MOM5_CAEEL
ID MOM5_CAEEL Reviewed; 570 AA.
AC A0A0K3AWM6; G5EEF7;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 11-NOV-2015, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Protein mom-5 {ECO:0000303|PubMed:9288750};
DE Flags: Precursor;
GN Name=mom-5 {ECO:0000303|PubMed:9288750, ECO:0000312|WormBase:T23D8.1b};
GN ORFNames=T23D8.1 {ECO:0000312|WormBase:T23D8.1b};
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:AAC47750.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC47750.1};
RX PubMed=9288750; DOI=10.1016/s0092-8674(00)80531-0;
RA Rocheleau C.E., Downs W.D., Lin R., Wittmann C., Bei Y., Cha Y.-H., Ali M.,
RA Priess J.R., Mello C.C.;
RT "Wnt signaling and an APC-related gene specify endoderm in early C. elegans
RT embryos.";
RL Cell 90:707-716(1997).
RN [2] {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 [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9288749; DOI=10.1016/s0092-8674(00)80530-9;
RA Thorpe C.J., Schlesinger A., Carter J.C., Bowerman B.;
RT "Wnt signaling polarizes an early C. elegans blastomere to distinguish
RT endoderm from mesoderm.";
RL Cell 90:695-705(1997).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12810601; DOI=10.1242/dev.00563;
RA Park F.D., Priess J.R.;
RT "Establishment of POP-1 asymmetry in early C. elegans embryos.";
RL Development 130:3547-3556(2003).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15620652; DOI=10.1016/j.cub.2004.12.019;
RA Park F.D., Tenlen J.R., Priess J.R.;
RT "C. elegans MOM-5/frizzled functions in MOM-2/Wnt-independent cell polarity
RT and is localized asymmetrically prior to cell division.";
RL Curr. Biol. 14:2252-2258(2004).
RN [6] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=15990090; DOI=10.1016/j.ydbio.2005.05.024;
RA Hawkins N.C., Ellis G.C., Bowerman B., Garriga G.;
RT "MOM-5 frizzled regulates the distribution of DSH-2 to control C. elegans
RT asymmetric neuroblast divisions.";
RL Dev. Biol. 284:246-259(2005).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16109397; DOI=10.1016/j.ydbio.2005.07.014;
RA Zinovyeva A.Y., Forrester W.C.;
RT "The C. elegans Frizzled CFZ-2 is required for cell migration and interacts
RT with multiple Wnt signaling pathways.";
RL Dev. Biol. 285:447-461(2005).
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16516839; DOI=10.1016/j.devcel.2006.02.010;
RA Pan C.L., Howell J.E., Clark S.G., Hilliard M., Cordes S., Bargmann C.I.,
RA Garriga G.;
RT "Multiple Wnts and frizzled receptors regulate anteriorly directed cell and
RT growth cone migrations in Caenorhabditis elegans.";
RL Dev. Cell 10:367-377(2006).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=16930586; DOI=10.1016/j.ydbio.2006.06.050;
RA Gleason J.E., Szyleyko E.A., Eisenmann D.M.;
RT "Multiple redundant Wnt signaling components function in two processes
RT during C. elegans vulval development.";
RL Dev. Biol. 298:442-457(2006).
RN [10] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20126385; DOI=10.1371/journal.pbio.1000297;
RA Cabello J., Neukomm L.J., Guenesdogan U., Burkart K., Charette S.J.,
RA Lochnit G., Hengartner M.O., Schnabel R.;
RT "The Wnt pathway controls cell death engulfment, spindle orientation, and
RT migration through CED-10/Rac.";
RL PLoS Biol. 8:E1000297-E1000297(2010).
RN [11] {ECO:0000305}
RP FUNCTION.
RX PubMed=22022276; DOI=10.1371/journal.pgen.1002308;
RA Yamamoto Y., Takeshita H., Sawa H.;
RT "Multiple Wnts redundantly control polarity orientation in Caenorhabditis
RT elegans epithelial stem cells.";
RL PLoS Genet. 7:E1002308-E1002308(2011).
RN [12] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=23295860; DOI=10.1038/msb.2012.64;
RA Tan R.Z., Ji N., Mentink R.A., Korswagen H.C., van Oudenaarden A.;
RT "Deconvolving the roles of Wnt ligands and receptors in sensing and
RT amplification.";
RL Mol. Syst. Biol. 9:631-631(2013).
