SYG1_CAEEL
ID SYG1_CAEEL Reviewed; 730 AA.
AC B1Q236; H2L0B4;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Synaptogenesis protein syg-1 {ECO:0000305};
DE AltName: Full=Synaptogenesis abnormal protein 1 {ECO:0000312|WormBase:K02E10.8b};
DE Flags: Precursor;
GN Name=syg-1 {ECO:0000312|WormBase:K02E10.8b};
GN ORFNames=K02E10.8 {ECO:0000312|WormBase:K02E10.8b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12628183; DOI=10.1016/s0092-8674(03)00113-2;
RA Shen K., Bargmann C.I.;
RT "The immunoglobulin superfamily protein SYG-1 determines the location of
RT specific synapses in C. elegans.";
RL Cell 112:619-630(2003).
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15035988; DOI=10.1016/s0092-8674(04)00251-x;
RA Shen K., Fetter R.D., Bargmann C.I.;
RT "Synaptic specificity is generated by the synaptic guidepost protein SYG-2
RT and its receptor, SYG-1.";
RL Cell 116:869-881(2004).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SKR-1, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17626846; DOI=10.1126/science.1145727;
RA Ding M., Chao D., Wang G., Shen K.;
RT "Spatial regulation of an E3 ubiquitin ligase directs selective synapse
RT elimination.";
RL Science 317:947-951(2007).
RN [5] {ECO:0000305}
RP TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=18675916; DOI=10.1016/j.mcn.2008.07.001;
RA Chao D.L., Shen K.;
RT "Functional dissection of SYG-1 and SYG-2, cell adhesion molecules required
RT for selective synaptogenesis in C. elegans.";
RL Mol. Cell. Neurosci. 39:248-257(2008).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SYG-2, AND TISSUE SPECIFICITY.
RX PubMed=21858180; DOI=10.1371/journal.pone.0023598;
RA Wanner N., Noutsou F., Baumeister R., Walz G., Huber T.B.,
RA Neumann-Haefelin E.;
RT "Functional and spatial analysis of C. elegans SYG-1 and SYG-2, orthologs
RT of the Neph/nephrin cell adhesion module directing selective
RT synaptogenesis.";
RL PLoS ONE 6:E23598-E23598(2011).
RN [7] {ECO:0000305}
RP FUNCTION, INTERACTION WITH THE WAVE REGULATORY COMPLEX, AND MUTAGENESIS OF
RP 671-SER-PHE-672.
RX PubMed=24439377; DOI=10.1016/j.cell.2013.12.009;
RA Chia P.H., Chen B., Li P., Rosen M.K., Shen K.;
RT "Local F-actin network links synapse formation and axon branching.";
RL Cell 156:208-220(2014).
RN [8] {ECO:0007744|PDB:4OF0, ECO:0007744|PDB:4OF3, ECO:0007744|PDB:4OF6}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 19-282 IN COMPLEX WITH SYG-2,
RP FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BOND, GLYCOSYLATION AT ASN-93 AND
RP ASN-206, AND MUTAGENESIS OF GLN-54; PHE-60 AND GLN-105.
RX PubMed=24485456; DOI=10.1016/j.cell.2014.01.004;
RA Ozkan E., Chia P.H., Wang R.R., Goriatcheva N., Borek D., Otwinowski Z.,
RA Walz T., Shen K., Garcia K.C.;
RT "Extracellular architecture of the SYG-1/SYG-2 adhesion complex instructs
RT synaptogenesis.";
RL Cell 156:482-494(2014).
CC -!- FUNCTION: Cell adhesion protein (PubMed:15035988). Involved in synapse
CC formation in the HSNL egg-laying motor neuron (PubMed:12628183,
CC PubMed:15035988, PubMed:21858180, PubMed:24485456). Inhibits assembly
CC of the SCF(sel-10) E3 ubiquitin ligase complex at synapses, and
CC protects them from elimination (PubMed:17626846). Also required for F-
CC actin assembly at the synaptic region and for axon branch formation
CC (PubMed:24439377). {ECO:0000269|PubMed:12628183,
CC ECO:0000269|PubMed:15035988, ECO:0000269|PubMed:17626846,
CC ECO:0000269|PubMed:21858180, ECO:0000269|PubMed:24439377,
CC ECO:0000269|PubMed:24485456}.
CC -!- SUBUNIT: Interacts with skr-1 (PubMed:17626846). Interacts with syg-2
CC (PubMed:21858180, PubMed:24485456). Interacts with the WAVE regulatory
CC complex; the interaction leads to formation of a synaptic F-actin
CC network that is required for synapse formation and axon branching
CC (PubMed:24439377). {ECO:0000269|PubMed:17626846,
CC ECO:0000269|PubMed:21858180, ECO:0000269|PubMed:24439377,
CC ECO:0000269|PubMed:24485456}.
