ID   SNG1_PONAB              Reviewed;         234 AA.
AC   Q5R703;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Synaptogyrin-1 {ECO:0000305};
GN   Name=SYNGR1 {ECO:0000250|UniProtKB:O43759};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May play a role in regulated exocytosis. Modulates the
CC       localization of synaptophysin/SYP into synaptic-like microvesicles and
CC       may therefore play a role in synaptic-like microvesicle formation
CC       and/or maturation (By similarity). Involved in the regulation of short-
CC       term and long-term synaptic plasticity (By similarity).
CC       {ECO:0000250|UniProtKB:O55100, ECO:0000250|UniProtKB:Q62876}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC       vesicle membrane {ECO:0000250|UniProtKB:Q62876}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:Q62876}. Melanosome
CC       {ECO:0000250|UniProtKB:O43759}.
CC   -!- SIMILARITY: Belongs to the synaptogyrin family. {ECO:0000305}.
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DR   EMBL; CR860320; CAH92457.1; -; mRNA.
DR   RefSeq; NP_001126448.1; NM_001132976.1.
DR   AlphaFoldDB; Q5R703; -.
DR   STRING; 9601.ENSPPYP00000013210; -.
DR   Ensembl; ENSPPYT00000035410; ENSPPYP00000026737; ENSPPYG00000031983.
DR   GeneID; 100173433; -.
DR   KEGG; pon:100173433; -.
DR   CTD; 9145; -.
DR   eggNOG; KOG0698; Eukaryota.
DR   eggNOG; KOG4016; Eukaryota.
DR   GeneTree; ENSGT00950000182935; -.
DR   InParanoid; Q5R703; -.
DR   OrthoDB; 1549362at2759; -.
DR   Proteomes; UP000001595; Chromosome 22.
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:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR   GO; GO:0045055; P:regulated exocytosis; ISS:UniProtKB.
DR   GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
DR   GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IEA:Ensembl.
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; Reference proteome; Synapse;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..234
FT                   /note="Synaptogyrin-1"
FT                   /id="PRO_0000343946"
FT   TOPO_DOM        1..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q62876"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..71
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q62876"
FT   TRANSMEM        72..92
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        93..103
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q62876"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        125..148
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250|UniProtKB:Q62876"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..234
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:Q62876"
FT   DOMAIN          20..173
FT                   /note="MARVEL"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00581"
FT   REGION          192..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:O43759"
SQ   SEQUENCE   234 AA;  25513 MW;  2DB9639FE5F93F50 CRC64;
     MEGGAYGAGK AGGAFDPYAL VRQPHTILRV VSWLFSIVVF GSIVNEGYLN SASEGEEFCI
     YNRNPNACSY GVAVGVLAFL TCLLYLALDV YFPQISSVKD RKKAVLSDIG VSAFWAFLWF
     VGFCYLANQW QVSKPKDNPL NEGTDAARAA IAFSFFSIFT WAGQAVLAFQ RYQIGADSAL
     FSQDYMDPSQ DSSMPYAPYV EPSTGPDPAG MGGTYQQPAN TFDTEPQGYQ SQGY