PPN1_CAEEL
ID PPN1_CAEEL Reviewed; 2167 AA.
AC O76840; Q22911; Q8I7I0; Q8MPV5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Papilin;
DE AltName: Full=Abnormal cell migration protein 6;
DE Flags: Precursor;
GN Name=mig-6; Synonyms=ppn-1; ORFNames=C37C3.6;
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 [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 [2]
RP FUNCTION.
RX PubMed=11076767; DOI=10.1242/dev.127.24.5475;
RA Kramerova I.A., Kawaguchi N., Fessler L.I., Nelson R.E., Chen Y.,
RA Kramerov A.A., Kusche-Gullberg M., Kramer J.M., Ackley B.D., Sieron A.L.,
RA Prockop D.J., Fessler J.H.;
RT "Papilin in development; a pericellular protein with a homology to the
RT ADAMTS metalloproteinases.";
RL Development 127:5475-5485(2000).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-386; ASN-445; ASN-541; ASN-568;
RP ASN-638; ASN-857; ASN-933 AND ASN-1090, 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 [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-445; ASN-857 AND ASN-1090, 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 [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-268; ASN-386; ASN-445; ASN-541;
RP ASN-568; ASN-638; ASN-857; ASN-933; ASN-1090 AND ASN-1992, AND
RP 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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND ALTERNATIVE SPLICING.
RX PubMed=19297413; DOI=10.1242/dev.028472;
RA Kawano T., Zheng H., Merz D.C., Kohara Y., Tamai K.K., Nishiwaki K.,
RA Culotti J.G.;
RT "C. elegans mig-6 encodes papilin isoforms that affect distinct aspects of
RT DTC migration, and interacts genetically with mig-17 and collagen IV.";
RL Development 136:1433-1442(2009).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP TYR-650; CYS-848; 878-GLY-CYS-879; GLY-965 AND CYS-973.
RX PubMed=20805556; DOI=10.1534/genetics.110.120519;
RA Jafari G., Burghoorn J., Kawano T., Mathew M., Moerck C., Axaeng C.,
RA Ailion M., Thomas J.H., Culotti J.G., Swoboda P., Pilon M.;
RT "Genetics of extracellular matrix remodeling during organ growth using the
RT Caenorhabditis elegans pharynx model.";
RL Genetics 186:969-982(2010).
CC -!- FUNCTION: Involved in pharynx morphogenesis probably by remodeling the
CC basement membrane. {ECO:0000269|PubMed:20805556}.
CC -!- FUNCTION: [Isoform a]: Plays a role in embryogenesis, the second phase
CC of distal cell tip migration and is required for distribution of the
CC metalloproteinase, mig-17, during organogenesis.
CC {ECO:0000269|PubMed:19297413}.
CC -!- FUNCTION: [Isoform b]: Plays a role in post embryonic distal cell tip
CC migration (PubMed:19297413). Essential extracellular matrix (ECM)
CC protein required for hypodermal enclosure in the embryo
CC (PubMed:11076767). {ECO:0000269|PubMed:11076767,
CC ECO:0000269|PubMed:19297413}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:19297413}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b; Synonyms=mig-6L;
CC IsoId=O76840-1; Sequence=Displayed;
CC Name=a; Synonyms=mig-6S;
CC IsoId=O76840-2; Sequence=VSP_020308, VSP_020309;
CC Name=c;
CC IsoId=O76840-3; Sequence=VSP_020307, VSP_020308, VSP_020309;
CC -!- TISSUE SPECIFICITY: Localizes to the basement membranes of the gonad
CC primordium, pharynx and intestine (at protein level) (PubMed:19297413).
CC Expressed in head and CAN neurons, coelomocytes, body-wall muscles and
CC anal depressor and sphincter and stomatointestinal muscles
CC (PubMed:19297413, PubMed:20805556). Expressed Isoform a: is expressed
CC in body wall muscles and distal cell tips (PubMed:19297413). Isoform b:
CC expressed in embryonic muscles (PubMed:19297413).
CC {ECO:0000269|PubMed:19297413, ECO:0000269|PubMed:20805556}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected is intestinal
CC primordium at the E16 embryonic stage followed by expression in future
CC head neurons and head muscle cells at the comma and 1.5-fold stages
CC (PubMed:20805556). Expressed in larvae and adults (PubMed:19297413,
CC PubMed:20805556). {ECO:0000269|PubMed:19297413,
CC ECO:0000269|PubMed:20805556}.
CC -!- SIMILARITY: Belongs to the papilin family. {ECO:0000305}.
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DR EMBL; FO080808; CCD66947.1; -; Genomic_DNA.
DR EMBL; FO080808; CCD66945.1; -; Genomic_DNA.
DR EMBL; FO080808; CCD66946.1; -; Genomic_DNA.
DR PIR; C89114; C89114.
