PAT3_CAEEL
ID PAT3_CAEEL Reviewed; 809 AA.
AC Q27874;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Integrin beta pat-3;
DE AltName: Full=Paralyzed arrest at two-fold protein 3;
DE Flags: Precursor;
GN Name=pat-3 {ECO:0000312|WormBase:ZK1058.2};
GN ORFNames=ZK1058.2 {ECO:0000312|WormBase:ZK1058.2};
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 [GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7744961; DOI=10.1083/jcb.129.4.1127;
RA Gettner S.N., Kenyon C., Reichardt L.F.;
RT "Characterization of beta pat-3 heterodimers, a family of essential
RT integrin receptors in C. elegans.";
RL J. Cell Biol. 129:1127-1141(1995).
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 INTERACTION WITH INA-1, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=9247263; DOI=10.1016/s0896-6273(00)80347-5;
RA Baum P.D., Garriga G.;
RT "Neuronal migrations and axon fasciculation are disrupted in ina-1 integrin
RT mutants.";
RL Neuron 19:51-62(1997).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-400, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=12754521; DOI=10.1038/nbt829;
RA Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J.,
RA Kasai K., Takahashi N., Isobe T.;
RT "Lectin affinity capture, isotope-coded tagging and mass spectrometry to
RT identify N-linked glycoproteins.";
RL Nat. Biotechnol. 21:667-672(2003).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-141 AND ASN-269, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15888633; DOI=10.1093/glycob/cwi075;
RA Fan X., She Y.-M., Bagshaw R.D., Callahan J.W., Schachter H., Mahuran D.J.;
RT "Identification of the hydrophobic glycoproteins of Caenorhabditis
RT elegans.";
RL Glycobiology 15:952-964(2005).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17326220; DOI=10.1002/dvdy.21091;
RA Ono K., Yu R., Ono S.;
RT "Structural components of the nonstriated contractile apparatuses in the
RT Caenorhabditis elegans gonadal myoepithelial sheath and their essential
RT roles for ovulation.";
RL Dev. Dyn. 236:1093-1105(2007).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-141; ASN-269; ASN-400; ASN-530
RP AND ASN-672, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19023419; DOI=10.1371/journal.pgen.1000269;
RA Lucanic M., Cheng H.J.;
RT "A RAC/CDC-42-independent GIT/PIX/PAK signaling pathway mediates cell
RT migration in C. elegans.";
RL PLoS Genet. 4:E1000269-E1000269(2008).
RN [9]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=20385102; DOI=10.1016/j.bbrc.2010.04.049;
RA Zaidel-Bar R., Miller S., Kaminsky R., Broday L.;
RT "Molting-specific downregulation of C. elegans body-wall muscle attachment
RT sites: the role of RNF-5 E3 ligase.";
RL Biochem. Biophys. Res. Commun. 395:509-514(2010).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20226672; DOI=10.1016/j.cub.2010.01.062;
RA Hsu T.Y., Wu Y.C.;
RT "Engulfment of apoptotic cells in C. elegans is mediated by integrin
RT alpha/SRC signaling.";
RL Curr. Biol. 20:477-486(2010).
RN [11]
RP FUNCTION, COMPONENT OF AN INTEGRIN CONTAINING ATTACHMENT COMPLEX, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=22253611; DOI=10.1371/journal.pgen.1002471;
RA Etheridge T., Oczypok E.A., Lehmann S., Fields B.D., Shephard F.,
RA Jacobson L.A., Szewczyk N.J.;
RT "Calpains mediate integrin attachment complex maintenance of adult muscle
RT in Caenorhabditis elegans.";
RL PLoS Genet. 8:E1002471-E1002471(2012).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=22479198; DOI=10.1371/journal.pgen.1002602;
RA Joyce P.I., Satija R., Chen M., Kuwabara P.E.;
RT "The atypical calpains: evolutionary analyses and roles in Caenorhabditis
RT elegans cellular degeneration.";
RL PLoS Genet. 8:E1002602-E1002602(2012).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=23283987; DOI=10.1091/mbc.e12-06-0478;
RA Warner A., Xiong G., Qadota H., Rogalski T., Vogl A.W., Moerman D.G.,
RA Benian G.M.;
RT "CPNA-1, a copine domain protein, is located at integrin adhesion sites and
RT is required for myofilament stability in Caenorhabditis elegans.";
RL Mol. Biol. Cell 24:601-616(2013).