RN [13] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP LYS-343; LYS-430; LYS-442; LYS-445; LYS-541 AND LYS-548.
RX PubMed=24401370; DOI=10.1242/dev.101600;
RA Moffat L.L., Robinson R.E., Bakoulis A., Clark S.G.;
RT "The conserved transmembrane RING finger protein PLR-1 downregulates Wnt
RT signaling by reducing Frizzled, Ror and Ryk cell-surface levels in C.
RT elegans.";
RL Development 141:617-628(2014).
RN [14] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=25373777; DOI=10.1016/j.devcel.2014.08.008;
RA Mentink R.A., Middelkoop T.C., Rella L., Ji N., Tang C.Y., Betist M.C.,
RA van Oudenaarden A., Korswagen H.C.;
RT "Cell intrinsic modulation of Wnt signaling controls neuroblast migration
RT in C. elegans.";
RL Dev. Cell 31:188-201(2014).
RN [15] {ECO:0000305}
RP FUNCTION.
RX PubMed=25917219; DOI=10.1016/j.ydbio.2015.04.015;
RA Chien S.C., Gurling M., Kim C., Craft T., Forrester W., Garriga G.;
RT "Autonomous and nonautonomous regulation of Wnt-mediated neuronal polarity
RT by the C. elegans Ror kinase CAM-1.";
RL Dev. Biol. 404:55-65(2015).
RN [16] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=26292279; DOI=10.1371/journal.pgen.1005446;
RA Levy-Strumpf N., Krizus M., Zheng H., Brown L., Culotti J.G.;
RT "The Wnt frizzled receptor MOM-5 regulates the UNC-5 Netrin receptor
RT through small GTPase-dependent signaling to determine the polarity of
RT migrating cells.";
RL PLoS Genet. 11:E1005446-E1005446(2015).
CC -!- FUNCTION: Receptor for Wnt proteins (PubMed:16930586, PubMed:22022276,
CC PubMed:23295860, PubMed:24401370, PubMed:26292279). Most frizzled
CC receptors are coupled to the beta-catenin canonical signaling pathway,
CC which leads to the activation of disheveled proteins, inhibition of
CC gsk-3 kinase, nuclear accumulation of beta-catenin and activation of
CC Wnt target genes (Probable). A second signaling pathway involving PKC
CC and calcium fluxes has been seen for some family members, but it is not
CC yet clear if it represents a distinct pathway or if it can be
CC integrated in the canonical pathway, as pkc seems to be required for
CC Wnt-mediated inactivation of gsk-3 kinase (Probable). Both pathways
CC seem to involve interactions with G-proteins (Probable). Required in
CC embryonic development for the correct positioning and orientation of
CC the mitotic spindles and division planes in blastomere cells
CC (PubMed:9288749, PubMed:9288750, PubMed:20126385). During early
CC embryonic cell divisions, directs the asymmetric positioning of
CC transcription factors such as pop-1 and dsh-2 in daughter cells in
CC order to determine cell fate specification (PubMed:12810601,
CC PubMed:15620652, PubMed:15990090). Acts redundantly with other Wnt
CC receptors such as lin-17 to control vulval precursor cell specification
CC and also the polarity of different cell types including distal tip
CC cells, seam cells, AVG interneurons and P-cells and their descendants
CC (PubMed:16930586, PubMed:20126385, PubMed:22022276, PubMed:23295860,
CC PubMed:24401370, PubMed:26292279). Plays a role in the migration of
CC cell types including distal tip cells and the QR neuroblast
CC descendants, QR.p and QR.pa during larval development (PubMed:20126385,
CC PubMed:25373777, PubMed:26292279). Negatively regulates the unc-
CC 6/Netrin receptors unc-5 and unc-40 to control distal tip cell polarity
CC and migration (PubMed:26292279). Acts through ced-5/DOCK180 and ced-
CC 10/Rac to control both distal tip cell migration and the phagocytic
CC clearance of apoptotic cell corpses (PubMed:20126385). Furthermore, it
CC is also required for the migration and axon guidance of the different
CC neuronal cell types including CAN, ALM, HSN and the two mechanosensory
CC neurons AVM and PVM (PubMed:16109397, PubMed:16516839,
CC PubMed:25917219). Mediates Wnt receptor cfz-2 in directing ALM
