ID SYG2_CAEEL Reviewed; 1270 AA.
AC Q9U3P2;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 173.
DE RecName: Full=Synaptogenesis protein syg-2 {ECO:0000305};
DE AltName: Full=Synaptogenesis abnormal protein 2 {ECO:0000312|WormBase:C26G2.1a};
DE Flags: Precursor;
GN Name=syg-2 {ECO:0000312|WormBase:C26G2.1a};
GN ORFNames=C26G2.1 {ECO:0000312|WormBase:C26G2.1a};
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, DEVELOPMENTAL STAGE, 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 [3] {ECO:0000305}
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, 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 [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH SYG-1, 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 [5] {ECO:0007744|PDB:4OFK, ECO:0007744|PDB:4OFP, ECO:0007744|PDB:4OFY}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 20-430 IN COMPLEX WITH SYG-1,
RP FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BOND, GLYCOSYLATION AT ASN-27;
RP ASN-149; ASN-185; ASN-223; ASN-251; ASN-311 AND ASN-391, AND MUTAGENESIS OF
RP GLN-53; LEU-61; GLN-105 AND ARG-115.
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). Determines synapse
CC formation (PubMed:15035988, PubMed:21858180, PubMed:24485456). Required
CC for correct localization of syg-1 at synaptic sites (PubMed:15035988).
CC {ECO:0000269|PubMed:15035988, ECO:0000269|PubMed:21858180,
CC ECO:0000269|PubMed:24485456}.
CC -!- SUBUNIT: Interacts with syg-1. {ECO:0000269|PubMed:21858180,
CC ECO:0000269|PubMed:24485456}.
CC -!- INTERACTION:
CC Q9U3P2; B1Q236: syg-1; NbExp=5; IntAct=EBI-9211201, EBI-321771;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000255}. Synapse {ECO:0000269|PubMed:24485456}.
CC -!- TISSUE SPECIFICITY: Expressed in vulval epithelial cells.
CC {ECO:0000269|PubMed:18675916, ECO:0000269|PubMed:21858180}.
CC -!- DEVELOPMENTAL STAGE: Expressed in head neurons and body wall muscles
CC during embryogenesis (PubMed:15035988). Expressed in head and body wall
CC muscles and in punctate structures near the ventral nerve cord during
CC larval stages L1 and L2 (PubMed:15035988). Expressed in primary vulval
CC epithelial cells from larval stage L3, with expression increasing upon
CC entry into L4 and diminished within six hours of adulthood
CC (PubMed:15035988, PubMed:18675916). {ECO:0000269|PubMed:15035988,
CC ECO:0000269|PubMed:18675916}.
CC -!- DOMAIN: The first five extracellular Ig-like domains are required for
CC correct localization of syg-1. {ECO:0000269|PubMed:18675916}.
CC -!- DOMAIN: The cytoplasmic domain is necessary for syg-2 subcellular
CC localization. {ECO:0000269|PubMed:18675916}.
CC -!- DISRUPTION PHENOTYPE: Animals are viable, fertile, egg-laying
CC proficient and coordinated. Abnormal synaptic vesicle clustering in the
CC HSNL motor neuron from larval stage L3 through to adulthood. Reduced
CC accumulation of synaptic vesicle proteins snb-1 and cat-1 in HSNL motor
CC neuron. Defective synapse specificity due to altered distribution of
CC synapses. syg-1 is mis-localized and diffusely distributed on the axon
CC of the HSNL neuron. {ECO:0000269|PubMed:15035988}.
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DR EMBL; BX284606; CAB63432.1; -; Genomic_DNA.
DR RefSeq; NP_001309467.1; NM_001322664.1.
DR PDB; 4OFK; X-ray; 1.80 A; A/B=327-430.
DR PDB; 4OFP; X-ray; 3.00 A; A/B/C/D=231-430.
DR PDB; 4OFY; X-ray; 3.30 A; D/E/F=20-430.
DR PDBsum; 4OFK; -.
DR PDBsum; 4OFP; -.
