GenomeNet

Database: UniProt
Entry: Q27874
LinkDB: Q27874
Original site: Q27874 
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   10-APR-2019, entry version 164.
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
RT   investigating 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
RT   integrin mutants.";
RL   Neuron 19:51-62(1997).
RN   [4]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-400, AND IDENTIFICATION BY
RP   MASS 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
RT   to 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.,
RA   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
RT   the Caenorhabditis elegans gonadal myoepithelial sheath and their
RT   essential roles for ovulation.";
RL   Dev. Dyn. 236:1093-1105(2007).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-141; ASN-269; ASN-400;
RP   ASN-530 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
RT   attachment 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
RT   muscle 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
RT   Caenorhabditis 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
RT   sites and is required for myofilament stability in Caenorhabditis
RT   elegans.";
RL   Mol. Biol. Cell 24:601-616(2013).
RN   [14]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PHOSPHORYLATION AT TYR-792,
RP   DISRUPTION 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
RT   DEP-1 attenuates EGFR signaling in C. elegans.";
RL   PLoS Genet. 13:E1006592-E1006592(2017).
CC   -!- FUNCTION: Integrin alpha ina-1/beta pat-3 is a receptor for
CC       laminin. Integrin alpha pat-2/beta pat-3 recognizes the sequence
CC       R-G-D in its ligands (Probable). Plays a role in cell migration,
CC       morphogenesis and probably in cell-cell interactions
CC       (PubMed:19023419, PubMed:17326220, PubMed:23283987). During gonad
CC       morphogenesis, involved in distal tip cell (DTC)-mediated guidance
CC       of gonad elongation, in maintaining their sharp tapering
CC       morphology and in their migration (PubMed:19023419). Component of
CC       an integrin containing attachment complex, which is required for
CC       muscle development and maintenance (PubMed:22253611). Involved in
CC       the assembly of dense bodies and M lines during body wall muscle
CC       embryonic development by recruiting one of their components, cpna-
CC       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
CC       as a receptor for apoptotic cells, plays a role in the clearance
CC       of apoptotic cells during mid-embryogenesis (PubMed:20226672).
CC       Required for ovulation (PubMed:17326220). Dephosphorylated,
CC       probably within the alpha pat-2/beta pat-3 integrin receptor
CC       complex, by the phosphatase dep-1, which leads to down-stream
CC       effects including the negative regulation of let-23 signaling and
CC       vulval induction (PubMed:28135265). When unphosphosphorylated,
CC       recruits the cytoplasmic adapter protein tln-1 to the plasma
CC       membrane of secondary vulval precursor cells (PubMed:28135265).
CC       This promotes the linking of focal adhesion sites to the F-actin
CC       cytoskeleton, and it also acts to restrict the mobility of the
CC       let-23 receptor on the plasma membrane of vulval cells which
CC       thereby attenuates let-23 signaling (PubMed:28135265).
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:0000305}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit (Probable).
CC       Interacts with alpha subunit ina-1 (PubMed:9247263). Interacts
CC       with alpha subunit pat-2 (Probable). Component of an integrin
CC       containing attachment complex, composed of at least pat-2, pat-3,
CC       pat-4, pat-6, unc-52, unc-97 and unc-112 (PubMed:22253611).
CC       {ECO:0000269|PubMed:9247263, ECO:0000305,
CC       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
CC       membrane protein {ECO:0000305}. Basal cell membrane
CC       {ECO:0000269|PubMed:28135265}; Single-pass type I membrane protein
CC       {ECO:0000305}. Cytoplasm, myofibril, sarcomere, M line
CC       {ECO:0000269|PubMed:22479198, ECO:0000269|PubMed:23283987}. Cell
CC       junction, focal adhesion {ECO:0000269|PubMed:20385102}. Note=In
CC       body wall muscle cells localizes to the base of thick filament M-
CC       lines, dense bodies (Z-disks) and in adhesion plaques which form
CC       between adjacent cells (PubMed:22479198, PubMed:20385102). In body
CC       wall muscles, colocalizes with cpna-1 at integrin adhesion
CC       structures (M line and dense bodies) (PubMed:23283987). Deacreased
CC       localization to dense bodies during the L2/L3 molt
CC       (PubMed:20385102). In myoepithelial sheath cells, colocalizes in
CC       dense bodies-like structures with actin thin filaments, deb-
CC       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
CC       level) (PubMed:23283987, PubMed:20385102). Expressed in gonadal
CC       sheath cells and spermatheca (PubMed:17326220). Expressed in
CC       vulval cells and along the basal laminae that separate the vulval
CC       cells from the uterus (at the protein level) (PubMed:28135265).
