LAR_CAEEL
ID LAR_CAEEL Reviewed; 2200 AA.
AC Q9BMN8; Q09434; Q17859; Q20137; Q9BMN7;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Tyrosine-protein phosphatase Lar-like;
DE EC=3.1.3.48;
DE AltName: Full=Protein-tyrosine phosphate 3;
DE Flags: Precursor;
GN Name=ptp-3; ORFNames=C09D8.1/C09D8.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|EMBL:AAK01632.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, AND ALTERNATIVE
RP SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=11959824; DOI=10.1242/dev.129.9.2141;
RA Harrington R.J., Gutch M.J., Hengartner M.O., Tonks N.K., Chisholm A.D.;
RT "The C. elegans LAR-like receptor tyrosine phosphatase PTP-3 and the VAB-1
RT Eph receptor tyrosine kinase have partly redundant functions in
RT morphogenesis.";
RL Development 129:2141-2153(2002).
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 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-574 AND ASN-1212, 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).
CC -!- FUNCTION: Has a role in early neural and epidermal development;
CC neuroblast movements during closure of the gastrulation cleft and
CC epidermal morphogenesis. Vab-1 and ptp-3 may function redundantly
CC within the same sets of neuronal precursors.
CC {ECO:0000269|PubMed:11959824}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000250|UniProtKB:P16621, ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell membrane;
CC Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000269|PubMed:11959824}; Synonyms=ptp-3a;
CC IsoId=Q9BMN8-1; Sequence=Displayed;
CC Name=b {ECO:0000269|PubMed:11959824}; Synonyms=ptp-3b;
CC IsoId=Q9BMN8-2; Sequence=VSP_007007, VSP_007008;
CC -!- TISSUE SPECIFICITY: Both isoforms are ubiquitously expressed in early
CC embryos. In later embryos, larvae and adults expression is highest in
CC the nerve ring, dorsal cord, ventral cord and epithelial tissues.
CC {ECO:0000269|PubMed:11959824}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily. {ECO:0000305}.
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DR EMBL; AF316539; AAK01632.1; -; mRNA.
DR EMBL; AF316540; AAK01633.1; -; mRNA.
DR EMBL; Z46811; CAA86842.3; ALT_SEQ; Genomic_DNA.
DR EMBL; Z49938; CAA86842.3; JOINED; Genomic_DNA.
DR EMBL; Z49938; CAA90189.3; ALT_SEQ; Genomic_DNA.
DR EMBL; Z46811; CAA90189.3; JOINED; Genomic_DNA.
DR EMBL; Z49938; CAD31752.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z46811; CAD31752.1; JOINED; Genomic_DNA.
DR EMBL; Z46811; CAD31753.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z49938; CAD31753.1; JOINED; Genomic_DNA.
DR PIR; T19121; T19121.
DR RefSeq; NP_001021942.1; NM_001026771.2.
DR RefSeq; NP_001021943.1; NM_001026772.3.
DR RefSeq; NP_001293468.1; NM_001306539.1.
DR RefSeq; NP_001293469.1; NM_001306540.1.
DR AlphaFoldDB; Q9BMN8; -.
DR SMR; Q9BMN8; -.
DR BioGRID; 39995; 9.
DR STRING; 6239.C09D8.1j; -.
DR iPTMnet; Q9BMN8; -.
DR EPD; Q9BMN8; -.
DR PaxDb; Q9BMN8; -.
DR PeptideAtlas; Q9BMN8; -.
DR PRIDE; Q9BMN8; -.
DR EnsemblMetazoa; C09D8.1a.1; C09D8.1a.1; WBGene00004215.
DR EnsemblMetazoa; C09D8.1b.1; C09D8.1b.1; WBGene00004215.
DR GeneID; 174685; -.
DR UCSC; C09D8.1d; c. elegans. [Q9BMN8-1]
DR CTD; 174685; -.
DR WormBase; C09D8.1a; CE30244; WBGene00004215; ptp-3.
DR WormBase; C09D8.1b; CE30245; WBGene00004215; ptp-3.
DR eggNOG; KOG4228; Eukaryota.
