LIPA_CAEEL
ID LIPA_CAEEL Reviewed; 1139 AA.
AC Q21049;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Liprin-alpha;
DE AltName: Full=LAR-interacting protein alpha;
DE AltName: Full=Synapse defective protein 2;
GN Name=syd-2 {ECO:0000312|WormBase:F59F5.6};
GN ORFNames=F59F5.6 {ECO:0000312|WormBase:F59F5.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10517634; DOI=10.1038/43886;
RA Zhen M., Jin Y.;
RT "The liprin protein SYD-2 regulates the differentiation of presynaptic
RT termini in C. elegans.";
RL Nature 401:371-375(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=9624153; DOI=10.1074/jbc.273.25.15611;
RA Serra-Pages C., Medley Q.G., Tang M., Hart A., Streuli M.;
RT "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-
RT interacting proteins.";
RL J. Biol. Chem. 273:15611-15620(1998).
RN [4]
RP FUNCTION.
RX PubMed=19290026; DOI=10.1007/s12264-009-0119-9;
RA Wang D.Y., Wang Y.;
RT "HLB-1 functions as a new regulator for the organization and function of
RT neuromuscular junctions in nematode Caenorhabditis elegans.";
RL Neurosci. Bull. 25:75-86(2009).
CC -!- FUNCTION: May play a role in regulating the structure of the neuronal
CC region, called the active zone, from which synaptic vesicles send
CC neurotransmitter signals across the synapse (PubMed:10517634,
CC PubMed:19290026). This may be in association with the liprin-beta
CC protein hlb-1 (PubMed:19290026). {ECO:0000269|PubMed:10517634,
CC ECO:0000269|PubMed:19290026}.
CC -!- INTERACTION:
CC Q21049; P23678-1: unc-104; NbExp=9; IntAct=EBI-327903, EBI-15812209;
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:10517634}.
CC Note=Presynaptic region.
CC -!- TISSUE SPECIFICITY: Detected in vulval muscle and other cells near the
CC vulva; in neurons located in the lateral ganglion, posterior ganglion,
CC ventral cord and lateral body; and in pharyngeal and body wall muscle
CC cells. {ECO:0000269|PubMed:9624153}.
CC -!- SIMILARITY: Belongs to the liprin family. Liprin-alpha subfamily.
CC {ECO:0000305}.
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DR EMBL; BX284606; CAA90660.1; -; Genomic_DNA.
DR EMBL; AF170122; AAD47840.1; -; mRNA.
DR PIR; T23018; T23018.
DR RefSeq; NP_509768.1; NM_077367.6.
DR AlphaFoldDB; Q21049; -.
DR SMR; Q21049; -.
DR BioGRID; 46167; 9.
DR DIP; DIP-26340N; -.
DR IntAct; Q21049; 2.
DR STRING; 6239.F59F5.6; -.
DR iPTMnet; Q21049; -.
DR EPD; Q21049; -.
DR PaxDb; Q21049; -.
DR PeptideAtlas; Q21049; -.
DR PRIDE; Q21049; -.
DR EnsemblMetazoa; F59F5.6.1; F59F5.6.1; WBGene00006364.
DR EnsemblMetazoa; F59F5.6.2; F59F5.6.2; WBGene00006364.
DR GeneID; 181255; -.
DR KEGG; cel:CELE_F59F5.6; -.
DR UCSC; F59F5.6; c. elegans.
DR CTD; 181255; -.
DR WormBase; F59F5.6; CE03447; WBGene00006364; syd-2.
DR eggNOG; KOG0249; Eukaryota.
DR GeneTree; ENSGT01050000244900; -.
DR HOGENOM; CLU_006923_0_0_1; -.
DR InParanoid; Q21049; -.
DR OMA; KERMVAM; -.
DR OrthoDB; 440941at2759; -.
DR PhylomeDB; Q21049; -.
DR Reactome; R-CEL-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-CEL-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-CEL-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-CEL-388844; Receptor-type tyrosine-protein phosphatases.
DR PRO; PR:Q21049; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006364; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:WormBase.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:GOC.
DR GO; GO:0048786; C:presynaptic active zone; IDA:WormBase.
DR GO; GO:0097445; C:presynaptic active zone dense projection; IDA:WormBase.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0140660; F:cytoskeletal motor activator activity; IMP:WormBase.
DR GO; GO:0019894; F:kinesin binding; IPI:WormBase.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:WormBase.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IMP:WormBase.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; IMP:WormBase.
DR GO; GO:0008088; P:axo-dendritic transport; IGI:WormBase.
DR GO; GO:0040011; P:locomotion; IGI:WormBase.
DR GO; GO:0007626; P:locomotory behavior; IMP:WormBase.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IDA:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:1903744; P:positive regulation of anterograde synaptic vesicle transport; IMP:WormBase.
