SNG2_HUMAN
ID SNG2_HUMAN Reviewed; 224 AA.
AC O43760; O43762; Q3KQZ2; Q658S7;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Synaptogyrin-2 {ECO:0000305};
DE AltName: Full=Cellugyrin {ECO:0000250|UniProtKB:O54980};
GN Name=SYNGR2 {ECO:0000312|HGNC:HGNC:11499};
GN ORFNames=UNQ352/PRO615 {ECO:0000312|EMBL:AAQ89275.1};
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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, Lymph, and Skin;
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 [5]
RP PROTEIN SEQUENCE OF 1-18, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (FEB-2005) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-224 (ISOFORM 1).
RC TISSUE=Stomach;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
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 [9]
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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SFTS PHLEBOVIRUS NNS
RP PROTEIN (MICROBIAL INFECTION), SUBCELLULAR LOCATION (MICROBIAL INFECTION),
RP AND INDUCTION BY SFTS PHLEBOVIRUS (MICROBIAL INFECTION).
RX PubMed=27226560; DOI=10.1074/jbc.m116.715599;
RA Sun Q., Qi X., Zhang Y., Wu X., Liang M., Li C., Li D., Cardona C.J.,
RA Xing Z.;
RT "Synaptogyrin-2 promotes replication of a novel tick-borne bunyavirus
RT through interacting with viral nonstructural protein NSs.";
RL J. Biol. Chem. 291:16138-16149(2016).
CC -!- FUNCTION: May play a role in regulated exocytosis. In neuronal cells,
CC modulates the localization of synaptophysin/SYP into synaptic-like
CC microvesicles and may therefore play a role in the formation and/or the
CC maturation of this vesicles. May also play a role in GLUT4 storage and
CC transport to the plasma membrane. {ECO:0000250|UniProtKB:O54980}.
CC -!- FUNCTION: (Microbial infection) May play a role in the assembly of
CC cytoplasmic inclusion bodies required for SFTS phlebovirus replication.
CC {ECO:0000269|PubMed:27226560}.
CC -!- SUBUNIT: (Microbial infection) Interacts with SFTS phlebovirus protein
CC NSs; may be involved in virus replication.
CC {ECO:0000269|PubMed:27226560}.
CC -!- INTERACTION:
CC O43760; Q6AZY7: SCARA3; NbExp=3; IntAct=EBI-2826419, EBI-8657660;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:O54980}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC membrane {ECO:0000250|UniProtKB:O54980}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Localizes to cytoplasmic vesicles associated with
CC the recycling endosomes. {ECO:0000250|UniProtKB:O54980}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet. Note=(Microbial infection) Upon
CC SFTS phlebovirus infection, the protein localizes in lipid droplets and
CC inclusion bodies. {ECO:0000269|PubMed:27226560}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43760-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43760-2; Sequence=VSP_056179;
CC -!- TISSUE SPECIFICITY: Ubiquitous; low expression in brain.
CC {ECO:0000269|PubMed:9760194}.
CC -!- INDUCTION: (Microbial infection) Up-regulated upon SFTS phlebovirus
CC infection (at protein level). {ECO:0000269|PubMed:27226560}.
CC -!- PTM: May be tyrosine phosphorylated by Src.
CC {ECO:0000250|UniProtKB:O54980}.
CC -!- SIMILARITY: Belongs to the synaptogyrin family. {ECO:0000305}.
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DR EMBL; AJ002308; CAA05325.1; -; mRNA.
DR EMBL; AJ002310; CAA05327.1; -; Genomic_DNA.
DR EMBL; AJ002312; CAA05327.1; JOINED; Genomic_DNA.
DR EMBL; AY358916; AAQ89275.1; -; mRNA.
DR EMBL; AC021593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000407; AAH00407.1; -; mRNA.
DR EMBL; BC029755; AAH29755.1; -; mRNA.
DR EMBL; BC105992; AAI05993.1; -; mRNA.
DR EMBL; AL833010; CAH56291.1; -; mRNA.
DR CCDS; CCDS11753.1; -. [O43760-1]
DR CCDS; CCDS86641.1; -. [O43760-2]
DR RefSeq; NP_001307452.1; NM_001320523.1.
DR RefSeq; NP_004701.1; NM_004710.4. [O43760-1]
DR RefSeq; XP_005257849.1; XM_005257792.3.
DR AlphaFoldDB; O43760; -.
DR BioGRID; 114591; 100.
DR IntAct; O43760; 35.
DR MINT; O43760; -.