CC -!- INTERACTION:
CC B1Q236; Q9U3P2: syg-2; NbExp=5; IntAct=EBI-321771, EBI-9211201;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000255}. Cell projection, axon
CC {ECO:0000269|PubMed:12628183, ECO:0000269|PubMed:15035988,
CC ECO:0000269|PubMed:17626846}. Synapse {ECO:0000269|PubMed:12628183,
CC ECO:0000269|PubMed:24485456}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:K02E10.8b};
CC IsoId=B1Q236-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:K02E10.8a};
CC IsoId=B1Q236-2; Sequence=VSP_057850, VSP_057851;
CC -!- TISSUE SPECIFICITY: Expression in head motor neurons, occasionally in
CC HSN neurons and weakly in other cells in the vulval region
CC (PubMed:12628183). Expressed in the primary synapse region of HSNL
CC motor neuron (PubMed:18675916, PubMed:21858180).
CC {ECO:0000269|PubMed:12628183, ECO:0000269|PubMed:18675916,
CC ECO:0000269|PubMed:21858180}.
CC -!- DEVELOPMENTAL STAGE: Localized to the primary synapse region in the
CC vulva from early larval stage L4 to young adult stage.
CC {ECO:0000269|PubMed:17626846}.
CC -!- DOMAIN: The first Ig-like domain is necessary for localization to the
CC primary synapse region of HSNL motor neurons.
CC {ECO:0000269|PubMed:18675916}.
CC -!- DISRUPTION PHENOTYPE: Animals are viable, fertile and coordinated
CC (PubMed:12628183). Defective HSN axon branching at the vulva
CC (PubMed:12628183). Abnormal synaptic vesicle clustering in HSNL motor
CC neuron (PubMed:12628183, PubMed:15035988). Synapses in the secondary
CC synapse region, anterior to the vulva, are not eliminated during
CC synapse development and persist into adulthood (PubMed:17626846).
CC {ECO:0000269|PubMed:12628183, ECO:0000269|PubMed:15035988,
CC ECO:0000269|PubMed:17626846}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. {ECO:0000305}.
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DR EMBL; BX284606; CCD72282.1; -; Genomic_DNA.
DR EMBL; BX284606; CCD72283.1; -; Genomic_DNA.
DR RefSeq; NP_001123159.1; NM_001129687.2. [B1Q236-1]
DR RefSeq; NP_508457.3; NM_076056.6. [B1Q236-2]
DR PDB; 4OF0; X-ray; 2.30 A; A=19-271.
DR PDB; 4OF3; X-ray; 2.50 A; A/B=19-282.
DR PDB; 4OF6; X-ray; 1.70 A; A/B=19-129.
DR PDB; 4OF7; X-ray; 2.10 A; A/B/C/D=19-129.
DR PDB; 4OFY; X-ray; 3.30 A; A/B/C=19-271.
DR PDBsum; 4OF0; -.
DR PDBsum; 4OF3; -.
DR PDBsum; 4OF6; -.
DR PDBsum; 4OF7; -.
DR PDBsum; 4OFY; -.
DR AlphaFoldDB; B1Q236; -.
DR SMR; B1Q236; -.
DR ComplexPortal; CPX-2973; syg-1-syg-2 cell adhesion complex.
DR IntAct; B1Q236; 1.
DR STRING; 6239.K02E10.8b; -.
DR EPD; B1Q236; -.
DR PaxDb; B1Q236; -.
DR PeptideAtlas; B1Q236; -.
DR PRIDE; B1Q236; -.
DR EnsemblMetazoa; K02E10.8a.1; K02E10.8a.1; WBGene00006365. [B1Q236-2]
DR EnsemblMetazoa; K02E10.8b.1; K02E10.8b.1; WBGene00006365. [B1Q236-1]
DR GeneID; 180555; -.
DR UCSC; K02E10.8b; c. elegans. [B1Q236-1]
DR CTD; 180555; -.
DR WormBase; K02E10.8a; CE37121; WBGene00006365; syg-1. [B1Q236-2]
DR WormBase; K02E10.8b; CE42267; WBGene00006365; syg-1. [B1Q236-1]
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000168476; -.
DR HOGENOM; CLU_013520_2_1_1; -.
DR InParanoid; B1Q236; -.
DR OMA; ITWTRRG; -.
DR OrthoDB; 269917at2759; -.
DR PRO; PR:B1Q236; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006365; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; B1Q236; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:WormBase.
DR GO; GO:0098636; C:protein complex involved in cell adhesion; IPI:ComplexPortal.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0097060; C:synaptic membrane; IDA:ComplexPortal.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:WormBase.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; IMP:UniProtKB.
DR GO; GO:0048755; P:branching morphogenesis of a nerve; IMP:WormBase.
