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Database: UniProt
Entry: Q9BMN8
LinkDB: Q9BMN8
Original site: Q9BMN8 
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   26-NOV-2014, entry version 112.
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 {ECO:0000312|EMBL:AAK01632.1};
RN   [1] {ECO:0000305}
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
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: Protein tyrosine phosphate + H(2)O = protein
CC       tyrosine + phosphate. {ECO:0000250|UniProtKB:P16621,
CC       ECO:0000255|PROSITE-ProRule:PRU10044}.
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 {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
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. {ECO:0000269|PubMed:11959824}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2A subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 9 fibronectin type-III domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00316}.
CC   -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC       domains. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 2 tyrosine-protein phosphatase domains.
CC       {ECO:0000255|PROSITE-ProRule:PRU00160}.
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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   BioGrid; 39995; 3.
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. [Q9BMN8-1]
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   InParanoid; Q9BMN8; -.
DR   KO; K05695; -.
DR   PhylomeDB; Q9BMN8; -.
DR   Reactome; REACT_255531; ECM proteoglycans.
DR   NextBio; 885058; -.
DR   PRO; PR:Q9BMN8; -.
DR   ExpressionAtlas; Q9BMN8; baseline.
DR   GO; GO:0005912; C:adherens junction; IMP:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045202; C:synapse; IDA:WormBase.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
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:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:GOC.
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   Gene3D; 2.60.40.10; -; 11.
DR   Gene3D; 3.90.190.10; -; 2.
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; IPR029021; Prot-tyrosine_phosphatase-like.
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; SSF49265; 7.
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; 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       {ECO:0000255}.
FT   CHAIN        43   2200       Tyrosine-protein phosphatase Lar-like.
FT                                /FTId=PRO_0000025430.
FT   TOPO_DOM     43   1497       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1498   1518       Helical. {ECO:0000255}.
FT   TOPO_DOM   1519   2200       Cytoplasmic. {ECO:0000255}.
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      341    434       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      439    535       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      539    628       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      633    748       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      752    856       Fibronectin type-III 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      857    956       Fibronectin type-III 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN      957   1053       Fibronectin type-III 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1058   1158       Fibronectin type-III 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1181   1287       Fibronectin type-III 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1647   1902       Tyrosine-protein phosphatase 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00160}.
FT   DOMAIN     1933   2192       Tyrosine-protein phosphatase 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00160}.
FT   REGION     1843   1849       Substrate binding. {ECO:0000250}.
FT   ACT_SITE   1843   1843       Phosphocysteine intermediate.
FT                                {ECO:0000250}.
FT   ACT_SITE   2133   2133       Phosphocysteine intermediate.
FT                                {ECO:0000250}.
FT   BINDING    1811   1811       Substrate. {ECO:0000250}.
FT   BINDING    1887   1887       Substrate. {ECO:0000250}.
FT   CARBOHYD      8      8       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    116    116       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    269    269       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    315    315       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    574    574       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:17761667}.
FT   CARBOHYD    945    945       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    988    988       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1069   1069       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1141   1141       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1212   1212       N-linked (GlcNAc...).
FT                                {ECO:0000269|PubMed:17761667}.
FT   CARBOHYD   1330   1330       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     69    122       {ECO:0000250|UniProtKB:P16621,
FT                                ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    172    225       {ECO:0000250|UniProtKB:P16621,
FT                                ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    272    318       {ECO:0000250|UniProtKB:P16621,
FT                                ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   VAR_SEQ       1    713       Missing (in isoform b).
FT                                {ECO:0000303|PubMed:11959824}.
FT                                /FTId=VSP_007007.
FT   VAR_SEQ     714    748       SDLLPYSSYEITVAASTMDGYGPESSIRVVKTLED -> MG
FT                                TPATTIAAINNNFRKFFILFLLLLAPTCRGQQK (in
FT                                isoform b).
FT                                {ECO:0000303|PubMed:11959824}.
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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