DR PDBsum; 4OFY; -.
DR AlphaFoldDB; Q9U3P2; -.
DR SMR; Q9U3P2; -.
DR ComplexPortal; CPX-2973; syg-1-syg-2 cell adhesion complex.
DR IntAct; Q9U3P2; 1.
DR STRING; 6239.C26G2.1b.1; -.
DR GlyCosmos; Q9U3P2; 7 sites, No reported glycans.
DR EPD; Q9U3P2; -.
DR PaxDb; 6239-C26G2-1; -.
DR PeptideAtlas; Q9U3P2; -.
DR EnsemblMetazoa; C26G2.1a.1; C26G2.1a.1; WBGene00007750.
DR GeneID; 181561; -.
DR UCSC; C26G2.1; c. elegans.
DR AGR; WB:WBGene00007750; -.
DR WormBase; C26G2.1a; CE51296; WBGene00007750; syg-2.
DR eggNOG; KOG3515; Eukaryota.
DR HOGENOM; CLU_003881_1_0_1; -.
DR InParanoid; Q9U3P2; -.
DR OMA; CEVSNIM; -.
DR PhylomeDB; Q9U3P2; -.
DR Reactome; R-CEL-373753; Nephrin family interactions.
DR PRO; PR:Q9U3P2; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00007750; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR ExpressionAtlas; Q9U3P2; baseline and differential.
DR GO; GO:0005911; C:cell-cell junction; 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:0097060; C:synaptic membrane; IDA:ComplexPortal.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:WormBase.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
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:0035418; P:protein localization to synapse; 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 CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 10.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
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 InterPro; IPR013106; Ig_V-set.
DR PANTHER; PTHR11640:SF164; MAM DOMAIN-CONTAINING GLYCOSYLPHOSPHATIDYLINOSITOL ANCHOR PROTEIN 1; 1.
DR PANTHER; PTHR11640; NEPHRIN; 1.
DR Pfam; PF08205; C2-set_2; 2.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF13927; Ig_3; 2.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 8.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 8.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Neurogenesis; Reference proteome; Repeat;
KW Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1270
FT /note="Synaptogenesis protein syg-2"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433879"
FT TOPO_DOM 20..1084
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1085..1105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1106..1270
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 20..120
FT /note="Ig-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 126..221
FT /note="Ig-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 235..324
FT /note="Ig-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 331..426
FT /note="Ig-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 431..576
FT /note="Ig-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 581..685
FT /note="Ig-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 782..866
FT /note="Ig-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 872..965
FT /note="Ig-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 976..1066
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1231..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:4OFY"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:4OFY"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:4OFY"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:4OFY"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:4OFP, ECO:0007744|PDB:4OFY"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:4OFY"
FT CARBOHYD 391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PDB:4OFK, ECO:0007744|PDB:4OFP"
FT DISULFID 40..104
FT /evidence="ECO:0007744|PDB:4OFY"
FT DISULFID 152..209
FT /evidence="ECO:0007744|PDB:4OFY"
FT DISULFID 256..308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 352..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 454..558
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 606..667
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 803..850
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 895..953
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT MUTAGEN 53
FT /note="Q->A: Reduced syg-1 binding."
FT /evidence="ECO:0000269|PubMed:24485456"
FT MUTAGEN 61
FT /note="L->A: Reduced syg-1 binding."
FT /evidence="ECO:0000269|PubMed:24485456"
FT MUTAGEN 105
FT /note="Q->A: Loss of syg-1 interaction."
FT /evidence="ECO:0000269|PubMed:24485456"
FT MUTAGEN 115
FT /note="R->A: Reduced syg-1 binding."
