seroussi E., Fransson I., Guilbaud C., Collins J.E.,
RA Dunham I., Blennow E., Roe B.A., Piehl F., Dumanski J.P.;
RT "Characterization of the human synaptogyrin gene family.";
RL Hum. Genet. 103:131-141(1998).
RN [2]
RP SEQUENCE REVISION.
RA Kedra D.;
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
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).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=B-cell;
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: May play a role in regulated exocytosis. May indirectly
CC regulate the activity of the plasma membrane dopamine transporter
CC SLC6A3 and thereby regulate dopamine transport back from the synaptic
CC cleft into the presynaptic terminal. {ECO:0000250|UniProtKB:Q8R191}.
CC -!- SUBUNIT: Interacts (via N-terminus) with SLC6A3 (via N-terminus). May
CC interact with VMAT2. {ECO:0000250|UniProtKB:Q8R191}.
CC -!- INTERACTION:
CC O43761; Q96CM8: ACSF2; NbExp=3; IntAct=EBI-11321949, EBI-2876502;
CC O43761; P53367: ARFIP1; NbExp=3; IntAct=EBI-11321949, EBI-2808808;
CC O43761; Q08426: EHHADH; NbExp=3; IntAct=EBI-11321949, EBI-2339219;
CC O43761; Q05329: GAD2; NbExp=3; IntAct=EBI-11321949, EBI-9304251;
CC O43761; C9JCN9: HSBP1L1; NbExp=3; IntAct=EBI-11321949, EBI-2685549;
CC O43761; Q92993: KAT5; NbExp=3; IntAct=EBI-11321949, EBI-399080;
CC O43761; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-11321949, EBI-11742507;
CC O43761; Q504T8: MIDN; NbExp=3; IntAct=EBI-11321949, EBI-7153979;
CC O43761; Q00013: MPP1; NbExp=3; IntAct=EBI-11321949, EBI-711788;
CC O43761; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-11321949, EBI-11978907;
CC O43761; O60664: PLIN3; NbExp=3; IntAct=EBI-11321949, EBI-725795;
CC O43761; Q96T60: PNKP; NbExp=3; IntAct=EBI-11321949, EBI-1045072;
CC O43761; P17252: PRKCA; NbExp=3; IntAct=EBI-11321949, EBI-1383528;
CC O43761; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-11321949, EBI-9090795;
CC O43761; Q9Y371: SH3GLB1; NbExp=6; IntAct=EBI-11321949, EBI-2623095;
CC O43761; Q9NZD8: SPG21; NbExp=5; IntAct=EBI-11321949, EBI-742688;
CC O43761; P49638: TTPA; NbExp=3; IntAct=EBI-11321949, EBI-10210710;
CC O43761; P61981: YWHAG; NbExp=3; IntAct=EBI-11321949, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000250|UniProtKB:Q8R191}; Multi-pass membrane
CC protein {ECO:0000255}. Synapse {ECO:0000250|UniProtKB:Q8R191}.
CC Note=Found at the neuromuscular synapses.
CC {ECO:0000250|UniProtKB:Q8R191}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and placenta.
CC {ECO:0000269|PubMed:9760194}.
CC -!- SIMILARITY: Belongs to the synaptogyrin family. {ECO:0000305}.
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DR EMBL; AJ002309; CAA05326.2; -; mRNA.
DR EMBL; AK313894; BAG36617.1; -; mRNA.
DR EMBL; CH471112; EAW85577.1; -; Genomic_DNA.
DR EMBL; BC014087; AAH14087.1; -; mRNA.
DR CCDS; CCDS10456.1; -.
DR RefSeq; NP_004200.2; NM_004209.5.
DR AlphaFoldDB; O43761; -.
DR BioGRID; 114590; 64.
DR IntAct; O43761; 22.
DR MINT; O43761; -.
DR STRING; 9606.ENSP00000248121; -.
