ID   SNG2_BOVIN              Reviewed;         224 AA.
AC   A7E3W5;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Synaptogyrin-2 {ECO:0000305};
DE   AltName: Full=Cellugyrin {ECO:0000250|UniProtKB:O54980};
GN   Name=SYNGR2 {ECO:0000250|UniProtKB:O43760};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
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   -!- 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}.
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; BT030736; ABS45052.1; -; mRNA.
DR   RefSeq; NP_001093828.1; NM_001100358.1.
DR   AlphaFoldDB; A7E3W5; -.
DR   STRING; 9913.ENSBTAP00000025388; -.
DR   PaxDb; A7E3W5; -.
DR   PRIDE; A7E3W5; -.
DR   Ensembl; ENSBTAT00000025388; ENSBTAP00000025388; ENSBTAG00000019069.
DR   GeneID; 513812; -.
DR   KEGG; bta:513812; -.
DR   CTD; 9144; -.
DR   VEuPathDB; HostDB:ENSBTAG00000019069; -.
DR   VGNC; VGNC:107278; SYNGR2.
DR   eggNOG; KOG4016; Eukaryota.
DR   GeneTree; ENSGT00950000182935; -.
DR   HOGENOM; CLU_079186_1_0_1; -.
DR   InParanoid; A7E3W5; -.
DR   OMA; MQSSAYG; -.
DR   OrthoDB; 1549362at2759; -.
DR   TreeFam; TF320995; -.
DR   Proteomes; UP000009136; Chromosome 19.
DR   Bgee; ENSBTAG00000019069; Expressed in choroid plexus and 106 other tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   2: Evidence at transcript level;
KW   Acetylation; Cytoplasmic vesicle; Membrane; Phosphoprotein;
KW   Reference proteome; Synapse; Transmembrane; Transmembrane helix.
FT   CHAIN           1..224
FT                   /note="Synaptogyrin-2"
FT                   /id="PRO_0000343947"
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   REGION          196..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        203..217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:O43760"
FT   MOD_RES         3
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O43760"
SQ   SEQUENCE   224 AA;  25139 MW;  1A0078AAD4A7A487 CRC64;
     MESGAYGAPR AGGSFDLRRF LKQPQVVVRA VCLVFALIVF SCIFGEGYSN THDSQQQYCV
     FNRNEDACRY GSAIGVLAFL ASAFFFVVDI YFPQISNATD RKYLVIGDLL FSALWTFLWF
     VGFCFLTNQW AATKKNDVHV EADSARAAIT FSFFSIFSWC VLAFLAYQRY KAGVDEFIQN
     YVDPTPDPST AYASYPGVPA DTYQQPPFTQ NAESTEGYQP PPVY