DR GO; GO:0098609; P:cell-cell adhesion; IDA:ComplexPortal.
DR GO; GO:0007267; P:cell-cell signaling; IMP:WormBase.
DR GO; GO:0048668; P:collateral sprouting; IMP:UniProtKB.
DR GO; GO:0007416; P:synapse assembly; IDA:ComplexPortal.
DR GO; GO:0050808; P:synapse organization; IMP:WormBase.
DR GO; GO:0008039; P:synaptic target recognition; IMP:WormBase.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 4.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Cell projection; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Neurogenesis; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..730
FT /note="Synaptogenesis protein syg-1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433878"
FT TOPO_DOM 19..551
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 573..730
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 23..123
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 131..265
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 270..352
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 357..433
FT /note="Ig-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 441..540
FT /note="Ig-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:4OF3, ECO:0007744|PDB:4OF6,
FT ECO:0007744|PDB:4OFY"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:4OF3"
FT DISULFID 44..104
FT /evidence="ECO:0007744|PDB:4OF3"
FT DISULFID 152..246
FT /evidence="ECO:0007744|PDB:4OF3"
FT DISULFID 292..336
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 378..420
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 462..519
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 666..703
FT /note="EHSYGSFGSGLSTPGGVSDMYGVAMSDKLPVMETLQEV -> VRRGDERQIA
FT GYGDATGSGDSQNVQLQLPLVAGSGPTN (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_057850"
FT VAR_SEQ 704..730
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_057851"
FT MUTAGEN 54
FT /note="Q->A: Reduced syg-2 interaction."
FT /evidence="ECO:0000269|PubMed:24485456"
FT MUTAGEN 60
FT /note="F->A: Reduced syg-2 interaction."
FT /evidence="ECO:0000269|PubMed:24485456"
FT MUTAGEN 105
FT /note="Q->A: Reduced syg-2 interaction."
FT /evidence="ECO:0000269|PubMed:24485456"
FT MUTAGEN 671..672
FT /note="SF->AA: Impaired binding to WAVE complex."
FT /evidence="ECO:0000269|PubMed:24439377"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:4OF6"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:4OF6"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:4OF6"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:4OF6"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:4OF6"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4OF6"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:4OF6"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:4OF6"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:4OF6"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4OF6"
FT STRAND 100..106
FT /evidence="ECO:0007829|PDB:4OF6"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:4OF6"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:4OF0"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:4OF3"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:4OF0"
FT STRAND 148..159
FT /evidence="ECO:0007829|PDB:4OF0"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:4OF0"
FT STRAND 173..179
FT /evidence="ECO:0007829|PDB:4OF0"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:4OF0"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:4OF0"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:4OF0"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:4OF0"
FT STRAND 243..249
FT /evidence="ECO:0007829|PDB:4OF0"
FT STRAND 257..267
FT /evidence="ECO:0007829|PDB:4OF0"
SQ SEQUENCE 730 AA; 81107 MW; A1B9796DDF95727A CRC64;
MVRWQTWPLL LLFQLVTCQQ LQQRIVEAPK DTLAAVGETA ILTCRVEHQQ GPVQWMKDDF
GLGTDRDKPL PGNKRYRMVG SAANGEYNLE ISNVTLFDDD DFACQISESD HAKAVVSSKA
KLTVLVRPTP PKIVKSHHSL KAIAGDPITQ SCLSRKGKPP PTIGWAIASD EHGKHIVSWL
GESRSKFGGI HAKPEISQET VIAHVNETTQ VEEGGNNSRE DSSIYSIMSN LSFIPRPEDD
HKYLICISQH MTFPNKIEVD SVKLSLRYAP QINLTVASKL PLRENGSALL ACNVNAKPLD
NVKISWYKGN QKLRETGDTL TFETLKMEDH NRDIFCEATN EIGTTRGSIK LNVAFGARIM
STSQDKEVNE GDNAFFHCAT LANPAPAIFW TRGDSDEIIG HGENLTLENV RTWQQGNYNC
TATVEGFRKQ ILSHYLHIRG PPTVSMKDEV SASLDEATEI ICEISGRPKT NNVRWTVNGK
EINFNNGRIT VHQYPKPYGK ESILKIKDLK EEDFGVYNCS ANNGLGFDNR GTLLKKRNIL
DWIVITAKFD RMVALAIISA GVLLVSLLCC LCMCRSNCRS RKSKFIDDQS DVTVKCEALD
GQYFPEMYSS SPVDNVHLST KDYISIPQNN PDLDFLGATG SFGPPGGLYP KCFNNSANEY
IYNRYEHSYG SFGSGLSTPG GVSDMYGVAM SDKLPVMETL QEVETPKTSN YNFLSSPEVV
RPISRTSTHV