CC       {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:20385102,
CC       ECO:0000269|PubMed:23283987, 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
CC       (DTC) causes DTC migration and guidance defects during the second
CC       phase of 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
CC       endomitotic mature oocytes (PubMed:17326220). RNAi-mediated
CC       knockdown results in increased mobility of let-23 receptor on the
CC       plasma membrane of vulval cells resulting in enhanced activity of
CC       the signaling pathway (PubMed:28135265). RNAi-mediated knockdown
CC       in vulval precursor cells in a let-60 gain of function mutant
CC       background results in increased vulval induction and an adjacent
CC       primary fate (Apf) phenotype whereby secondary vulval precursor
CC       cells transform into primary-like vulval cells (PubMed:28135265).
CC       RNAi-mediated knockdown results in impaired mobility,
CC       mitochondrial fragmentation and disrupted integrin attachment
CC       complexes in muscle (PubMed:22253611). This leads to degradation
CC       of muscle proteins in the cytosol, myofibrillar defects and
CC       disruption of sarcomere organization (PubMed:22253611).
CC       {ECO:0000269|PubMed:17326220, ECO:0000269|PubMed:19023419,
CC       ECO:0000269|PubMed:20226672, ECO:0000269|PubMed:22253611,
CC       ECO:0000269|PubMed:28135265}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
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   UniGene; Cel.5347; -.
DR   ProteinModelPortal; Q27874; -.
DR   SMR; Q27874; -.
DR   BioGrid; 40742; 11.
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   PRIDE; Q27874; -.
DR   EnsemblMetazoa; ZK1058.2; ZK1058.2; 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   eggNOG; ENOG410XP60; LUCA.
DR   GeneTree; ENSGT00950000182617; -.
DR   HOGENOM; HOG000252936; -.
DR   InParanoid; Q27874; -.
DR   KO; K05719; -.
DR   OMA; VVETPEC; -.
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-1566948; Elastic fibre formation.
DR   Reactome; R-CEL-2129379; Molecules associated with elastic fibres.
DR   Reactome; R-CEL-216083; Integrin cell surface interactions.
DR   Reactome; R-CEL-3000170; Syndecan interactions.
DR   Reactome; R-CEL-354192; Integrin alphaIIb beta3 signaling.
DR   Reactome; R-CEL-4420097; VEGFA-VEGFR2 Pathway.
DR   Reactome; R-CEL-445144; Signal transduction by L1.
DR   Reactome; R-CEL-445355; Smooth Muscle Contraction.
DR   Reactome; R-CEL-446343; Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   Reactome; R-CEL-8874081; MET activates PTK2 signaling.
DR   SignaLink; Q27874; -.
DR   PRO; PR:Q27874; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00003930; Expressed in 5 organ(s), highest expression level in multi-cellular organism.
DR   GO; GO:0009925; C:basal plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IDA:WormBase.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
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: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: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; Complete proteome;
KW   Cytoplasm; Glycoprotein; Integrin; Membrane; Phosphoprotein; Receptor;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     19       {ECO:0000255}.
FT   CHAIN        20    809       Integrin beta pat-3.
FT                                /FTId=PRO_0000016358.
FT   TOPO_DOM     20    737       Extracellular. {ECO:0000255}.
FT   TRANSMEM    738    758       Helical. {ECO:0000255}.
FT   TOPO_DOM    759    809       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      153    352       VWFA.
FT   MOD_RES     792    792       Phosphotyrosine.
FT                                {ECO:0000269|PubMed:28135265}.
FT   CARBOHYD     47     47       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    141    141       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:15888633,
FT                                ECO:0000269|PubMed:17761667}.
FT   CARBOHYD    269    269       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:15888633,
FT                                ECO:0000269|PubMed:17761667}.
FT   CARBOHYD    373    373       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    400    400       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:12754521,
FT                                ECO:0000269|PubMed:17761667}.
FT   CARBOHYD    530    530       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:17761667}.
FT   CARBOHYD    672    672       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:17761667}.
FT   CARBOHYD    693    693       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    721    721       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   MUTAGEN     792    792       Y->F: In zh105; abolishes phosphorylation
FT                                and enhances recruitment of tln-1 to the
FT                                plasma membrane. Reduces the vulval lumen
FT                                diameter and partially suppresses the Apf
FT                                phenotype caused by hyperactive let-23
FT                                signaling in the double dep-1/lip-1 loss
FT                                of function mutant. Increases vulval
FT                                induction in the dep-1/lin-7 loss of
FT                                function mutant.
FT                                {ECO:0000269|PubMed:28135265}.
FT   MUTAGEN     796    798       TTT->AAA: Abolishes association with the
FT                                phosphatase dep-1.
FT                                {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
//
DBGET integrated database retrieval system