DR iPTMnet; O43761; -.
DR PhosphoSitePlus; O43761; -.
DR BioMuta; SYNGR3; -.
DR EPD; O43761; -.
DR MassIVE; O43761; -.
DR MaxQB; O43761; -.
DR PaxDb; O43761; -.
DR PeptideAtlas; O43761; -.
DR PRIDE; O43761; -.
DR ProteomicsDB; 49154; -.
DR Antibodypedia; 23420; 114 antibodies from 27 providers.
DR DNASU; 9143; -.
DR Ensembl; ENST00000248121.7; ENSP00000248121.2; ENSG00000127561.16.
DR GeneID; 9143; -.
DR KEGG; hsa:9143; -.
DR MANE-Select; ENST00000248121.7; ENSP00000248121.2; NM_004209.6; NP_004200.2.
DR UCSC; uc002cod.3; human.
DR CTD; 9143; -.
DR DisGeNET; 9143; -.
DR GeneCards; SYNGR3; -.
DR HGNC; HGNC:11501; SYNGR3.
DR HPA; ENSG00000127561; Tissue enriched (brain).
DR MIM; 603927; gene.
DR neXtProt; NX_O43761; -.
DR OpenTargets; ENSG00000127561; -.
DR PharmGKB; PA36283; -.
DR VEuPathDB; HostDB:ENSG00000127561; -.
DR eggNOG; KOG4016; Eukaryota.
DR GeneTree; ENSGT00950000182935; -.
DR HOGENOM; CLU_079186_0_1_1; -.
DR InParanoid; O43761; -.
DR OMA; ACRFGVV; -.
DR OrthoDB; 1549362at2759; -.
DR PhylomeDB; O43761; -.
DR TreeFam; TF320995; -.
DR PathwayCommons; O43761; -.
DR SignaLink; O43761; -.
DR BioGRID-ORCS; 9143; 18 hits in 1074 CRISPR screens.
DR ChiTaRS; SYNGR3; human.
DR GenomeRNAi; 9143; -.
DR Pharos; O43761; Tbio.
DR PRO; PR:O43761; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O43761; protein.
DR Bgee; ENSG00000127561; Expressed in middle temporal gyrus and 129 other tissues.
DR ExpressionAtlas; O43761; baseline and differential.
DR Genevisible; O43761; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IBA:GO_Central.
DR GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR GO; GO:0001504; P:neurotransmitter uptake; IEA:Ensembl.
DR GO; GO:0032411; P:positive regulation of transporter activity; ISS:UniProtKB.
DR GO; GO:0045055; P:regulated exocytosis; ISS:UniProtKB.
DR GO; GO:0021762; P:substantia nigra development; HEP:UniProtKB.
DR InterPro; IPR008253; Marvel.
DR InterPro; IPR016579; Synaptogyrin.
DR PANTHER; PTHR10838; PTHR10838; 1.
DR Pfam; PF01284; MARVEL; 1.
DR PIRSF; PIRSF011282; Synaptogyrin; 1.
DR PROSITE; PS51225; MARVEL; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasmic vesicle; Membrane; Reference proteome; Synapse;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..229
FT /note="Synaptogyrin-3"
FT /id="PRO_0000183996"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 20..172
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT REGION 209..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
SQ SEQUENCE 229 AA; 24555 MW; 0755812EDD4AD4C5 CRC64;
MEGASFGAGR AGAALDPVSF ARRPQTLLRV ASWVFSIAVF GPIVNEGYVN TDSGPELRCV
FNGNAGACRF GVALGLGAFL ACAAFLLLDV RFQQISSVRD RRRAVLLDLG FSGLWSFLWF
VGFCFLTNQW QRTAPGPATT QAGDAARAAI AFSFFSILSW VALTVKALQR FRLGTDMSLF
ATEQLSTGAS QAYPGYPVGS GVEGTETYQS PPFTETLDTS PKGYQVPAY
