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Receptor-type tyrosine-protein phosphatase F (EC 3.1.3.48) (Leukocyte common antigen related) (LAR)

 PTPRF_MOUSE             Reviewed;        1898 AA.
A2A8L5; Q6PG86; Q9EQ17;
14-APR-2009, integrated into UniProtKB/Swiss-Prot.
20-FEB-2007, sequence version 1.
18-JUL-2018, entry version 110.
RecName: Full=Receptor-type tyrosine-protein phosphatase F;
EC=3.1.3.48;
AltName: Full=Leukocyte common antigen related;
Short=LAR;
Flags: Precursor;
Name=Ptprf; Synonyms=Lar;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Thymus;
PubMed=11241288;
DOI=10.1002/1521-4141(200103)31:3<832::AID-IMMU832>3.0.CO;2-D;
Terszowski G., Jankowski A., Hendriks W.J.A.J., Rolink A.G.,
Kisielow P.;
"Within the hemopoietic system, LAR phosphatase is a T cell lineage-
specific adhesion receptor-like protein whose phosphatase activity
appears dispensable for T cell development, repertoire selection and
function.";
Eur. J. Immunol. 31:832-840(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 370-1898.
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-721; ASN-936; ASN-941 AND
ASN-960.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Liver, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-226, HEPARIN-BINDING
REGION, AND DISULFIDE BONDS.
PubMed=21402080; DOI=10.1016/j.jmb.2011.03.013;
Biersmith B.H., Hammel M., Geisbrecht E.R., Bouyain S.;
"The immunoglobulin-like domains 1 and 2 of the protein tyrosine
phosphatase LAR adopt an unusual horseshoe-like conformation.";
J. Mol. Biol. 408:616-627(2011).
-!- FUNCTION: Possible cell adhesion receptor. It possesses an
intrinsic protein tyrosine phosphatase activity (PTPase) and
dephosphorylates EPHA2 regulating its activity (By similarity).
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- SUBUNIT: Interacts with GRIP1. Interacts with PPFIA1, PPFIA2 and
PPFIA3. Interacts with PTPRF. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in the cell of the T lineage but not
in cells of any other hemopoietic lineage.
{ECO:0000269|PubMed:11241288}.
-!- DOMAIN: The first PTPase domain has enzymatic activity, while the
second one seems to affect the substrate specificity of the first
one. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Receptor class 2A subfamily. {ECO:0000305}.
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EMBL; AF300943; AAG40194.1; -; mRNA.
EMBL; AL807774; CAM17264.1; -; Genomic_DNA.
EMBL; AL626764; CAM17264.1; JOINED; Genomic_DNA.
EMBL; AL626764; CAM27382.1; -; Genomic_DNA.
EMBL; AL807774; CAM27382.1; JOINED; Genomic_DNA.
EMBL; BC057166; AAH57166.1; -; mRNA.
CCDS; CCDS18546.1; -.
RefSeq; NP_035343.2; NM_011213.2.
UniGene; Mm.29855; -.
PDB; 3PXH; X-ray; 2.00 A; A=30-226.
PDBsum; 3PXH; -.
ProteinModelPortal; A2A8L5; -.
SMR; A2A8L5; -.
BioGrid; 202497; 4.
IntAct; A2A8L5; 3.
STRING; 10090.ENSMUSP00000039368; -.
iPTMnet; A2A8L5; -.
PhosphoSitePlus; A2A8L5; -.
SwissPalm; A2A8L5; -.
MaxQB; A2A8L5; -.
PaxDb; A2A8L5; -.
PeptideAtlas; A2A8L5; -.
PRIDE; A2A8L5; -.
Ensembl; ENSMUST00000049074; ENSMUSP00000039368; ENSMUSG00000033295.
GeneID; 19268; -.
KEGG; mmu:19268; -.
UCSC; uc008ujq.1; mouse.
CTD; 5792; -.
MGI; MGI:102695; Ptprf.
eggNOG; KOG4228; Eukaryota.
eggNOG; COG5599; LUCA.
GeneTree; ENSGT00760000118900; -.
HOGENOM; HOG000010250; -.
InParanoid; A2A8L5; -.
KO; K05695; -.