FT /evidence="ECO:0000269|PubMed:24485456"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:4OFY"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 148..159
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 188..196
FT /evidence="ECO:0007829|PDB:4OFY"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:4OFY"
FT TURN 214..217
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 218..230
FT /evidence="ECO:0007829|PDB:4OFY"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:4OFP"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:4OFP"
FT STRAND 251..259
FT /evidence="ECO:0007829|PDB:4OFP"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:4OFP"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:4OFP"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:4OFY"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:4OFP"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:4OFP"
FT STRAND 299..311
FT /evidence="ECO:0007829|PDB:4OFP"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:4OFP"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:4OFP"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:4OFK"
FT STRAND 340..343
FT /evidence="ECO:0007829|PDB:4OFK"
FT STRAND 346..354
FT /evidence="ECO:0007829|PDB:4OFK"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:4OFK"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:4OFK"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:4OFK"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:4OFK"
FT STRAND 383..395
FT /evidence="ECO:0007829|PDB:4OFK"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:4OFK"
FT STRAND 405..414
FT /evidence="ECO:0007829|PDB:4OFK"
FT STRAND 417..428
FT /evidence="ECO:0007829|PDB:4OFK"
SQ SEQUENCE 1270 AA; 142027 MW; D2E8B0A8935B4AB5 CRC64;
MLSQAILLWL FGSIHISSQF FLESPSNLST IAGESITFRC SAEKSPEPIV YSQWKSNTGS
LLGYHQEGIL PGHQGRFSYI KQNAEELHLK ITHVNLDDDG EYECQMLHPE EGPIRAKSFL
NIIVPPQLVY FSNYQPNSII AVKENTPLNI TCVVPNVKPE PEVLWYMDGK VMSRDVKQAS
TPHLNKTFTV YTSLVVQSDR NDHGKVITCE AFQKETDIRI TTNTTLDVLF PPSDPTVEIL
RNPSALRSGD NVTIACSVTG GNPPPDVFWY HENKRLQSHS TLDTRSKEIK NIYSFIASQN
DNMAEYECRA NNSRTGNPKR KAMKLEVNYP PASVELFGES NIRYGSSANI QCKSLPSNPA
SQITWIINGR SVPTPTQREF VVENGIVSSS NVSVHSNELS VEAHQINVEC MATNPEGSSA
KQHVIKIIAP PKAPIITGLE DRKFFEGDIV NVTCEAQGGN PLAELSWYRG SEKHLVKGRK
KMKWSQVKKK LVMSLLCLCE VVIMNFFRFS KNVFYFFRFT LFIECGVNGA HNEVAGFSSY
STLALRVDRT MNTQRLKCEA TNAALDEPLI ESQYLSVYYP PRRVLIRPAD SGDQRLLVGK
SARLVCGTLS SNPAAHISWQ FSRATDDNKV HLGDVSLNET TRDNGFNVEN VLSFTPTEEY
DGTVVHCIAN HPEWKHSVNT SFPLNVMYPP KMLVNDPVTV VMSEGDSFKE NLTVRGNPAI
SLWQWRKNGV PFDHTIGRVF ARGAVLSGKQ LLSTDAGVYT LTATNSVGST NITIKLAVEY
SARITSISTP VIAATGDTVL LECEADGEPS KANMIHWYKN GEILAAQHRG HKKAILRLNA
TEQQSGEYTC KADNGIGVPA EGQTFLLVNS APRVLPVARY AKTAGILGGV AKARCKVYAV
PTVEFVWEKD EQLIKKNSSK YSIVNTQIDY STYESTLWIK NIVPDDYTKK VKCIARNSFG
TDHLSIPIIP PTHPDEPFNL TMTNSTLNTI SVAWEPRFDG GSDQIFEVKY RRQNDDLIHL
VNTTHTNLRL SGLATANTYF FQIRSINARG FASSWTSPVI FATLNEDGVN VAMIRNEKLK
LTTWIPYILI FIVLFMLLNV VICCFVCNRT KKRKLREKTE MARTAINGGD VRQVQMYGTM
MGNDGMSRRD IDDRPEMSED EHSVRTMIEV SPNGYMQPIE PMLYESTGLL EYDYQTRSYM
GSSQGTRSMT YANVPYPEPP QPSYHSNWNS LQRQSNNNTS PQHHLSTFIN PNMGVRAGPI
NYAQLDGDLV
//