CC migration, but may also act redundantly with the Wnt receptors cfz-2
CC and mig-1 to direct the migration of other neuronal cell types
CC including CAN and HSN (PubMed:16109397, PubMed:16516839). Mediates Wnt
CC ligand egl-20 in the control of the anterior-posterior axon guidance of
CC AVM and PVM neurons (PubMed:16516839). {ECO:0000269|PubMed:12810601,
CC ECO:0000269|PubMed:15620652, ECO:0000269|PubMed:15990090,
CC ECO:0000269|PubMed:16109397, ECO:0000269|PubMed:16516839,
CC ECO:0000269|PubMed:16930586, ECO:0000269|PubMed:20126385,
CC ECO:0000269|PubMed:22022276, ECO:0000269|PubMed:24401370,
CC ECO:0000269|PubMed:25373777, ECO:0000269|PubMed:25917219,
CC ECO:0000269|PubMed:26292279, ECO:0000269|PubMed:9288749,
CC ECO:0000269|PubMed:9288750, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15620652,
CC ECO:0000269|PubMed:24401370}; Multi-pass membrane protein
CC {ECO:0000255}. Early endosome {ECO:0000269|PubMed:15620652,
CC ECO:0000269|PubMed:24401370}. Note=Uniformaly localized along the cell
CC membrane throughout the cell cycle, but occasionally enriched at
CC prophase towards the posterior pole of the cell (PubMed:15620652).
CC Sequestered from the cell membrane to endosomes by plr-1 to prevent Wnt
CC signaling (PubMed:24401370). {ECO:0000269|PubMed:15620652,
CC ECO:0000269|PubMed:24401370}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b {ECO:0000312|WormBase:T23D8.1b};
CC IsoId=A0A0K3AWM6-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:T23D8.1a};
CC IsoId=A0A0K3AWM6-2; Sequence=VSP_058705;
CC -!- DEVELOPMENTAL STAGE: Expressed in the 32-cell stage ABar blastomere and
CC onwards into late embryogenesis (PubMed:15620652, PubMed:24401370). In
CC late embryogenesis, enriched at the leading edges of postmitotic
CC epidermal cells during ventral enclosure (PubMed:15620652).
CC Asymmetrically expressed during the larval stages of development in
CC cells of the gonad, vulva, tail, nervous system and hypodermis
CC (PubMed:15620652). Expressed predominantly in QR neuroblast descendants
CC and to a lesser extent in QL neuroblast descendants during the larval
CC stages of development (PubMed:25373777). Expressed highly in anterior
CC P-cells during larval development (PubMed:23295860). Post-
CC embryonically, it is up-regulated at the transition phase after dorsal-
CC ventral migration of distal tip cells and at the beginning of their
CC anterior-posterior migration (PubMed:26292279).
CC {ECO:0000269|PubMed:15620652, ECO:0000269|PubMed:23295860,
CC ECO:0000269|PubMed:24401370, ECO:0000269|PubMed:25373777,
CC ECO:0000269|PubMed:26292279}.
CC -!- DOMAIN: The FZ domain is involved in binding with Wnt ligands.
CC {ECO:0000250|UniProtKB:Q9VVX3}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal with severely defective
CC embryonic morphogenesis (PubMed:9288749, PubMed:9288750,
CC PubMed:15620652). Embryos have defective mitotic spindle orientation in
CC the 8-cell stage ABar blastomere (PubMed:9288749, PubMed:9288750,
CC PubMed:20126385). Furthermore, there is disrupted asymmetric
CC distribution of the transcription factor pop-1 and the disheveled
CC homolog dsh-2, which are required for cell fate decisions in 8-cell
CC stage ABar blastomeres and their descendants (PubMed:12810601,
CC PubMed:15990090). There is also abnormal distal tip cell migration
CC along the anterior-posterior axis of the body and defective clearance
CC of apoptotic cell corpses in embryos (PubMed:20126385,
CC PubMed:26292279). Both double knockout with unc-5 RNAi and knockdown by
CC RNAi in an unc-40 mutant background suppresses the migratory defect of
CC distal tip cells in the mom-5 and unc-40 single mutants
CC (PubMed:26292279). Double knockout with Wnt receptor cfz-2 results in
CC enhanced CAN neuron migration defects and also rescues the ALM
CC migration defects in the single cfz-2 knockout (PubMed:16109397).