OMA; AWHKHNT; -.
OrthoDB; EOG091G11WG; -.
PhylomeDB; A2A8L5; -.
TreeFam; TF312900; -.
Reactome; R-MMU-388844; Receptor-type tyrosine-protein phosphatases.
Reactome; R-MMU-8849932; Synaptic adhesion-like molecules.
PRO; PR:A2A8L5; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000033295; -.
ExpressionAtlas; A2A8L5; baseline and differential.
Genevisible; A2A8L5; MM.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0060076; C:excitatory synapse; ISO:MGI.
GO; GO:0030426; C:growth cone; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0043005; C:neuron projection; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0050839; F:cell adhesion molecule binding; ISO:MGI.
GO; GO:0035373; F:chondroitin sulfate proteoglycan binding; IPI:MGI.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0005158; F:insulin receptor binding; ISO:MGI.
GO; GO:0042301; F:phosphate ion binding; ISO:MGI.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:MGI.
GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; ISO:MGI.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:MGI.
GO; GO:0031345; P:negative regulation of cell projection organization; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; ISO:MGI.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:MGI.
GO; GO:0051387; P:negative regulation of neurotrophin TRK receptor signaling pathway; ISO:MGI.
GO; GO:1900121; P:negative regulation of receptor binding; ISS:UniProtKB.
GO; GO:0007399; P:nervous system development; ISO:MGI.
GO; GO:0031102; P:neuron projection regeneration; IMP:MGI.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
GO; GO:0006470; P:protein dephosphorylation; ISO:MGI.
GO; GO:0048679; P:regulation of axon regeneration; IMP:MGI.
GO; GO:0010975; P:regulation of neuron projection development; IMP:MGI.
GO; GO:0050803; P:regulation of synapse structure or activity; ISO:MGI.
CDD; cd00063; FN3; 8.
Gene3D; 2.60.40.10; -; 11.
Gene3D; 3.90.190.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF00041; fn3; 7.
Pfam; PF07679; I-set; 3.
Pfam; PF00102; Y_phosphatase; 2.
PRINTS; PR00700; PRTYPHPHTASE.
SMART; SM00060; FN3; 8.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 3.
SMART; SM00194; PTPc; 2.
SMART; SM00404; PTPc_motif; 2.
SUPFAM; SSF48726; SSF48726; 3.
SUPFAM; SSF49265; SSF49265; 5.
SUPFAM; SSF52799; SSF52799; 2.
PROSITE; PS50853; FN3; 8.
PROSITE; PS50835; IG_LIKE; 3.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
1: Evidence at protein level;
3D-structure; Cell adhesion; Complete proteome; Disulfide bond;
Glycoprotein; Heparin-binding; Hydrolase; Immunoglobulin domain;
Membrane; Phosphoprotein; Protein phosphatase; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 1898 Receptor-type tyrosine-protein
phosphatase F.
/FTId=PRO_0000370193.
TOPO_DOM 30 1254 Extracellular. {ECO:0000255}.
TRANSMEM 1255 1275 Helical. {ECO:0000255}.
TOPO_DOM 1276 1898 Cytoplasmic. {ECO:0000255}.
DOMAIN 33 123 Ig-like C2-type 1.
DOMAIN 135 224 Ig-like C2-type 2.
DOMAIN 232 314 Ig-like C2-type 3.
DOMAIN 321 411 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 416 510 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 514 604 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 609 706 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 711 810 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 811 904 Fibronectin type-III 6.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 909 1001 Fibronectin type-III 7.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1005 1089 Fibronectin type-III 8.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1343 1598 Tyrosine-protein phosphatase 1.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
DOMAIN 1630 1889 Tyrosine-protein phosphatase 2.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 68 77 Heparin-binding.
REGION 1539 1545 Substrate binding. {ECO:0000250}.
ACT_SITE 1539 1539 Phosphocysteine intermediate.
{ECO:0000250}.
ACT_SITE 1830 1830 Phosphocysteine intermediate.
{ECO:0000250}.
BINDING 1507 1507 Substrate. {ECO:0000250}.
BINDING 1583 1583 Substrate. {ECO:0000250}.
MOD_RES 1296 1296 Phosphoserine.
