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SYG2_CAEEL
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   03-AUG-2022, entry version 165.
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.C26G2.1; -.
DR   EPD; Q9U3P2; -.
DR   PaxDb; Q9U3P2; -.
DR   PeptideAtlas; Q9U3P2; -.
DR   EnsemblMetazoa; C26G2.1a.1; C26G2.1a.1; WBGene00007750.
DR   GeneID; 181561; -.
DR   UCSC; C26G2.1; c. elegans.
DR   CTD; 181561; -.
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   PRO; PR:Q9U3P2; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00007750; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   ExpressionAtlas; Q9U3P2; baseline and differential.
DR   GO; GO:0005911; C:cell-cell junction; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of 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; -; 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   Pfam; PF08205; C2-set_2; 2.
DR   Pfam; PF00041; fn3; 1.
DR   Pfam; PF07679; I-set; 2.
DR   SMART; SM00060; FN3; 1.
DR   SMART; SM00409; IG; 6.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF48726; SSF48726; 8.
DR   SUPFAM; SSF49265; SSF49265; 1.
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
 
 
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