CC Double knockout with Wnt receptor mig-1 results in enhanced HSN neuron
CC migration defects and also in anterior-posterior axon guidance defects
CC of PVM and AVM touch neurons (PubMed:16516839). RNAi-mediated knockdown
CC results in embryonic lethality, but surviving animals display
CC morphogenesis defects and PHA phasmid neuron duplication
CC (PubMed:15990090). {ECO:0000269|PubMed:12810601,
CC ECO:0000269|PubMed:15620652, ECO:0000269|PubMed:15990090,
CC ECO:0000269|PubMed:16109397, ECO:0000269|PubMed:16516839,
CC ECO:0000269|PubMed:20126385, ECO:0000269|PubMed:26292279,
CC ECO:0000269|PubMed:9288749, ECO:0000269|PubMed:9288750}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
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DR EMBL; AF013953; AAC47750.1; -; mRNA.
DR EMBL; BX284601; CAB03398.1; -; Genomic_DNA.
DR EMBL; BX284601; CTQ86376.1; -; Genomic_DNA.
DR PIR; T25162; T25162.
DR RefSeq; NP_001300437.1; NM_001313508.1. [A0A0K3AWM6-1]
DR RefSeq; NP_492635.1; NM_060234.4. [A0A0K3AWM6-2]
DR AlphaFoldDB; A0A0K3AWM6; -.
DR SMR; A0A0K3AWM6; -.
DR STRING; 6239.T23D8.1; -.
DR EnsemblMetazoa; T23D8.1a.1; T23D8.1a.1; WBGene00003397. [A0A0K3AWM6-2]
DR EnsemblMetazoa; T23D8.1b.1; T23D8.1b.1; WBGene00003397. [A0A0K3AWM6-1]
DR GeneID; 172856; -.
DR KEGG; cel:CELE_T23D8.1; -.
DR CTD; 172856; -.
DR WormBase; T23D8.1a; CE14048; WBGene00003397; mom-5. [A0A0K3AWM6-2]
DR WormBase; T23D8.1b; CE50472; WBGene00003397; mom-5. [A0A0K3AWM6-1]
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000166686; -.
DR OMA; IVIACCF; -.
DR OrthoDB; 330751at2759; -.
DR Reactome; R-CEL-4086398; Ca2+ pathway.
DR Reactome; R-CEL-4086400; PCP/CE pathway.
DR Reactome; R-CEL-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-CEL-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-CEL-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR SignaLink; A0A0K3AWM6; -.
DR PRO; PR:A0A0K3AWM6; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003397; Expressed in germ line (C elegans) and 13 other tissues.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:WormBase.
DR GO; GO:0042813; F:Wnt receptor activity; ISS:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:UniProtKB.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:UniProtKB.
DR GO; GO:0001714; P:endodermal cell fate specification; IMP:WormBase.
DR GO; GO:0043652; P:engulfment of apoptotic cell; IMP:WormBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR GO; GO:0007369; P:gastrulation; IMP:WormBase.
DR GO; GO:1904936; P:interneuron migration; IGI:UniProtKB.
DR GO; GO:0070986; P:left/right axis specification; IMP:UniProtKB.
DR GO; GO:0097475; P:motor neuron migration; IGI:UniProtKB.
DR GO; GO:0097402; P:neuroblast migration; IMP:UniProtKB.
DR GO; GO:0001764; P:neuron migration; IGI:UniProtKB.
DR GO; GO:1905488; P:positive regulation of anterior/posterior axon guidance; IGI:UniProtKB.
DR GO; GO:1903356; P:positive regulation of distal tip cell migration; IMP:UniProtKB.
DR GO; GO:1901076; P:positive regulation of engulfment of apoptotic cell; IDA:UniProtKB.
DR GO; GO:1905485; P:positive regulation of motor neuron migration; IGI:UniProtKB.
DR GO; GO:1905491; P:positive regulation of sensory neuron axon guidance; IGI:UniProtKB.