{ECO:0000250|UniProtKB:P10586}.
CARBOHYD 117 117 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 250 250 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 721 721 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 936 936 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 941 941 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 957 957 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 960 960 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
DISULFID 54 107 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21402080}.
DISULFID 156 207 {ECO:0000255|PROSITE-ProRule:PRU00114,
ECO:0000269|PubMed:21402080}.
DISULFID 253 298 {ECO:0000255|PROSITE-ProRule:PRU00114}.
CONFLICT 47 47 G -> E (in Ref. 1; AAG40194).
{ECO:0000305}.
CONFLICT 482 482 I -> V (in Ref. 1; AAG40194).
{ECO:0000305}.
CONFLICT 514 515 QP -> RS (in Ref. 1; AAG40194).
{ECO:0000305}.
CONFLICT 579 579 H -> R (in Ref. 1; AAG40194).
{ECO:0000305}.
CONFLICT 1006 1006 A -> T (in Ref. 1; AAG40194).
{ECO:0000305}.
CONFLICT 1184 1184 V -> A (in Ref. 3; AAH57166).
{ECO:0000305}.
CONFLICT 1374 1374 N -> D (in Ref. 1; AAG40194).
{ECO:0000305}.
STRAND 31 37 {ECO:0000244|PDB:3PXH}.
STRAND 42 45 {ECO:0000244|PDB:3PXH}.
STRAND 50 60 {ECO:0000244|PDB:3PXH}.
STRAND 63 68 {ECO:0000244|PDB:3PXH}.
STRAND 78 83 {ECO:0000244|PDB:3PXH}.
HELIX 84 86 {ECO:0000244|PDB:3PXH}.
STRAND 88 93 {ECO:0000244|PDB:3PXH}.
HELIX 98 101 {ECO:0000244|PDB:3PXH}.
STRAND 103 110 {ECO:0000244|PDB:3PXH}.
STRAND 115 125 {ECO:0000244|PDB:3PXH}.
STRAND 136 139 {ECO:0000244|PDB:3PXH}.
STRAND 144 146 {ECO:0000244|PDB:3PXH}.
STRAND 148 150 {ECO:0000244|PDB:3PXH}.
STRAND 152 154 {ECO:0000244|PDB:3PXH}.
STRAND 157 159 {ECO:0000244|PDB:3PXH}.
STRAND 165 170 {ECO:0000244|PDB:3PXH}.
TURN 177 179 {ECO:0000244|PDB:3PXH}.
STRAND 180 186 {ECO:0000244|PDB:3PXH}.
STRAND 192 194 {ECO:0000244|PDB:3PXH}.
HELIX 199 201 {ECO:0000244|PDB:3PXH}.
STRAND 203 211 {ECO:0000244|PDB:3PXH}.
STRAND 214 217 {ECO:0000244|PDB:3PXH}.
STRAND 221 225 {ECO:0000244|PDB:3PXH}.
SEQUENCE 1898 AA; 211489 MW; 903FF6814F0BC914 CRC64;
MAPEPAPGRR MVPLVPALVM LGLMAGAHGD SKPVFVKVPE DQTGLSGGVA SFVCQATGEP
KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR DEAIYECTAT NSLGEINTSA
KLSVLEEDQL PSGFPTIDMG PQLKVVEKGR TATMLCAAGG NPDPEISWFK DFLPVDPAAS
NGRIKQLRSG ALQIESSEES DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS
QEVMPGGSVN LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV MRSANYTCVA
ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNTEPVSFY GIQYRAAGTD