DR PIR; T34395; T34395.
DR RefSeq; NP_505017.1; NM_072616.4. [O76840-1]
DR RefSeq; NP_505018.1; NM_072617.4.
DR RefSeq; NP_741569.1; NM_171931.4. [O76840-3]
DR AlphaFoldDB; O76840; -.
DR SMR; O76840; -.
DR BioGRID; 44205; 32.
DR DIP; DIP-24457N; -.
DR IntAct; O76840; 12.
DR STRING; 6239.C37C3.6b.2; -.
DR MEROPS; I02.968; -.
DR MEROPS; I02.978; -.
DR iPTMnet; O76840; -.
DR EPD; O76840; -.
DR PaxDb; O76840; -.
DR PeptideAtlas; O76840; -.
DR PRIDE; O76840; -.
DR EnsemblMetazoa; C37C3.6a.1; C37C3.6a.1; WBGene00003242. [O76840-2]
DR EnsemblMetazoa; C37C3.6a.2; C37C3.6a.2; WBGene00003242. [O76840-2]
DR EnsemblMetazoa; C37C3.6b.1; C37C3.6b.1; WBGene00003242. [O76840-1]
DR EnsemblMetazoa; C37C3.6c.1; C37C3.6c.1; WBGene00003242. [O76840-3]
DR GeneID; 179162; -.
DR KEGG; cel:CELE_C37C3.6; -.
DR UCSC; C37C3.6a.2; c. elegans. [O76840-1]
DR CTD; 179162; -.
DR WormBase; C37C3.6a; CE17535; WBGene00003242; mig-6. [O76840-2]
DR WormBase; C37C3.6b; CE17536; WBGene00003242; mig-6. [O76840-1]
DR WormBase; C37C3.6c; CE30735; WBGene00003242; mig-6. [O76840-3]
DR eggNOG; KOG4597; Eukaryota.
DR GeneTree; ENSGT00940000171211; -.
DR HOGENOM; CLU_000391_0_0_1; -.
DR InParanoid; O76840; -.
DR OMA; KHGCCPD; -.
DR OrthoDB; 56186at2759; -.
DR PhylomeDB; O76840; -.
DR SignaLink; O76840; -.
DR PRO; PR:O76840; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003242; Expressed in larva and 11 other tissues.
DR GO; GO:0005604; C:basement membrane; IDA:WormBase.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0000902; P:cell morphogenesis; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0048598; P:embryonic morphogenesis; IMP:WormBase.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0032504; P:multicellular organism reproduction; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR CDD; cd00109; KU; 11.
DR Gene3D; 2.20.100.10; -; 5.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 4.10.410.10; -; 11.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF05986; ADAM_spacer1; 1.
DR Pfam; PF00014; Kunitz_BPTI; 11.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00131; KU; 11.
DR SMART; SM00209; TSP1; 7.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF57362; SSF57362; 11.
DR SUPFAM; SSF82895; SSF82895; 6.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 10.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 11.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Basement membrane; Developmental protein;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Immunoglobulin domain;
KW Protease inhibitor; Proteoglycan; Reference proteome; Repeat; Secreted;
KW Serine protease inhibitor; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..2167
FT /note="Papilin"
FT /id="PRO_0000248545"
FT DOMAIN 76..123
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 341..402
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 404..459
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 461..525
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 585..643
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 645..702
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1089..1141
FT /note="BPTI/Kunitz inhibitor 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 1150..1202
FT /note="BPTI/Kunitz inhibitor 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 1271..1321
FT /note="BPTI/Kunitz inhibitor 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 1375..1425
FT /note="BPTI/Kunitz inhibitor 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 1447..1497
FT /note="BPTI/Kunitz inhibitor 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 1504..1554
FT /note="BPTI/Kunitz inhibitor 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 1621..1671
FT /note="BPTI/Kunitz inhibitor 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 1731..1781
FT /note="BPTI/Kunitz inhibitor 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 1790..1840
FT /note="BPTI/Kunitz inhibitor 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 1853..1903
FT /note="BPTI/Kunitz inhibitor 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 1914..1964
FT /note="BPTI/Kunitz inhibitor 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 2124..2163