DR STRING; 9606.ENSP00000225777; -.
DR GlyGen; O43760; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43760; -.
DR PhosphoSitePlus; O43760; -.
DR SwissPalm; O43760; -.
DR BioMuta; SYNGR2; -.
DR EPD; O43760; -.
DR jPOST; O43760; -.
DR MassIVE; O43760; -.
DR MaxQB; O43760; -.
DR PaxDb; O43760; -.
DR PeptideAtlas; O43760; -.
DR PRIDE; O43760; -.
DR ProteomicsDB; 49153; -. [O43760-1]
DR TopDownProteomics; O43760-1; -. [O43760-1]
DR Antibodypedia; 32546; 260 antibodies from 31 providers.
DR DNASU; 9144; -.
DR Ensembl; ENST00000225777.8; ENSP00000225777.2; ENSG00000108639.8. [O43760-1]
DR Ensembl; ENST00000585591.5; ENSP00000465678.1; ENSG00000108639.8. [O43760-1]
DR Ensembl; ENST00000588282.5; ENSP00000467600.1; ENSG00000108639.8. [O43760-2]
DR GeneID; 9144; -.
DR KEGG; hsa:9144; -.
DR MANE-Select; ENST00000225777.8; ENSP00000225777.2; NM_004710.7; NP_004701.1.
DR UCSC; uc002jut.4; human. [O43760-1]
DR CTD; 9144; -.
DR DisGeNET; 9144; -.
DR GeneCards; SYNGR2; -.
DR HGNC; HGNC:11499; SYNGR2.
DR HPA; ENSG00000108639; Low tissue specificity.
DR MIM; 603926; gene.
DR neXtProt; NX_O43760; -.
DR OpenTargets; ENSG00000108639; -.
DR PharmGKB; PA36281; -.
DR VEuPathDB; HostDB:ENSG00000108639; -.
DR eggNOG; KOG4016; Eukaryota.
DR GeneTree; ENSGT00950000182935; -.
DR HOGENOM; CLU_079186_1_0_1; -.
DR InParanoid; O43760; -.
DR OMA; NQWAATR; -.
DR OrthoDB; 1549362at2759; -.
DR PhylomeDB; O43760; -.
DR TreeFam; TF320995; -.
DR PathwayCommons; O43760; -.
DR SignaLink; O43760; -.
DR BioGRID-ORCS; 9144; 15 hits in 1076 CRISPR screens.
DR ChiTaRS; SYNGR2; human.
DR GenomeRNAi; 9144; -.
DR Pharos; O43760; Tbio.
DR PRO; PR:O43760; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O43760; protein.
DR Bgee; ENSG00000108639; Expressed in mucosa of transverse colon and 199 other tissues.
DR ExpressionAtlas; O43760; baseline and differential.
DR Genevisible; O43760; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0031594; C:neuromuscular junction; IBA:GO_Central.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0045055; P:regulated exocytosis; ISS:UniProtKB.
DR GO; GO:0048499; P:synaptic vesicle membrane organization; ISS: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; Alternative splicing; Cytoplasmic vesicle;
KW Direct protein sequencing; Host-virus interaction; Lipid droplet; Membrane;
KW Phosphoprotein; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..224
FT /note="Synaptogyrin-2"
FT /id="PRO_0000183993"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 20..171
FT /note="MARVEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 160..224
FT /note="GVLASLAYQRYKAGVDDFIQNYVDPTPDPNTAYASYPGASVDNYQQPPFTQN
FT AETTEGYQPPPVY -> VGWPGAGSWVKGGGGWGPPPTCTLLCSPCRVCWPPWPTSATR
FT LAWTTSSRITLTPLRTPTLPTPPTQVHLWTTTNSHPSPRTRRPPRATSRPLCTERRLAW
FT EGGQRGPSPLPWTFP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056179"
FT CONFLICT 160..162
FT /note="GVL -> VGW (in Ref. 1; CAA05327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 224 AA; 24810 MW; EC92C95CE9E5BD41 CRC64;
MESGAYGAAK AGGSFDLRRF LTQPQVVARA VCLVFALIVF SCIYGEGYSN AHESKQMYCV
FNRNEDACRY GSAIGVLAFL ASAFFLVVDA YFPQISNATD RKYLVIGDLL FSALWTFLWF
VGFCFLTNQW AVTNPKDVLV GADSVRAAIT FSFFSIFSWG VLASLAYQRY KAGVDDFIQN
YVDPTPDPNT AYASYPGASV DNYQQPPFTQ NAETTEGYQP PPVY
