[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). PubMed=2944116 [NCBI, ExPASy, EBI, Israel, Japan] Saga Y., Tung J.-S., Shen F.-W., Boyse E.A.; "Sequences of Ly-5 cDNA: isoform-related diversity of Ly-5 mRNA."; Proc. Natl. Acad. Sci. U.S.A. 83:6940-6944(1986).
[2]	ERRATUM, AND SEQUENCE REVISION. Saga Y., Tung J.-S., Shen F.-W., Boyse E.A.; Proc. Natl. Acad. Sci. U.S.A. 84:1991-1991(1987).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). STRAIN=BALB/c; PubMed=1822988 [NCBI, ExPASy, EBI, Israel, Japan] Zebedee S.L., Barritt D.S., Raschke W.C.; "Comparison of mouse Ly5a and Ly5b leucocyte common antigen alleles."; Dev. Immunol. 1:243-254(1991).
[4]	NUCLEOTIDE SEQUENCE OF 1-226 (ISOFORM 2). PubMed=3037546 [NCBI, ExPASy, EBI, Israel, Japan] Saga Y., Tung J.-S., Shen F.-W.W., Boyse E.A.; "Alternative use of 5' exons in the specification of Ly-5 isoforms distinguishing hematopoietic cell lineages."; Proc. Natl. Acad. Sci. U.S.A. 84:5364-5368(1987).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22. PubMed=3211131 [NCBI, ExPASy, EBI, Israel, Japan] Saga Y., Tung J.-S., Shen F.-W.W., Pancoast T.C., Boyse E.A.; "Organization of the Ly-5 gene."; Mol. Cell. Biol. 8:4889-4895(1988).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22. PubMed=2522930 [NCBI, ExPASy, EBI, Israel, Japan] Johnson N.A., Meyer C.M., Pingel J.T., Thomas M.L.; "Sequence conservation in potential regulatory regions of the mouse and human leukocyte common antigen gene."; J. Biol. Chem. 264:6220-6229(1989).
[7]	NUCLEOTIDE SEQUENCE [MRNA] OF 10-263 (ISOFORM 3). TISSUE=T-cell; PubMed=3864163 [NCBI, ExPASy, EBI, Israel, Japan] Shen F.-W., Saga Y., Litman G., Freeman G., Tung J.-S., Cantor H., Boyse E.A.; "Cloning of Ly-5 cDNA."; Proc. Natl. Acad. Sci. U.S.A. 82:7360-7363(1985).
[8]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 31-73. DOI=10.1007/BF00345505; PubMed=3417340 [NCBI, ExPASy, EBI, Israel, Japan] Tung J.-S., Saga Y., Boyse E.A.; "Structural features of Ly-5 glycoproteins of the mouse and counterparts in other mammals."; Immunogenetics 28:271-277(1988).
[9]	NUCLEOTIDE SEQUENCE OF 730-838. PubMed=1932742 [NCBI, ExPASy, EBI, Israel, Japan] Yi T., Cleveland J.L., Ihle J.N.; "Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification."; Blood 78:2222-2228(1991).
[10]	NUCLEOTIDE SEQUENCE [MRNA] OF 961-1291. PubMed=2948186 [NCBI, ExPASy, EBI, Israel, Japan] Raschke W.C.; "Cloned murine T200 (Ly-5) cDNA reveals multiple transcripts within B- and T-lymphocyte lineages."; Proc. Natl. Acad. Sci. U.S.A. 84:161-165(1987).
[11]	PARTIAL PROTEIN SEQUENCE. DOI=10.1007/BF00404697; PubMed=3570377 [NCBI, ExPASy, EBI, Israel, Japan] Gonez L.J., Walker I.D., Sandrin M.S., McKenzie I.F.; "High sequence conservation between rat (T200) and mouse (Ly-5) leukocyte common antigens."; Immunogenetics 25:263-266(1987).
[12]	INTERACTION WITH GANAB AND PRKCSH. DOI=10.1074/jbc.272.20.13117; PubMed=9148925 [NCBI, ExPASy, EBI, Israel, Japan] Arendt C.W., Ostergaard H.L.; "Identification of the CD45-associated 116-kDa and 80-kDa proteins as the alpha- and beta-subunits of alpha-glucosidase II."; J. Biol. Chem. 272:13117-13125(1997).