DR GO; GO:1905608; P:positive regulation of presynapse assembly; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
DR GO; GO:0043113; P:receptor clustering; ISS:WormBase.
DR GO; GO:0050807; P:regulation of synapse organization; IGI:UniProtKB.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IMP:WormBase.
DR GO; GO:0050808; P:synapse organization; IMP:WormBase.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:UniProtKB.
DR CDD; cd09562; SAM_liprin-alpha1_2_3_4_repeat1; 1.
DR CDD; cd09565; SAM_liprin-alpha1_2_3_4_repeat2; 1.
DR CDD; cd09568; SAM_liprin-alpha1_2_3_4_repeat3; 1.
DR Gene3D; 1.10.150.50; -; 3.
DR InterPro; IPR029515; Liprin.
DR InterPro; IPR037620; Liprin-alpha_SAM_rpt_1.
DR InterPro; IPR037621; Liprin-alpha_SAM_rpt_2.
DR InterPro; IPR037622; Liprin-alpha_SAM_rpt_3.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR030442; Syd-2.
DR PANTHER; PTHR12587; PTHR12587; 1.
DR PANTHER; PTHR12587:SF20; PTHR12587:SF20; 1.
DR Pfam; PF00536; SAM_1; 2.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00454; SAM; 3.
DR SUPFAM; SSF47769; SSF47769; 2.
DR PROSITE; PS50105; SAM_DOMAIN; 3.
PE 1: Evidence at protein level;
KW Coiled coil; Reference proteome; Repeat; Synapse.
FT CHAIN 1..1139
FT /note="Liprin-alpha"
FT /id="PRO_0000191038"
FT DOMAIN 867..933
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 952..1016
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 1040..1109
FT /note="SAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 700..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 30..144
FT /evidence="ECO:0000255"
FT COILED 172..298
FT /evidence="ECO:0000255"
FT COILED 329..517
FT /evidence="ECO:0000255"
FT COILED 655..701
FT /evidence="ECO:0000255"
FT COMPBIAS 702..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1139 AA; 130334 MW; 31A34BE5FB5AB99D CRC64;
MSYSNGNINC DIMPTISEDG VDNGGPIDEP SDRDNIEQLM MNMLEDRDKL QEQLENYKVQ
LENAGLRTKE VEKERDMMKR QFEVHTQNLP QELQTMTREL CLLKEQLLEK DEEIVELKAE
RNNTRLLLEH LECLVSRHER SLRMTVMKRQ AQNHAGVSSE VEVLKALKSL FEHHKALDEK
VRERLRVAME RVATLEEELS TKGDENSSLK ARIATYAAEA EEAMASNAPI NGSISSESAN
RLIEMQEALE RMKTELANSL KQSTEITTRN AELEDQLTED AREKHAAQES IVRLKNQICE
LDAQRTDQET RITTFESRFL TAQRESTCIR DLNDKLEHQL ANKDAAVRLN EEKVHSLQER
LELAEKQLAQ SLKKAESLPS VEAELQQRME ALTAAEQKSV SAEERIQRLD RNIQELSAEL
ERAVQRERMN EEHSQRLSST VDKLLSESND RLQLHLKERM QALDDKNRLT QQLDGTKKIY
DQAERIKDRL QRDNESLRQE IEALRQQLYN ARTAQFQSRM HAIPFTHAQN IVQQQPQASI
AQQSAYQMYK QQPAQQYQTV GMRRPNKGRI SALQDDPNKV QTLNEQEWDR LQQAHVLANV
QQAFSSSPSL ADVGQSTLPR PNTAVQHQQD DMMNSGMGMP SGMQGGMQGG MGGGQDAQML
ASMLQDRLDA INTEIRLIQQ EKHHAERVAE QLERSSREFY DDQGISTRSS PRASPQLDNM
RQHKYNTLPA NVSGDRRYDI YGNPQFVDDR MVRDLDYEPR RGYNQFDEMQ YERDRMSPAS
SVASSTDGVL GGKKKRSNSS SGLKTLGRFF NKKKNSSSDL FKRNGDYSDG EQSGTEGNQK
ADYDRRKKKK HELLEEAMKA RTPFALWNGP TVVAWLELWV GMPAWYVAAC RANVKSGAIM
SALSDQEIQK EIGISNPLHR LKLRLAIQEM VSLTSPSAPR TARLTLAFGD MNHEYIGNDW
LPCLGLAQYR SAFMECLLDA RMLEHLSKRD LRTHLRMVDT FHRTSLQYGI MCLKKVNYDK
KVLADRRKAC DNINTDLLVW SNERVQRWVE EIGLGVFSRN LVDSGIHGAL IALDETFDAS
AFAYALQIGS QDVPNRQLLE KKFIGLVNDH RQQSDPHPRS GSSRKNDSIA KSYEFHLYT