GPFQEVDGVA STRYSIGGLS PFSEYAFRVL AVNSIGRGPP SEAVRARTGE QAPSSPPRRV
QARMLSASTM LVQWEPPEEP NGLVRGYRVY YTPDSRRPLS AWHKHNTDAG LLTTVGSLLP
GITYSLRVLA FTAVGDGPPS PTIQVKTQQG VPAQPADFQA NAESDTRIQL SWLLPPQERI
VKYELVYWAA EDEGQQHKVT FDPTSSYTLE DLKPDTLYHF QLAARSDLGV GVFTPTVEAR
TAQSTPSAPP QKVTCVSTGS TTVRVSWVPP PADSRNGIIT QYSVAYEAVD GEDRKRHVVD
GISREHSSWD LLGLEKWTEY RVWVRAHTDV GPGPESSPVL VRTDEDVPSG PPRKVEVEPL
NSTAVHVSWK LPVPNKQHGQ IRGYQVTYVR LENGEPRGQP IIQDVMLAEA QETTISGLTP
ETTYSITVAA YTTKGDGARS KPKVVTTTGA VPGRPTMMVS TTAMHTALLQ WHPPKELPGE
LLGYRLQYRR ADEARPNTID FGKDDQHFTV TGLHKGATYV FRLAAKNRAG PGEEFEKEIT
TPEDVPSGFP QNLRVTGLTT STTELTWDPP VLAERNGHIT NYTVVYRDIN SQLELQNVTN
DTHLTLLGLK PDTTYDIKVR AHTSKGAGPL SPSIQSRTMP VEQVFAKNFR VAAAMKTSVL
LSWEVPDSYK SAVPFKILYN GQSVEVDGHS MRKLIADLQP NTEYSFVLMN RGSSAGGLQH
LVSIRTAPDL LPQKPLPASA FIEDGRFSLS MPQVQDPSLV RWFYIVVVPI DRVGGNLLAP
RWNTPEELEL DELLEAIEQG EEKQRRRRRQ AERLKPYVAA QVDVLPDTFT LGDKKSYRGF
YNRPLSPDLS YQCFVLASLK EPMDQKRYAS SPYSDEIVVQ VTPAQQQEEP EMLWVTGPVL
AVILIILIVI AILLFKRKRT HSPSSKDEQS IGLKDSLLAH SSDPVEMRRL NYQTPGMRDH
PPIPITDLAD NIERLKANDG LKFSQEYESI DPGQQFTWEN SNSEVNKPKN RYANVIAYDH
SRVLLTSIDG VPGSDYINAN YIDGYRKQNA YIATQGPLPE TMGDFWRMVW EQRTATVVMM
TRLEEKSRVK CDQYWPVRGT ETYGLIQVTL VDTVELATYT MRTFALHKSG SSEKRELRQF
QFMAWPDHGV PEYPTPILAF LRRVKACNPL DAGPMVVHCS AGVGRTGCFI VIDAMLERMK
HEKTVDIYGH VTCMRSQRNY MVQTEDQYVF IHEALLEAAM CGHTEVLARN LYAHIQKLGQ
VPPGESVTAM ELEFKLLANS KAHTSRFVSA NLPCNKFKNR LVNIMPYELT RVCLQPIRGV
EGSDYINASF LDGYRQQKAY IATQGPLAES TEDFWRMLWE HNSTIIVMLT KLREMGREKC
HQYWPAERSA RYQYFVVDPM AEYNMPQYIL REFKVTDARD GQSRTIRQFQ FTDWPEQGVP
KTGEGFIDFI GQVHKTKEQF GQDGPITVHC SAGVGRTGVF ITLSIVLERM RYEGVVDMFQ
TVKTLRTQRP AMVQTEDQYQ LCYRAALEYL GSFDHYAT


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U0954m CLIA LCA-related phosphatase,Lrp,Mouse,Mus musculus,Protein-tyrosine phosphatase alpha,Ptpa,Ptpra,PTPTY-28,Receptor-type tyrosine-protein phosphatase alpha,R-PTP-alpha 96T
E0954m ELISA LCA-related phosphatase,Lrp,Mouse,Mus musculus,Protein-tyrosine phosphatase alpha,Ptpa,Ptpra,PTPTY-28,Receptor-type tyrosine-protein phosphatase alpha,R-PTP-alpha 96T
E0954m ELISA kit LCA-related phosphatase,Lrp,Mouse,Mus musculus,Protein-tyrosine phosphatase alpha,Ptpa,Ptpra,PTPTY-28,Receptor-type tyrosine-protein phosphatase alpha,R-PTP-alpha 96T
EIAAB33100 105 kDa islet cell antigen,BEM-3,Brain-enriched membrane-associated protein tyrosine phosphatase,ICA105,PTP IA-2,PTPLP,Ptprn,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase-like N,R-P


 

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