Comments

FUNCTION: Required for T-cell activation through the antigen receptor. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits an dephosphorylates SKAP1 and FYN.
CATALYTIC ACTIVITY: Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate.
SUBUNIT: Interacts with SKAP1 (By similarity). Binds GANAB and PRKCSH.
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	B220
Isoform ID	P06800-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	P06800-2
Features which should be applied to build the isoform sequence: VSP_012441.

Name	3
Isoform ID	P06800-3
Features which should be applied to build the isoform sequence: VSP_012442.

DEVELOPMENTAL STAGE: Expression is restricted to the hematopoietic compartment of development.
DOMAIN: The first PTPase domain interacts with SKAP1 (By similarity).
PTM: Heavily N- and O-glycosylated.
SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Receptor class 1/6 subfamily.
SIMILARITY: Contains 2 fibronectin type-III domains.
SIMILARITY: Contains 2 tyrosine-protein phosphatase domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M14342; AAA39458.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M92933; AAA39459.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M17320; AAA60449.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M22456; AAB46374.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M11934; AAA39461.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M23241; AAA39460.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M15174; AAA40161.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M23354; AAA39462.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A23329; A23329.
A28334; A28334.
A28335; A28335.
I57644; I57644.

UniGene

Mm.391573

3D structure databases

HSSP

P18052; 1YFO. [HSSP ENTRY / PDB]

P06800; 612-1219.

PTM databases

P06800; -.

Organism-specific databases

MGI

MGI:97810; Ptprc.

Gene expression databases

ArrayExpress

P06800; -.

CleanEx

MM_PTPRC; -.

GermOnline

ENSMUSG00000026395; Mus musculus.

Ontologies

GO:0009897;	Cellular component: external side of plasma membrane (inferred from direct assay from MGI).
GO:0005925;	Cellular component: focal adhesion (inferred from direct assay from UniProtKB).
GO:0005887;	Cellular component: integral to plasma membrane (inferred from sequence or structural similarity from UniProtKB).
GO:0043395;	Molecular function: heparan sulfate proteoglycan binding (inferred from direct assay from MGI).
GO:0008201;	Molecular function: heparin binding (inferred from direct assay from MGI).
GO:0019901;	Molecular function: protein kinase binding (inferred from physical interaction from UniProtKB).
GO:0004725;	Molecular function: protein tyrosine phosphatase activity (inferred from sequence or structural similarity from UniProtKB).
GO:0000187;	Biological process: activation of MAPK activity (inferred from mutant phenotype from MGI).
GO:0051607;	Biological process: defense response to virus (inferred from mutant phenotype from UniProtKB).
GO:0034113;	Biological process: heterotypic cell-cell adhesion (inferred from mutant phenotype from MGI).
GO:0007159;	Biological process: leukocyte adhesion (inferred from mutant phenotype from MGI).
GO:0001960;	Biological process: negative regulation of cytokine mediated signaling pathway (inferred from direct assay from UniProtKB).
GO:0050732;	Biological process: negative regulation of peptidyl-tyrosine phosphorylation (inferred from mutant phenotype from MGI).
GO:0031953;	Biological process: negative regulation of protein amino acid autophosphorylation (inferred from mutant phenotype from MGI).
GO:0006469;	Biological process: negative regulation of protein kinase activity (inferred from direct assay from UniProtKB).
GO:0001915;	Biological process: negative regulation of T cell mediated cytotoxicity (inferred from mutant phenotype from UniProtKB).
GO:0045060;	Biological process: negative thymic T cell selection (inferred from mutant phenotype from MGI).
GO:0046641;	Biological process: positive regulation of alpha-beta T cell proliferation (inferred from mutant phenotype from MGI).
GO:0050857;	Biological process: positive regulation of antigen receptor-mediated signaling pathway (inferred from mutant phenotype from UniProtKB).
GO:0030890;	Biological process: positive regulation of B cell proliferation (inferred from mutant phenotype from MGI).
GO:0045588;	Biological process: positive regulation of gamma-delta T cell differentiation (inferred from mutant phenotype from MGI).
GO:0002925;	Biological process: positive regulation of humoral immune response mediated by circulating immunoglobulin (inferred from mutant phenotype from MGI).
GO:0048304;	Biological process: positive regulation of isotype switching to IgG isotypes (inferred from mutant phenotype from MGI).
GO:0043410;	Biological process: positive regulation of MAPKKK cascade (inferred from mutant phenotype from MGI).
GO:0001916;	Biological process: positive regulation of T cell mediated cytotoxicity (inferred from mutant phenotype from MGI).
GO:0045059;	Biological process: positive thymic T cell selection (inferred from mutant phenotype from MGI).
GO:0006470;	Biological process: protein amino acid dephosphorylation (inferred from direct assay from UniProtKB).
GO:0045577;	Biological process: regulation of B cell differentiation (inferred from mutant phenotype from MGI).
GO:0050855;	Biological process: regulation of B cell receptor signaling pathway (inferred from mutant phenotype from MGI).
GO:0051726;	Biological process: regulation of cell cycle (inferred from direct assay from UniProtKB).
GO:0051209;	Biological process: release of sequestered calcium ion into cytosol (inferred from direct assay from UniProtKB).
GO:0050852;	Biological process: T cell receptor signaling pathway (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR008957; Fibronectin_typ-III-like_fold.
IPR003961; FN_III.
IPR016335; Leukocyte_common_Ag.
IPR000387; Tyr_Pase.
IPR016130; Tyr_Pase_AS.
IPR000242; Tyr_Pase_rcpt/non-rcpt.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.30; FN_III-like; 1.