DR InParanoid; Q9BMN8; -.
DR PhylomeDB; Q9BMN8; -.
DR Reactome; R-CEL-388844; Receptor-type tyrosine-protein phosphatases.
DR PRO; PR:Q9BMN8; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004215; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR ExpressionAtlas; Q9BMN8; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:WormBase.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:WormBase.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; ISS:WormBase.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:UniProtKB.
DR GO; GO:0008544; P:epidermis development; IMP:WormBase.
DR GO; GO:0007369; P:gastrulation; IMP:WormBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:WormBase.
DR GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR GO; GO:0097402; P:neuroblast migration; IMP:WormBase.
DR GO; GO:0001764; P:neuron migration; IMP:WormBase.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0035418; P:protein localization to synapse; IMP:WormBase.
DR GO; GO:0007416; P:synapse assembly; IMP:WormBase.
DR CDD; cd00063; FN3; 8.
DR Gene3D; 2.60.40.10; -; 11.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00041; fn3; 6.
DR Pfam; PF07679; I-set; 2.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 9.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF49265; SSF49265; 6.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS50853; FN3; 9.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Disulfide bond;
KW Glycoprotein; Hydrolase; Immunoglobulin domain; Membrane;
KW Protein phosphatase; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..2200
FT /note="Tyrosine-protein phosphatase Lar-like"
FT /id="PRO_0000025430"
FT TOPO_DOM 43..1497
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1498..1518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1519..2200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 47..139
FT /note="Ig-like C2-type 1"
FT DOMAIN 151..240
FT /note="Ig-like C2-type 2"
FT DOMAIN 250..334
FT /note="Ig-like C2-type 3"
FT DOMAIN 341..434
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 439..535
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 539..628
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 633..748
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 752..856
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 857..956
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 957..1053
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1058..1158
FT /note="Fibronectin type-III 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1181..1287
FT /note="Fibronectin type-III 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1647..1902
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1933..2192
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1355..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1843
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 2133
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1811
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1843..1849
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1887
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 574
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 945
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 988
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1069
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CARBOHYD 1330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 69..122
FT /evidence="ECO:0000250|UniProtKB:P16621,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 172..225
FT /evidence="ECO:0000250|UniProtKB:P16621,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 272..318
FT /evidence="ECO:0000250|UniProtKB:P16621,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..713
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:11959824"
FT /id="VSP_007007"
FT VAR_SEQ 714..748
FT /note="SDLLPYSSYEITVAASTMDGYGPESSIRVVKTLED -> MGTPATTIAAINN
FT NFRKFFILFLLLLAPTCRGQQK (in isoform b)"
FT /evidence="ECO:0000303|PubMed:11959824"
FT /id="VSP_007008"
SQ SEQUENCE 2200 AA; 246620 MW; 43A5D8133EC07E37 CRC64;
MIQFRNKNNS MNRIARHLRN VARRKGSSLL LFLMLSTVLV AAKEDDPARL VVRPDSSTVV
DESKISFFCR ADGNPLPSVI WRVNGKSITD HNRISIKSLA TGLSTLRFER VSLDDNATVV
SCSADNGVAN PVVAEASLTV VPRDKVPIGF PQIELHPSLK SVEQGKTAYV SCRVRGDPRA
KVLWLRDLIP LDIRADGRYS VSTIGNPGAL MIQHAREEDQ GKYECIARNT LGVAHSKAAN
LYVKVRRVPP YFSYKLERQY VVGVGGNINL TCVAVGYPMP RVFWKKTDLM VLDDPSTAPI
GKNVLTLTHV ESTENFTCVA VSALGNIEAT TTVIAKELPP PPVNIVVSSV TSESVVITWK
PPKYNEAINK YVVNYRLKYS EGRSSRGKTM ETLENSLVID GLVAFQTYEF TVRSAGPVGV
GLESLPVEAQ TKPSKPATAP VSPQARSLNR DSILVKWGPC EQPNGLITGY KVYYTNDLVT
TPIREWKQHD AKSDEFMTTI NGLEPDSRYF VRVIAQNSEG DSPLSTLVTV ATRQGIPGQP
PMLTVKALDS RRMQLTWDKP LYSSPVVGYT VRYNTSDGEK ELTLTSPHEK HVVTGLHPDK
YYYFRVAAYS DRGQGEFTEP MISKTIASIP LSSPTIVSAA ATSSKSVEIR WKGPEQKKLN
GVLTAYRINY FRLEDSKTAN LESVEYDEDM DDSSSFLDRM SVVVPSDATS YVLSDLLPYS
SYEITVAAST MDGYGPESSI RVVKTLEDVP SAPRNFNAEL TSATSVKLTW DAPAAANGAL
LGYYVYLDRM VNGEPVVEKG SKKRIVMIRD SSKRYFELDS LDPNTEYSFR LNAFNRNGDG
EFSERKSIIT QGIPPEAPEI VSVSLDRDEP PVVARIEWKM PKMKPNETPI EKYNLWLRAQ
GYPDSYVKAK TVDGTDLSTT ISGLWMGVVY DVLLAAENRE GRSQNATETI ATPVGSPDGE
PIDVQYEVMK GKIVVSWRPP SEEKRNGNIT SYKAILSAMD ATADRYEQPV PAPSTSSTFE
VNVRRAYLFK VAAATMKGIG PYSPVLTINP DPAALVGPPT NVRVEATSNS TAVVQWDFES
QKADSFVVKY MHEPGNRMDT EKWKQLPVVS IDKENPKRFA VVSDLNAHKP YAFCVLAVKN
NLTLNEQFNK VRVTNYMTNF QRQGPCSDPP TVLESVTPTY MVQNLRVLWK TSNSVQLTWE
YNGPRNVGFY VNHTGRKDYV NHELQEKTMS TPGFGQDVDE KHREYLWTNL RPHMMYTIHV
GVRTLPPGAR KYWPQEVVTI TDPTGPPFVD VPKLVDSSGT QPGQQMIRLT PATEEYGPIS
HYWIILVPAN YSTEDVVNLD PIELEKATAE KRAQLARSLS VSPSKKLKRK ASEVGDDSQS
ASYHPKEKRA RRATVPGAYV TARLSADRVK QQYRNNQPFI VGDSQLYDGF TNYPLEHNLH
YRLMMRAFAK NDVRTKDSFE QRAPMSEKLS RMYSDSVLTE PFTIKSALRG ASQKSSPWVG
ACIAFLVLFS IVGMLICWWL RCNKKSAGRH PRHGSITKVA LTGNIMNGGG GIPGETSKLL
STSNEYGRQI MNPYEQMNGN HHMESSMDLY PLPTSHSRSN GYAPVPVAIP SLPNNGNNMT
TVSHPAVPIA ELANHIERLR MNNNAGFQSE FESIETGQHF TWEHSSADMN KHKNRYANVA
AYDHSRVVLS NVEGYPGMDY INANYVDGYD KPRSYIATQG PLPETFSDFW RMVWEEQSVT
IVMLTNLEER SRVKCDQYWP SRGTATYGDI EVTLLESVHL AHYTMRTMRL KMVGEPEVRE
IKHLQYTAWP DHGVPDHPTP FLIFLKRVKT LNPNDAGPII SHCSAGIGRT GAFIVIDCML
ERLRYDNTVD IYGCVTALRA QRSYMVQTEE QYIFIHDAVL DAVNSGSTEV PASRLHQHLH
ILSQPSADQL SGIDMEFRHL TTLKWTSNRC TVANLPVNRP KNRMLSAVPY DSNRVIMRLL
PGADGSDYIN ASWIDGYKER GAYIATQAPT NETAADFWRA IWEHNSPIIA MLVRTNERGQ
EQCSDYWPLE TGVQVGMLVV EPMAEYDMKH YHLREFRISD INTREVRTVR QFHFMEWPDV
GKPHTADHFL DFVTQVHNTY AQFGCTGPIT VHCCSGAGRT AVFIALSIIL DRMRAEHVVD
VFTTVKLLRT ERQNMIQEPE QYHFLYLAAY EYLAAYDNFS