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 1239..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2075..2106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1239..1268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1556..1570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1591..1615
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2078..2106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 268
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:15888633, ECO:0000269|PubMed:17761667"
FT CARBOHYD 541
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 814
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 857
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:15888633, ECO:0000269|PubMed:17761667"
FT CARBOHYD 933
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:17761667"
FT CARBOHYD 1090
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754521,
FT ECO:0000269|PubMed:15888633, ECO:0000269|PubMed:17761667"
FT CARBOHYD 1848
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1992
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 2087
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 88..117
FT /evidence="ECO:0000250"
FT DISULFID 92..122
FT /evidence="ECO:0000250"
FT DISULFID 103..107
FT /evidence="ECO:0000250"
FT DISULFID 353..396
FT /evidence="ECO:0000250"
FT DISULFID 357..401
FT /evidence="ECO:0000250"
FT DISULFID 368..382
FT /evidence="ECO:0000250"
FT DISULFID 1089..1141
FT /evidence="ECO:0000250"
FT DISULFID 1099..1124
FT /evidence="ECO:0000250"
FT DISULFID 1116..1137
FT /evidence="ECO:0000250"
FT DISULFID 1150..1202
FT /evidence="ECO:0000250"
FT DISULFID 1161..1185
FT /evidence="ECO:0000250"
FT DISULFID 1177..1198
FT /evidence="ECO:0000250"
FT DISULFID 1271..1321
FT /evidence="ECO:0000250"
FT DISULFID 1280..1304
FT /evidence="ECO:0000250"
FT DISULFID 1296..1317
FT /evidence="ECO:0000250"
FT DISULFID 1375..1425
FT /evidence="ECO:0000250"
FT DISULFID 1384..1408
FT /evidence="ECO:0000250"
FT DISULFID 1400..1421
FT /evidence="ECO:0000250"
FT DISULFID 1447..1497
FT /evidence="ECO:0000250"
FT DISULFID 1456..1480
FT /evidence="ECO:0000250"
FT DISULFID 1472..1493
FT /evidence="ECO:0000250"
FT DISULFID 1504..1554
FT /evidence="ECO:0000250"
FT DISULFID 1513..1537
FT /evidence="ECO:0000250"
FT DISULFID 1529..1550
FT /evidence="ECO:0000250"
FT DISULFID 1621..1671
FT /evidence="ECO:0000250"
FT DISULFID 1630..1654
FT /evidence="ECO:0000250"
FT DISULFID 1646..1667
FT /evidence="ECO:0000250"
FT DISULFID 1731..1781
FT /evidence="ECO:0000250"
FT DISULFID 1740..1764
FT /evidence="ECO:0000250"
FT DISULFID 1756..1777
FT /evidence="ECO:0000250"
FT DISULFID 1790..1840
FT /evidence="ECO:0000250"
FT DISULFID 1799..1823
FT /evidence="ECO:0000250"
FT DISULFID 1815..1836
FT /evidence="ECO:0000250"
FT DISULFID 1853..1903
FT /evidence="ECO:0000250"
FT DISULFID 1862..1886
FT /evidence="ECO:0000250"
FT DISULFID 1878..1899
FT /evidence="ECO:0000250"
FT DISULFID 1914..1964
FT /evidence="ECO:0000250"
FT DISULFID 1923..1947
FT /evidence="ECO:0000250"
FT DISULFID 1939..1960
FT /evidence="ECO:0000250"
FT VAR_SEQ 1367..1438
FT /note="SNSKQRDACHLNVDQGRCKGAFDSWYYEVATGSCVTFKYTGCGGNANRFASK
FT DQCESLCVKPASEAASAGID -> Y (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_020307"
FT VAR_SEQ 1556..1558
FT /note="KDD -> SKF (in isoform a and isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_020308"
FT VAR_SEQ 1559..2167
FT /note="Missing (in isoform a and isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_020309"
FT MUTAGEN 650
FT /note="Y->D: In k177; no pharyngeal defects."
FT /evidence="ECO:0000269|PubMed:20805556"
FT MUTAGEN 848
FT /note="C->Y: In ev701; no pharyngeal defects."
FT /evidence="ECO:0000269|PubMed:20805556"
FT MUTAGEN 878..879
FT /note="GC->EY: In ev700; no pharyngeal defects."
FT /evidence="ECO:0000269|PubMed:20805556"
FT MUTAGEN 965
FT /note="G->E: In sa580; pharynx is twisted without affecting
FT feeding or pumping rate. Causes some twisting in amphid
FT neurons close to the pharynx."
FT /evidence="ECO:0000269|PubMed:20805556"
FT MUTAGEN 973
FT /note="C->Y: In et4; pharynx is twisted without affecting
FT feeding or pumping rate. Causes some twisting in amphid
FT neurons close to the pharynx. NO defect in mig-17
FT localization."