Pfam

PF00102; Y_phosphatase; 2.
Pfam graphical view of domain structure.

PIRSF

PIRSF002004; Leukocyte_common_antigen; 1.

PRINTS

PR00700; PRTYPHPHTASE.

SMART

SM00060; FN3; 2.
SM00194; PTPc; 2.
SMART graphical view of domain structure.

PROSITE

PS50853; FN3; 2.
PS00383; TYR_PHOSPHATASE_1; 1.
PS50056; TYR_PHOSPHATASE_2; 2.
PS50055; TYR_PHOSPHATASE_PTP; 2.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSMUSG00000026395; Mus musculus. [Contig view]

Phylogenomic databases

HOVERGEN

P06800; -.

Other

SOURCE

Ptprc; Mus musculus.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Direct protein sequencing; Glycoprotein; Hydrolase; Membrane; Phosphoprotein; Protein phosphatase; Repeat; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`
`CHAIN`	`24 1291`	`1268`	`Leukocyte common antigen.`	`PRO_0000025471`
`TOPO_DOM`	`24 564`	`541`	`Extracellular (Potential).`
`TRANSMEM`	`565 586`	`22`	`Potential.`
`TOPO_DOM`	`587 1291`	`705`	`Cytoplasmic (Potential).`
`DOMAIN`	`371 467`	`97`	`Fibronectin type-III 1.`
`DOMAIN`	`472 559`	`88`	`Fibronectin type-III 2.`
`DOMAIN`	`640 899`	`260`	`Tyrosine-protein phosphatase 1.`
`DOMAIN`	`931 1214`	`284`	`Tyrosine-protein phosphatase 2.`
`ACT_SITE`	`840 840`		`Phosphocysteine intermediate (By similarity).`
`ACT_SITE`	`1155 1155`		`Phosphocysteine intermediate (By similarity).`
`MOD_RES`	`984 984`		`Phosphoserine (By similarity).`
`MOD_RES`	`992 992`		`Phosphoserine (By similarity).`
`MOD_RES`	`996 996`		`Phosphoserine (By similarity).`
`CARBOHYD`	`64 64`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`150 150`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`161 161`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`207 207`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`211 211`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`218 218`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`253 253`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`258 258`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`290 290`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`311 311`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`322 322`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`347 347`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`416 416`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`427 427`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`457 457`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`489 489`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`518 518`		`N-linked (GlcNAc...) (Potential).`
`VAR_SEQ`	`31 169`		`Missing (in isoform 3).`	`VSP_012442`
`VAR_SEQ`	`31 73`		`Missing (in isoform 2).`	`VSP_012441`
`CONFLICT`	`300 300`		`K -> E (in Ref. 3; AAA39459).`
`CONFLICT`	`398 398`		`V -> A (in Ref. 3; AAA39459).`
`CONFLICT`	`402 403`		`ES -> DP (in Ref. 3; AAA39459).`
`CONFLICT`	`476 476`		`N -> T (in Ref. 3; AAA39459).`
`CONFLICT`	`518 520`		`NTT -> KYN (in Ref. 3; AAA39459).`
`CONFLICT`	`528 528`		`G -> V (in Ref. 3; AAA39459).`
`CONFLICT`	`556 556`		`S -> N (in Ref. 3; AAA39459).`
`CONFLICT`	`588 588`		`S -> I (in Ref. 3; AAA39459).`
`CONFLICT`	`906 906`		`Q -> E (in Ref. 3; AAA39459).`
`CONFLICT`	`931 931`		`R -> L (in Ref. 3; AAA39459).`
`CONFLICT`	`953 953`		`G -> E (in Ref. 3; AAA39459).`
`CONFLICT`	`959 959`		`K -> N (in Ref. 3; AAA39459).`