RN [14]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT TYR-792, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF TYR-792 AND 796-THR--THR-798.
RX PubMed=28135265; DOI=10.1371/journal.pgen.1006592;
RA Walser M., Umbricht C.A., Froehli E., Nanni P., Hajnal A.;
RT "beta-Integrin de-phosphorylation by the density-enhanced phosphatase DEP-1
RT attenuates EGFR signaling in C. elegans.";
RL PLoS Genet. 13:E1006592-E1006592(2017).
RN [15]
RP FUNCTION, INTERACTION WITH TNS-1, AND MUTAGENESIS OF PRO-790.
RX PubMed=31109965; DOI=10.1523/jneurosci.2059-18.2019;
RA Hisamoto N., Shimizu T., Asai K., Sakai Y., Pastuhov S.I., Hanafusa H.,
RA Matsumoto K.;
RT "C. elegans Tensin Promotes Axon Regeneration by Linking the Met-like SVH-2
RT and Integrin Signaling Pathways.";
RL J. Neurosci. 39:5662-5672(2019).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=32053105; DOI=10.7554/elife.50986;
RA Haag A., Walser M., Henggeler A., Hajnal A.;
RT "The CHORD protein CHP-1 regulates EGF receptor trafficking and signaling
RT in C. elegans and in human cells.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Integrin alpha ina-1/beta pat-3 is a receptor for laminin.
CC Integrin alpha pat-2/beta pat-3 recognizes the sequence R-G-D in its
CC ligands (Probable). Plays a role in cell migration, morphogenesis and
CC probably in cell-cell interactions (PubMed:19023419, PubMed:17326220,
CC PubMed:23283987). During gonad morphogenesis, involved in distal tip
CC cell (DTC)-mediated guidance of gonad elongation, in maintaining their
CC sharp tapering morphology and in their migration (PubMed:19023419).
CC Component of an integrin containing attachment complex, which is
CC required for muscle development and maintenance (PubMed:22253611).
CC Involved in the assembly of dense bodies and M lines during body wall
CC muscle embryonic development by recruiting one of their components,
CC cpna-1, to integrin-mediated attachment sites (PubMed:23283987). May
CC play a similar role in the assembly of dense bodies in gonadal
CC myoepithelial sheath cells (PubMed:17326220). Probably by acting as a
CC receptor for apoptotic cells, plays a role in the clearance of
CC apoptotic cells during mid-embryogenesis (PubMed:20226672). Required
CC for ovulation (PubMed:17326220). Dephosphorylated, probably within the
CC alpha pat-2/beta pat-3 integrin receptor complex, by the phosphatase
CC dep-1, which leads to down-stream effects including the negative
CC regulation of let-23 signaling and vulval induction (PubMed:28135265).
CC When unphosphosphorylated, recruits the cytoplasmic adapter protein
CC tln-1 to the plasma membrane of secondary vulval precursor cells
CC (PubMed:28135265). This promotes the linking of focal adhesion sites to
CC the F-actin cytoskeleton, and it also acts to restrict the mobility of
CC the let-23 receptor on the plasma membrane of vulval cells which
CC thereby attenuates let-23 signaling (PubMed:28135265). Plays a role in
CC axon regeneration after injury (PubMed:31109965).
CC {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:19023419,
CC ECO:0000269|PubMed:20226672, ECO:0000269|PubMed:22253611,
CC ECO:0000269|PubMed:23283987, ECO:0000269|PubMed:28135265,
CC ECO:0000269|PubMed:31109965, ECO:0000305}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (Probable).
CC Interacts with alpha subunit ina-1 (PubMed:9247263). Interacts with
CC alpha subunit pat-2 (Probable). Component of an integrin containing
CC attachment complex, composed of at least pat-2, pat-3, pat-4, pat-6,
CC unc-52, unc-97 and unc-112 (PubMed:22253611). May interact with tns-1
CC (via C-terminus) (PubMed:31109965). {ECO:0000269|PubMed:31109965,
CC ECO:0000269|PubMed:9247263, ECO:0000305, ECO:0000305|PubMed:22253611}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9247263};
CC Single-pass type I membrane protein {ECO:0000305}. Lateral cell
CC membrane {ECO:0000269|PubMed:28135265}; Single-pass type I membrane
CC protein {ECO:0000305}. Basolateral cell membrane
CC {ECO:0000269|PubMed:28135265, ECO:0000269|PubMed:32053105}; Single-pass
CC type I membrane protein {ECO:0000305}. Cytoplasm, myofibril, sarcomere,
CC M line {ECO:0000269|PubMed:22479198, ECO:0000269|PubMed:23283987}. Cell
CC junction, focal adhesion {ECO:0000269|PubMed:20385102}. Note=In body
CC wall muscle cells localizes to the base of thick filament M-lines,
CC dense bodies (Z-disks) and in adhesion plaques which form between
CC adjacent cells (PubMed:22479198, PubMed:20385102). In body wall
CC muscles, colocalizes with cpna-1 at integrin adhesion structures (M
CC line and dense bodies) (PubMed:23283987). Decreased localization to
CC dense bodies during the L2/L3 molt (PubMed:20385102). In myoepithelial
CC sheath cells, colocalizes in dense bodies-like structures with actin
CC thin filaments, deb-1/vinculin and unc-52 (PubMed:17326220).
CC {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:20385102,
CC ECO:0000269|PubMed:22479198, ECO:0000269|PubMed:23283987}.
CC -!- TISSUE SPECIFICITY: Expressed in body wall muscles (at protein level)
CC (PubMed:23283987, PubMed:20385102). Expressed in gonadal sheath cells
CC and spermatheca (PubMed:17326220). Expressed in vulval cells and along
CC the basal laminae that separate the vulval cells from the uterus (at
CC the protein level) (PubMed:28135265). {ECO:0000269|PubMed:17326220,
CC ECO:0000269|PubMed:20385102, ECO:0000269|PubMed:23283987,
CC ECO:0000269|PubMed:28135265}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos (PubMed:9247263,
CC PubMed:23283987). Highly expressed in mid to late L3 stage larvae
CC (PubMed:28135265). Expressed in adult animals (PubMed:20385102).
CC {ECO:0000269|PubMed:20385102, ECO:0000269|PubMed:23283987,
CC ECO:0000269|PubMed:28135265, ECO:0000269|PubMed:9247263}.
CC -!- PTM: Phosphorylated. Dephosphorylated by dep-1.
CC {ECO:0000269|PubMed:28135265}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in distal tip cell (DTC)
CC causes DTC migration and guidance defects during the second phase of
CC gonad elongation resulting in a triangular shaped gonad
CC (PubMed:19023419). Embryos at the comma and 1.5-fold stages have
CC increased number of cell corpses (PubMed:20226672). RNAi-mediated
CC knockdown causes an accumulation in the proximal gonad of endomitotic
CC mature oocytes (PubMed:17326220). RNAi-mediated knockdown results in
CC increased mobility of let-23 receptor on the plasma membrane of vulval
CC cells resulting in enhanced activity of the signaling pathway
CC (PubMed:28135265). RNAi-mediated knockdown in vulval precursor cells in
CC a let-60 gain of function mutant background results in increased vulval
CC induction and an adjacent primary fate (Apf) phenotype whereby
CC secondary vulval precursor cells transform into primary-like vulval
CC cells (PubMed:28135265). RNAi-mediated knockdown results in impaired
CC mobility, mitochondrial fragmentation and disrupted integrin attachment
CC complexes in muscle (PubMed:22253611). This leads to degradation of
CC muscle proteins in the cytosol, myofibrillar defects and disruption of
CC sarcomere organization (PubMed:22253611). {ECO:0000269|PubMed:17326220,
CC ECO:0000269|PubMed:19023419, ECO:0000269|PubMed:20226672,
CC ECO:0000269|PubMed:22253611, ECO:0000269|PubMed:28135265}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; U19744; AAA85704.1; -; Genomic_DNA.
DR EMBL; BX284603; CAA84677.1; -; Genomic_DNA.
DR PIR; A57283; A57283.
DR RefSeq; NP_497787.1; NM_065386.5.
DR AlphaFoldDB; Q27874; -.
DR SMR; Q27874; -.
DR BioGRID; 40742; 18.
DR DIP; DIP-27060N; -.
DR IntAct; Q27874; 3.
DR STRING; 6239.ZK1058.2; -.
DR iPTMnet; Q27874; -.
DR EPD; Q27874; -.
DR PaxDb; Q27874; -.
DR PeptideAtlas; Q27874; -.
DR EnsemblMetazoa; ZK1058.2.1; ZK1058.2.1; WBGene00003930.
DR GeneID; 175504; -.
DR KEGG; cel:CELE_ZK1058.2; -.
DR UCSC; ZK1058.2; c. elegans.
DR CTD; 175504; -.
DR WormBase; ZK1058.2; CE01102; WBGene00003930; pat-3.
DR eggNOG; KOG1226; Eukaryota.
DR GeneTree; ENSGT01030000234611; -.
DR HOGENOM; CLU_011772_1_0_1; -.
DR InParanoid; Q27874; -.
DR OMA; NCVCGAC; -.
DR OrthoDB; 473040at2759; -.
DR PhylomeDB; Q27874; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-1236973; Cross-presentation of particulate exogenous antigens (phagosomes).
DR Reactome; R-CEL-1566977; Fibronectin matrix formation.
DR Reactome; R-CEL-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-CEL-210990; PECAM1 interactions.
DR Reactome; R-CEL-210991; Basigin interactions.
DR Reactome; R-CEL-216083; Integrin cell surface interactions.
DR Reactome; R-CEL-3000157; Laminin interactions.
DR Reactome; R-CEL-3000170; Syndecan interactions.
DR Reactome; R-CEL-3000178; ECM proteoglycans.
DR Reactome; R-CEL-354192; Integrin signaling.
DR Reactome; R-CEL-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
DR Reactome; R-CEL-445144; Signal transduction by L1.
DR Reactome; R-CEL-446107; Type I hemidesmosome assembly.
DR Reactome; R-CEL-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
DR Reactome; R-CEL-5674135; MAP2K and MAPK activation.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR PRO; PR:Q27874; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003930; Expressed in embryo and 4 other tissues.
DR GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IDA:WormBase.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0008305; C:integrin complex; IPI:WormBase.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0031430; C:M band; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:WormBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:WormBase.
DR GO; GO:0055120; C:striated muscle dense body; IDA:UniProtKB.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:UniProtKB.
DR GO; GO:0055001; P:muscle cell development; IMP:WormBase.
DR GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0048680; P:positive regulation of axon regeneration; IDA:UniProtKB.
DR GO; GO:1903356; P:positive regulation of distal tip cell migration; IMP:UniProtKB.
DR GO; GO:0040017; P:positive regulation of locomotion; IMP:UniProtKB.
DR GO; GO:1904901; P:positive regulation of myosin II filament organization; IMP:UniProtKB.
DR GO; GO:0060279; P:positive regulation of ovulation; IMP:UniProtKB.
DR GO; GO:0060298; P:positive regulation of sarcomere organization; IMP:UniProtKB.
DR GO; GO:0045987; P:positive regulation of smooth muscle contraction; IMP:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:1903354; P:regulation of distal tip cell migration; IMP:UniProtKB.
DR GO; GO:0040028; P:regulation of vulval development; IGI:UniProtKB.
DR GO; GO:0055002; P:striated muscle cell development; IMP:UniProtKB.
DR GO; GO:0072327; P:vulval cell fate specification; IGI:UniProtKB.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; PTHR10082; 1.
DR Pfam; PF07974; EGF_2; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 1.
DR SUPFAM; SSF69687; SSF69687; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cell membrane; Cytoplasm; Glycoprotein;
KW Integrin; Membrane; Phosphoprotein; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..809
FT /note="Integrin beta pat-3"
FT /id="PRO_0000016358"
FT TOPO_DOM 20..737
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 759..809
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 153..352
FT /note="VWFA"
FT MOD_RES 792
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:28135265"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15888633,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 373
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 672
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 693
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 790
FT /note="P->L: In ok804163; Impairs axon regeneration after
FT injury."
FT /evidence="ECO:0000269|PubMed:31109965"
FT MUTAGEN 792
FT /note="Y->F: In zh105; abolishes phosphorylation and
FT enhances recruitment of tln-1 to the plasma membrane.
FT Reduces the vulval lumen diameter and partially suppresses
FT the Apf phenotype caused by hyperactive let-23 signaling in
FT the double dep-1/lip-1 loss of function mutant. Increases
FT vulval induction in the dep-1/lin-7 loss of function
FT mutant."
FT /evidence="ECO:0000269|PubMed:28135265"
FT MUTAGEN 796..798
FT /note="TTT->AAA: Abolishes association with the phosphatase
FT dep-1."
FT /evidence="ECO:0000269|PubMed:28135265"
SQ SEQUENCE 809 AA; 90138 MW; 70C4AB01C8FE9189 CRC64;
MPPSTSLLLL AALLPFALPA SDWKTGEVTG KVVEKSEFPC YSLSRDNYTC SACIQYHESC
AWCGAPMFDE KKPYARCDSR AKLMEHGCPN SYIEDPATKL DITEDSKLSD QGQVESEEEA
VQIKPQEMYV EIRPKSRVRF NVTYRQAVDY PVDLYYLMDL SYSMKDDKQK LSELGDLLAE
RMRTVTKNFR LGFGSFIDKK LMPFIDPRIE KQLSPCPTPC AEPYGFKHQM SLTTNTAKFK
AEVDKAEISG NLDAPEGGFD AVVQALACNK TIGWRERARK MIVFSTDAGF HFAGDGRLAG
VVEPNDGTCH LDREGYYTET LNQDYPSIAL LHQMIKDRKA NVIFAVTKNN QDLYTQLSNA
LPDVSSSVGV LANDSRNIVD LIEKEYLKIS EKIIMVDNAN ASEGLKLTYR SMCLDGTTLK
DTNVCEGIRV GDEVQFEVTL ENTHCIDKRD FVLRIGPSGL DETLIVNVKV LCDCDCERQD
RIVTNSADCN GGDMVCGVCR CKGGNVGKYC ECNRPGMSTA ALNEKCKRTN ESAICEGRGV
CNCGRCECNP RANPEEQISG EFCECDNFNC PRHDRKICAE HGECNCGKCI CAPGWTGRAC
ECPISTDSCL SANGKICNGK GECICGRCRC FDSPDGNRYS GAKCEICPTC PTKCVEYKNC
VMCQQWQTGP LNETACDQCE FKVIPVEELP NLNETTPCQF VDPADDCTFY YLYYYDEATD
NATVWVRKHK DCPPPVPVLA IVLGVIAGIV ILGILLLLLW KLLTVLHDRS EYATFNNERL
MAKWDTNENP IYKQATTTFK NPVYAGKAN
