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 01-MAY-2013, entry version 101.
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 Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), FUNCTION, AND
RP ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=11959824;
RA Harrington R.J., Gutch M.J., Hengartner M.O., Tonks N.K.,
RA Chisholm A.D.;
RT "The C. elegans LAR-like receptor tyrosine phosphatase PTP-3 and the
RT VAB-1 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
RT investigating biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-574 AND ASN-1212, AND MASS
RP 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 -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
CC tyrosine + phosphate.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction. Cell
CC membrane; Single-pass type I membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a; Synonyms=ptp-3a;
CC IsoId=Q9BMN8-1; Sequence=Displayed;
CC Name=b; Synonyms=ptp-3b;
CC IsoId=Q9BMN8-2; Sequence=VSP_007007, VSP_007008;
CC -!- TISSUE SPECIFICITY: Both isoforms are ubiquitously expressed in
CC early embryos. In later embryos, larvae and adults expression is
CC highest in the nerve ring, dorsal cord, ventral cord and
CC epithelial tissues.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2A subfamily.
CC -!- SIMILARITY: Contains 9 fibronectin type-III domains.
CC -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC domains.
CC -!- SIMILARITY: Contains 2 tyrosine-protein phosphatase domains.
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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 UniGene; Cel.5177; -.
DR ProteinModelPortal; Q9BMN8; -.
DR SMR; Q9BMN8; 45-1043, 1623-2196.
DR MINT; MINT-1041938; -.
DR PaxDb; Q9BMN8; -.
DR PRIDE; Q9BMN8; -.
DR GeneID; 174685; -.
DR KEGG; cel:CELE_C09D8.1; -.
DR UCSC; C09D8.1d; c. elegans.
DR CTD; 174685; -.
DR WormBase; C09D8.1a; CE30244; WBGene00004215; ptp-3.
DR WormBase; C09D8.1b; CE30245; WBGene00004215; ptp-3.
DR eggNOG; COG5599; -.
DR HOGENOM; HOG000010250; -.
DR KO; K05695; -.
DR NextBio; 885058; -.
DR ArrayExpress; Q9BMN8; -.
DR GO; GO:0005912; C:adherens junction; IMP:UniProtKB.
DR GO; GO:0016021; C:integral to 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: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:0035418; P:protein localization to synapse; IMP:WormBase.
DR GO; GO:0007416; P:synapse assembly; IMP:WormBase.
DR Gene3D; 2.60.40.10; -; 11.
DR InterPro; IPR003961; Fibronectin_type3.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR000387; Tyr/Dual-sp_Pase.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt.
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; 2.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00194; PTPc; 2.
DR SUPFAM; SSF49265; FN_III-like; 9.
DR PROSITE; PS50853; FN3; 9.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00290; IG_MHC; FALSE_NEG.
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; Complete proteome;
KW Disulfide bond; Glycoprotein; Hydrolase; Immunoglobulin domain;
KW Membrane; Protein phosphatase; Receptor; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1 42 Potential.
FT CHAIN 43 2200 Tyrosine-protein phosphatase Lar-like.
FT /FTId=PRO_0000025430.
FT TOPO_DOM 43 1497 Extracellular (Potential).
FT TRANSMEM 1498 1518 Helical; (Potential).
FT TOPO_DOM 1519 2200 Cytoplasmic (Potential).
FT DOMAIN 47 139 Ig-like C2-type 1.
FT DOMAIN 151 240 Ig-like C2-type 2.
FT DOMAIN 250 334 Ig-like C2-type 3.
FT DOMAIN 339 431 Fibronectin type-III 1.
FT DOMAIN 436 532 Fibronectin type-III 2.
FT DOMAIN 537 625 Fibronectin type-III 3.
FT DOMAIN 630 745 Fibronectin type-III 4.
FT DOMAIN 750 850 Fibronectin type-III 5.
FT DOMAIN 854 952 Fibronectin type-III 6.
FT DOMAIN 957 1051 Fibronectin type-III 7.
FT DOMAIN 1055 1153 Fibronectin type-III 8.
FT DOMAIN 1178 1281 Fibronectin type-III 9.
FT DOMAIN 1647 1902 Tyrosine-protein phosphatase 1.
FT DOMAIN 1933 2192 Tyrosine-protein phosphatase 2.
FT REGION 1843 1849 Substrate binding (By similarity).
FT ACT_SITE 1843 1843 Phosphocysteine intermediate (By
FT similarity).
FT ACT_SITE 2133 2133 Phosphocysteine intermediate (By
FT similarity).
FT BINDING 1811 1811 Substrate (By similarity).
FT BINDING 1887 1887 Substrate (By similarity).
FT CARBOHYD 8 8 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 116 116 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 269 269 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 315 315 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 574 574 N-linked (GlcNAc...).
FT CARBOHYD 945 945 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 988 988 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1069 1069 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1141 1141 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 1212 1212 N-linked (GlcNAc...).
FT CARBOHYD 1330 1330 N-linked (GlcNAc...) (Potential).
FT DISULFID 69 122 Potential.
FT DISULFID 172 225 Potential.
FT DISULFID 272 318 Potential.
FT VAR_SEQ 1 713 Missing (in isoform b).
FT /FTId=VSP_007007.
FT VAR_SEQ 714 748 SDLLPYSSYEITVAASTMDGYGPESSIRVVKTLED -> MG
FT TPATTIAAINNNFRKFFILFLLLLAPTCRGQQK (in
FT isoform b).
FT /FTId=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
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