Sequence information

Length: 1291 AA [This is the length of the unprocessed precursor]

Molecular weight: 144404 Da [This is the MW of the unprocessed precursor]

CRC64: A8061F3590C0F4FA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGLWLKLLAF GFALLDTEVF VTGQTPTPSD ELSTTENALL LPQSDPLPAR TTESTPPSIS 

        70         80         90        100        110        120 
ERGNGSSETT YHPGVLSTLL PHLSPQPDSQ TPSAGGADTQ TFSSQADNPT LTPAPGGGTD 

       130        140        150        160        170        180 
PPGVPGERTV PGTIPADTAF PVDTPSLARN SSAASPTHTS NVSTTDISSG ASLTTLTPST 

       190        200        210        220        230        240 
LGLASTDPPS TTIATTTKQT CAAMFGNITV NYTYESSNQT FKADLKDVQN AKCGNEDCEN 

       250        260        270        280        290        300 
VLNNLEECSQ IKNISVSNDS CAPATTIDLY VPPGTDKFSL HDCTPKEKAN TSICLEWKTK 

       310        320        330        340        350        360 
NLDFRKCNSD NISYVLHCEP ENNTKCIRRN TFIPERCQLD NLRAQTNYTC VAEILYRGVK 

       370        380        390        400        410        420 
LVKNVINVQT DLGIPETPKP SCGDPAARKT LVSWPEPVSK PESASKPHGY VLCYKNNSEK 

       430        440        450        460        470        480 
CKSLPNNVTS FEVESLKPYK YYEVSLLAYV NGKIQRNGTA EKCNFHTKAD RPDKVNGMKT 

       490        500        510        520        530        540 
SRPTDNSINV TCGPPYETNG PKTFYILVVR SGGSFVTNTT KTNCQFYGDN LYYSTDYEFL 

       550        560        570        580        590        600 
VSFHNGVYEG DSVIRSESTN FNAKALIIFL VFLIIVTSIA LLVVLYKSYD LRKKRSSNLD 

       610        620        630        640        650        660 
EQQELVERDD EKQLMDVEPI HSDILLETYK RKIADEGRLF LAEFQSIPRV FSKFPIKDAR 

       670        680        690        700        710        720 
KPHNQNKNRY VDILPYDYNR VELSEINGDA GSTYINASYI DGFKEPRKYI AAQGPRDETV 

       730        740        750        760        770        780 
DDFWRMIWEQ KATVIVMVTR CEEGNRNKCA EYWPSMEEGT RAFKDIVVTI NDHKRCPDYI 

       790        800        810        820        830        840 
IQKLNVAHKK EKATGREVTH IQFTSWPDHG VPEDPHLLLK LRRRVNAFSN FFSGPIVVHC 

       850        860        870        880        890        900 
SAGVGRTGTY IGIDAMLEGL EAEGKVDVYG YVVKLRRQRC LMVQVEAQYI LIHQALVEYN 

       910        920        930        940        950        960 
QFGETQVNLS ELHSCLHNMK KRDPPSDPSP REAEYQRLPS YRSWRTQHIG NQGENKKKKR 

       970        980        990       1000       1010       1020 
NSNVVPYDFN RVPLKHELEM SKESEPESDE SSDDDSDSEE TSKYINASFV MSYWKPEMMI 

      1030       1040       1050       1060       1070       1080 
AAQGPLKETI GDFWQMIFQR KVKVIVMLTE LVNGDQEVCA QYWGEGKQTY GDMEVEMKDT 

      1090       1100       1110       1120       1130       1140 
NRASAYTLRT FELRHSKRKE PRTVYQYQCT TWKGEELPAE PKDLVSMIQD LKQKLPKASP 

      1150       1160       1170       1180       1190       1200 
EGMKYHKHAS ILVHCRDGSQ QTGLFCALFN LLESAETEDV VDVFQVVKSL RKARPGVVCS 

      1210       1220       1230       1240       1250       1260 
YEQYQFLYDI IASIYPAQNG QVKKTNSQDK IEFHNEVDGG KQDANCVRPD GPLNKAQEDS 

      1270       1280       1290 
RGVGTPEPTN SAEEPEHAAN GSASPAPTQS S

P06800 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools