IDA1_CAEEL
ID IDA1_CAEEL Reviewed; 767 AA.
AC G5EGJ5;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase-like ida-1 {ECO:0000305};
DE AltName: Full=Related to islet cell diabetic autoantigen protein {ECO:0000303|PubMed:11086294};
DE Flags: Precursor;
GN Name=ida-1 {ECO:0000303|PubMed:11086294, ECO:0000312|WormBase:B0244.2};
GN Synonyms=ia2 {ECO:0000303|PubMed:11206415};
GN ORFNames=B0244.2 {ECO:0000312|WormBase:B0244.2};
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|EMBL:AAK14908.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=11206415; DOI=10.1007/s001250051583;
RA Cai T., Krause M.W., Odenwald W.F., Toyama R., Notkins A.L.;
RT "The IA-2 gene family: homologs in Caenorhabditis elegans, Drosophila and
RT zebrafish.";
RL Diabetologia 44:81-88(2001).
RN [2] {ECO:0000312|EMBL:CAB52188.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11086294;
RX DOI=10.1002/1096-9861(20000101)429:1<127::aid-cne10>3.0.co;2-h;
RA Zahn T., MacMorris M.A., Dong W., Day R., Hutton J.C.;
RT "IDA-1, a Caenorhabditis elegans homolog of the diabetic autoantigens IA-2
RT and phogrin, is expressed in peptidergic neurons in the worm.";
RL J. Comp. Neurol. 429:127-143(2001).
RN [3] {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 [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15044551; DOI=10.1523/jneurosci.0101-04.2004;
RA Cai T., Fukushige T., Notkins A.L., Krause M.;
RT "Insulinoma-Associated Protein IA-2, a Vesicle Transmembrane Protein,
RT Genetically Interacts with UNC-31/CAPS and Affects Neurosecretion in
RT Caenorhabditis elegans.";
RL J. Neurosci. 24:3115-3124(2004).
RN [5] {ECO:0000305}
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=15180830; DOI=10.1111/j.1600-0854.2004.00195.x;
RA Zahn T.R., Angleson J.K., MacMorris M.A., Domke E., Hutton J.F.,
RA Schwartz C., Hutton J.C.;
RT "Dense core vesicle dynamics in Caenorhabditis elegans neurons and the role
RT of kinesin UNC-104.";
RL Traffic 5:544-559(2004).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17611271; DOI=10.1523/jneurosci.1405-07.2007;
RA Liu T., Kim K., Li C., Barr M.M.;
RT "FMRFamide-like neuropeptides and mechanosensory touch receptor neurons
RT regulate male sexual turning behavior in Caenorhabditis elegans.";
RL J. Neurosci. 27:7174-7182(2007).
RN [7] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19343207; DOI=10.1371/journal.pgen.1000447;
RA Cai T., Hirai H., Fukushige T., Yu P., Zhang G., Notkins A.L., Krause M.;
RT "Loss of the transcriptional repressor PAG-3/Gfi-1 results in enhanced
RT neurosecretion that is dependent on the dense-core vesicle membrane protein
RT IDA-1/IA-2.";
RL PLoS Genet. 5:E1000447-E1000447(2009).
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27116976; DOI=10.1534/genetics.115.186064;
RA Bhat J.M., Hutter H.;
RT "Pioneer Axon Navigation Is Controlled by AEX-3, a Guanine Nucleotide
RT Exchange Factor for RAB-3 in Caenorhabditis elegans.";
RL Genetics 203:1235-1247(2016).
CC -!- FUNCTION: Regulates dense-core vesicle (DCV) trafficking and/or
CC secretion (PubMed:19343207). Probably by controlling DCV trafficking,
CC plays a role in the AVG neuron-mediated formation of the right axon
CC tract of the ventral nerve cord (PubMed:27116976). Involved in
CC locomotion by regulating acetylcholine release (PubMed:15044551).
CC Probably by controlling the secretion of FLP neuropeptides, regulates
CC the turning step of male mating behavior (PubMed:17611271). Plays a
CC role in preventing dauer formation (PubMed:15044551).
CC {ECO:0000269|PubMed:15044551, ECO:0000269|PubMed:17611271,
CC ECO:0000269|PubMed:19343207, ECO:0000269|PubMed:27116976}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:15180830, ECO:0000305|PubMed:15044551}; Single-pass
CC type I membrane protein {ECO:0000305}. Perikaryon
CC {ECO:0000269|PubMed:15044551, ECO:0000269|PubMed:15180830}. Cell
CC projection, axon {ECO:0000269|PubMed:15044551,
CC ECO:0000269|PubMed:15180830}. Cell projection, dendrite
CC {ECO:0000269|PubMed:15180830}. Note=Localizes to dense-core vesicles
CC along axons. {ECO:0000269|PubMed:15044551,
CC ECO:0000269|PubMed:15180830}.
CC -!- TISSUE SPECIFICITY: In hermaphrodites specifically expressed in neurons
CC and in particular in the head nerve ring (ADE, ALA, ASI, ASK, AUA, ASG,
CC AVH and AVJ neurons), in the ventral nerve cord, pre-anal ganglia (PVP
CC neuron), in the tail (PHA, PHB and PHC neurons) and in vulval motor
CC neurons VC and HSN and the vulval uv1 cells (PubMed:11086294,
CC PubMed:11206415, PubMed:15044551, PubMed:15180830, PubMed:19343207). In
CC males, also expressed in neurons anterior to the nerve ring and male-
CC specific neurons in the tail (PubMed:11086294, PubMed:15180830).
CC {ECO:0000269|PubMed:11086294, ECO:0000269|PubMed:11206415,
CC ECO:0000269|PubMed:15044551, ECO:0000269|PubMed:15180830,
CC ECO:0000269|PubMed:19343207}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages including the dauer stage.
CC Expression in the ventral cord and near the vulva starts at the L4
CC larval stage. {ECO:0000269|PubMed:11086294}.
CC -!- PTM: Proteolytically cleaved probably at a dibasic consensus sequence
CC by egl-3. {ECO:0000269|PubMed:15180830}.
CC -!- DISRUPTION PHENOTYPE: Viable and fertile with a reduced brood size
CC (PubMed:15044551, PubMed:19343207). Locomotion is slightly slower and
CC the expulsion step of the defecation cycle is often missing
CC (PubMed:15044551). In males, impaired mating turning behavior
CC characterized by abnormal repetitive turning during the first turn
CC (PubMed:17611271). 50 percent reduction in dense-core vesicles in
CC ventral cord neurons (PubMed:19343207). Paralysis induced by
CC acetylcholinesterase inhibitor aldicarb is reduced in 50 percent of
CC mutants (PubMed:15044551). Resistant to aldicarb-induced reduction in
CC brood size (PubMed:19343207). In a unc-64 (e246) mutant background
CC increases dauer formation whereas in a unc-31 (e169) abolishes dauer
CC formation (PubMed:15044551). In a daf-2 (e1370) or daf-28 (sa191)
CC mutant background increases dauer formation (PubMed:15044551). In a
CC nid-1 (cg119) mutant background, abnormal cross-over of the AVG neuron
CC axon during the formation of the right axon tract of the ventral nerve
CC cord (PubMed:27116976). {ECO:0000269|PubMed:15044551,
CC ECO:0000269|PubMed:17611271, ECO:0000269|PubMed:19343207,
CC ECO:0000269|PubMed:27116976}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 8 subfamily. {ECO:0000305}.
CC -!- CAUTION: Lacks the typical Cys active site in position 696 that is
CC replaced by a Ser residue, preventing the tyrosine-protein phosphatase
CC activity. {ECO:0000305}.
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DR EMBL; AF126740; AAK14908.1; -; mRNA.
DR EMBL; AJ245560; CAB52188.1; -; mRNA.
DR EMBL; BX284603; CCD61500.1; -; Genomic_DNA.
DR RefSeq; NP_498245.2; NM_065844.5.
DR AlphaFoldDB; G5EGJ5; -.
DR SMR; G5EGJ5; -.
DR STRING; 6239.B0244.2; -.
DR EPD; G5EGJ5; -.
DR PaxDb; G5EGJ5; -.
DR PeptideAtlas; G5EGJ5; -.
DR EnsemblMetazoa; B0244.2.1; B0244.2.1; WBGene00002048.
DR GeneID; 175807; -.
DR KEGG; cel:CELE_B0244.2; -.
DR CTD; 175807; -.
DR WormBase; B0244.2; CE31867; WBGene00002048; ida-1.
DR eggNOG; KOG0793; Eukaryota.
DR GeneTree; ENSGT00940000169984; -.
DR HOGENOM; CLU_383214_0_0_1; -.
DR InParanoid; G5EGJ5; -.
DR OMA; STPEECK; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; G5EGJ5; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:G5EGJ5; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00002048; Expressed in larva and 4 other tissues.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0031045; C:dense core granule; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; TAS:WormBase.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; ISS:WormBase.
DR GO; GO:0006887; P:exocytosis; TAS:WormBase.
DR GO; GO:1905488; P:positive regulation of anterior/posterior axon guidance; IGI:UniProtKB.
DR GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IMP:WormBase.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0051046; P:regulation of secretion; IBA:GO_Central.
DR GO; GO:0007419; P:ventral cord development; IGI:UniProtKB.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR033522; IA-2/IA-2_beta.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR46106; PTHR46106; 2.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..767
FT /note="Receptor-type tyrosine-protein phosphatase-like ida-
FT 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5011414590"
FT TOPO_DOM 20..398
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..767
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 527..756
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 767 AA; 86706 MW; F05A7158404FDEC0 CRC64;
MRFFHSIIVL LFSISTGSAF LLYGCNLSEN LCDNDESCYP DGVFGQCYSS ESGSPEPTVL
DNLDDTQLEL LKLELTRLAA KDKDWGDEET QCVLAYFKMS MFYQLQYDPD FCQVRKPANV
WALIQLIDTG LTEDPTILDE DVNPENVTDE DMAQIIEQLK EPSLPTEEDI EEALNAQNED
VDDEILDQYV QAVVNNENPD FSELSDGQLN ILIGRLVDLK KNVENEEAQL LTGDGEQEMA
VPLDDLEERG EQAILKKDIE QVGEINQGLD NTEHKIVKGR KDQVVTRVDA NRVYLKVHLK
NEDQLMPLIE FLQNTIAIPN NLYFDDFQFE NGQLSMRISR FEGAKPKADK RIDSVEGVAS
AVYKRRKDIA RLSGADVRET GIGSGEDGSL PVESSERDWL LMPVLFVCAF TVTALGLVAA
VQIARSRRHY KDNIQQIAEQ LDGKNSFAYQ DLCRQRADGG RASKSSSTSS WCEETAVPTI
DISTGHVVLN FLQEYLSEPT KIEAQWNGIK DYRNEERTKT KAEKFASQNR TILPFDDNIV
DIDGKTAENE DFYLNASFIY DDDPRQAVYI AAQTPASSQI AAFWQTIWQH GVCLVVNLST
PEECKQEKNY WPDTGSEVHG AFEIHLVSEH IWSDDYLVRS FYLKNLQNSQ TRTITQFHYL
SWQKESTPTS AKSILEFRRK VNKSYRGRSS AVLVHSWDGS GRTGVYCAVD VLCARLLRGI
RQIDVVATVE HLRDQRDGMV ATGDQFKLVY GCVAQEVNHL LKSIATK