DR GO; GO:1904937; P:sensory neuron migration; IGI:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; ISS:WormBase.
DR GO; GO:0060069; P:Wnt signaling pathway, regulating spindle positioning; IMP:WormBase.
DR Gene3D; 1.10.2000.10; -; 1.
DR InterPro; IPR015526; Frizzled/SFRP.
DR InterPro; IPR000539; Frizzled/Smoothened_TM.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR017981; GPCR_2-like.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR Pfam; PF01534; Frizzled; 1.
DR Pfam; PF01392; Fz; 1.
DR PRINTS; PR00489; FRIZZLED.
DR SMART; SM00063; FRI; 1.
DR SMART; SM01330; Frizzled; 1.
DR SUPFAM; SSF63501; SSF63501; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Developmental protein; Disulfide bond;
KW Endosome; Glycoprotein; Membrane; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Wnt signaling pathway.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..570
FT /note="Protein mom-5"
FT /evidence="ECO:0000305"
FT /id="PRO_5005493958"
FT TOPO_DOM 17..230
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 231..251
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 265..285
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 286..319
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 320..340
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 349..369
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..395
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 396..416
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 450..470
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..515
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 516..536
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..570
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 32..148
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 37..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 45..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 82..119
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 108..145
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 112..136
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT VAR_SEQ 158..160
FT /note="NYR -> K (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_058705"
FT MUTAGEN 343
FT /note="K->R: Abolishes sequestration in endosomes by plr-1;
FT when associated with R-430; R-442; R-445; R-541 and R548."
FT /evidence="ECO:0000269|PubMed:24401370"
FT MUTAGEN 430
FT /note="K->R: Abolishes sequestration in endosomes by plr-1;
FT when associated with R-343; R-442; R-445; R-541 and R548."
FT /evidence="ECO:0000269|PubMed:24401370"
FT MUTAGEN 442
FT /note="K->R: Abolishes sequestration in endosomes by plr-1;
FT when associated with R-343; R-430; R-445; R-541 and R548."
FT /evidence="ECO:0000269|PubMed:24401370"
FT MUTAGEN 445
FT /note="K->R: Abolishes sequestration in endosomes by plr-1;
FT when associated with R-343; R-430; R-442; R-541 and R548."
FT /evidence="ECO:0000269|PubMed:24401370"
FT MUTAGEN 541
FT /note="K->R: Abolishes sequestration in endosomes by plr-1;
FT when associated with R-343; R-430; R-442; R-445 and R548."
FT /evidence="ECO:0000269|PubMed:24401370"
FT MUTAGEN 548
FT /note="K->R: Abolishes sequestration in endosomes by plr-1;
FT when associated with R-343; R-430; R-442; R-445 and R541."
FT /evidence="ECO:0000269|PubMed:24401370"
SQ SEQUENCE 570 AA; 63198 MW; 930A0AF0A83F3B7D CRC64;
MHRHILILFL FGCLSADQRL SSTSISSMNG FSTTRKCEHI TIPMCKNLDY NQTVFPNLLG
HTTQSEAGPA IAQFNPLIKV KCSEDIRLFL CTVYAPVCTV LEKPIQPCRE LCLSAKNGCE
SLMKKFGFQW PDQLDCNKFP VTDLCVGKNS SESSNSKNYR SSNDVTFGVS TIANEVVLSP
KKCPHHMHTT SGSHFSLPLL SGRLPECSLT CEADNQVPMM FDGRVRRILR IWTAAWSVAC
FVCSLFTLVT FLVDLSRFAY PVRPILYLAF CYLAISTVYM IGVVGEDGFA CGTYGSTPTT
LVTQGGENVG CSALAVVHYF FFMSSCAWWL VLCLAWFLAA NLKWGAESIA ALSPYFHAMC
WGVPAVLSVT VLVTNSVDGD VFTGICSVGN LNPSALVYFF FTPIVVSLAL GAVLLVCGIW
SMIRIRSYIK LQHADVERNI SKLEKLMLRI GAFAIMYSLP TAMNAAIMWY QAVNMPAWLE
GWLHHRCVRL QDRELFGFTY PVDDCPMDPK VAAPEIIVFL LKYVSQLVVG ITCAIWVVSS
KTLSSYHKAY LALSSRSPTV PAHVDQVNMR