FT /evidence="ECO:0000269|PubMed:20805556"
SQ SEQUENCE 2167 AA; 237601 MW; 96274786D52E3639 CRC64;
MRLLLFSAAL LLCSVPTWAF SLSSFFGSDV AQKPYLHPNS PPERDPASSR MKRQAYQVYV
DGDVSVTVDK SGQKETGNWG PWVPENECSR SCGGGVQLEK RQCSGDCTGA SVRYISCNLN
ACESGTDFRA EQCSKFNDEA LDGNYHKWTP YKGKNKCELV CKPESGNFYY KWADKVVDGT
KCDSKSNDIC VDGECLPVGC DGKLGSSLKF DKCGKCDGDG STCKTIEGRF DERNLSPGYH
DIIKLPEGAT NIKIQEARKS TNNLALKNGS DHFYLNGNGL IQVEKEVEVG GTIFVYDDAE
PETLSAQGPL SEELTVALLF RKGSRDTAIK YEFSIPLEEE VDYMYKFDNW TPCSVSCGKG
VQTRNLYCID GKNKGRVEDD LCEENNATKP EFEKSCETVD CEAEWFTGDW ESCSSTCGDQ
GQQYRVVYCH QVFANGRRVT VEDGNCTVER PPVKQTCNRF ACPEWQAGPW SACSEKCGDA
FQYRSVTCRS EKEGEEGKLL AADACPADEQ EKFDTERTCN LGPCEGLTFV TGEWNLCTRC
NDTEETREVT CKDSQGRAYP LEKCLVDNST EIPTDTRSCA TQPPCEYEWT VSEWSKCTTE
CGHGHKTRRV ICAIHQNGGL EVVDEGHCQA EKPEGKTNCT NEEKCTGTWY TSSWSECTAE
CGGGSQDRVA VCLNYDKKPV PEWCDEAVKP SEKQDCNVDD CPTCVDSEFG CCPDNSTFAT
GEFNFGCSNC SETEFGCCAD NVTVATGPNS KGCEEFVESP LNLEADVANA DAEASGDAPE
LCSVTNENGE AVDVECATIA PITALLGDGE LIGNDTDASN ETIHCSKTEF GCCPDWYTAA
SGKGNEGCPS FTLGGCNETQ FGCCHDDVTL ARGANLEGCG EPSCAASLYG CCKDRKTIAF
GPHYSGCERS SFPCELSDFG CCPDGETAAL GKNGTGCGEN CLTTKFGCCP DGKTTAKGSH
NEGCGCEFAQ YGCCPDGKSV AKGAGFYGCP ESCAQSQFGC CPDGKTRARG ENKEGCPCQY
TRYGCCPDGE TTALGPRNDG CDNCRYAKHG CCPDGETKAL GPDGAGCPPT TTPPFLMGGT
VAPHKIAACN QTQESGTVCG AGYKLAWHYD TTEGRCNQFW YGGCGGNDNN FASQDMCETI
CVEPPGKGRC YLPRVDGPLR CDQLQPRYYY DHSKKHCVAF WWRGCLGNAN NFNSFEECSM
FCKDVGPYDA PTTAAPPPPP QQNAQQYLPT PEVQQIEIQS AEQPQPQQPQ QQQQQQQQQP
QQPRQSMEDI CRSRQDAGPC ETYSDQWFYN AFSQECETFT YGGCGGNLNR FRSKDECEQR
CFFVHGAQPS AARQEQAQPA AQPAQPAQPS NIVSPPQQSA SPVVVPSNSK QRDACHLNVD
QGRCKGAFDS WYYEVATGSC VTFKYTGCGG NANRFASKDQ CESLCVKPAS EAASAGIDGA
AGINSVCDEA KDTGPCTNFV TKWYYNKADG TCNRFHYGGC QGTNNRFDNE QQCKAACQNH
KDACQLPKVQ GPCSGKHSYY YYNTASHQCE TFTYGGCLGN TNRFATIEEC QARCPKDDQT
TTTSQPEELP SLPLVQEDPQ PRPAFSLKQS FAHSRRRDAP FARSVSARHH TPDSEEERVD
CYAVPDPGSC GDYRLVWHYS ATSNSCRQFY YGGCAGNTNR FETRDKCETS CVAKIEERVE
SVSEASKSLE EVRLTDPRMD SHFGYHDPEV DQIEEEAEYV IVDTGALPEL CMLPEQRGSC
YDNILRWRFD SEKSQCVTFM YSGCNPNANH FTSQETCERA CGKWRNVAVC ELPAEHGDCQ
LAIPRWYHDP KTSQCQMMMW TGCGGNGNAF SSKADCESLC RVETLWSNNT DFCTLERSAG
PCTDSISMWY FDSTHLDCKP FTYGGCRGNQ NRFVSKEQCQ QSCRPGDTKS EDICTLRPEP
GPCRLGLEKY FYDPVIQSCH MFHYGGCEGN ANRFDSELDC FRRCSSVKVE ASESERVGQL
TSASTPVIYI VNKTAIFVGN TFRIRCNSYG VLPITWYKNG GLLQFGSRIT EENDDTLEIV
DALTADAGVY TCIAGQDSTM SEGVEVVIKR LPGHRTTSRP MLTPSKNFSL GTPPTPSPST
VSTTPFRIYT PGSAPSDARV SRPTSNSCMD VGNASTCDLI VKNGLCGKKR YGTFCCHTCT
RVHNFKF
