A2A8L5 (PTPRF_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Receptor-type tyrosine-protein phosphatase F
EC=3.1.3.48

Alternative name(s):
Leukocyte common antigen related
Short name=LAR

Gene names

Name:	Ptprf
Synonyms:	Lar

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1898 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) By similarity.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subunit structure	Interacts with GRIP1 By similarity. Interacts with PPFIA1, PPFIA2 and PPFIA3 By similarity. Interacts with PTPRF By similarity.
Subcellular location	Membrane; Single-pass membrane protein Potential.
Tissue specificity	Expressed in the cell of the T lineage but not in cells of any other hemopoietic lineage. Ref.1
Domain	The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one By similarity.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Receptor class 2A subfamily. Contains 8 fibronectin type-III domains. Contains 3 Ig-like C2-type (immunoglobulin-like) domains. Contains 2 tyrosine-protein phosphatase domains.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Ligand	Heparin-binding
Molecular function	Hydrolase Protein phosphatase Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	heparin binding Inferred from electronic annotation. Source: UniProtKB-KW protein tyrosine phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Potential

Chain

30 – 1898

1869

Receptor-type tyrosine-protein phosphatase F

PRO_0000370193

Regions

Topological domain

30 – 1254

1225

Extracellular Potential

Transmembrane

1255 – 1275

21

Helical; Potential

Topological domain

1276 – 1898

623

Cytoplasmic Potential

Domain

33 – 123

91

Ig-like C2-type 1

Domain

135 – 224

90

Ig-like C2-type 2

Domain

232 – 314

83

Ig-like C2-type 3

Domain

319 – 407

89

Fibronectin type-III 1

Domain

413 – 506

94

Fibronectin type-III 2

Domain

512 – 602

91

Fibronectin type-III 3

Domain

606 – 703

98

Fibronectin type-III 4

Domain

708 – 806

99

Fibronectin type-III 5

Domain

808 – 901

94

Fibronectin type-III 6

Domain

906 – 999

94

Fibronectin type-III 7

Domain

1002 – 1086

85

Fibronectin type-III 8

Domain

1343 – 1598

256

Tyrosine-protein phosphatase 1

Domain

1630 – 1889

260

Tyrosine-protein phosphatase 2

Region

68 – 77

10

Heparin-binding

Region

1539 – 1545

7

Substrate binding By similarity

Sites

Active site

1539

1

Phosphocysteine intermediate By similarity

Active site

1830

1

Phosphocysteine intermediate By similarity

Binding site

1507

1

Substrate By similarity

Binding site

1583

1

Substrate By similarity

Amino acid modifications

Glycosylation

117

1

N-linked (GlcNAc...) Potential

Glycosylation

250

1

N-linked (GlcNAc...) Potential

Glycosylation

295

1

N-linked (GlcNAc...) Potential

Glycosylation

721

1

N-linked (GlcNAc...) Ref.4

Glycosylation

936

1

N-linked (GlcNAc...) Ref.4

Glycosylation

941

1

N-linked (GlcNAc...) Ref.4

Glycosylation

957

1

N-linked (GlcNAc...) Potential

Glycosylation

960

1

N-linked (GlcNAc...) Ref.4

Disulfide bond

54 ↔ 107

Ref.5

Disulfide bond

156 ↔ 207

Ref.5

Disulfide bond

253 ↔ 298

By similarity

Experimental info

Sequence conflict

47

1

G → E in AAG40194. Ref.1

Sequence conflict

482

1

I → V in AAG40194. Ref.1

Sequence conflict

514 – 515

2

QP → RS in AAG40194. Ref.1

Sequence conflict

579

1

H → R in AAG40194. Ref.1

Sequence conflict

1006

1

A → T in AAG40194. Ref.1

Sequence conflict

1184

1

V → A in AAH57166. Ref.3

Sequence conflict

1374

1

N → D in AAG40194. Ref.1

Secondary structure

1

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1898

Helix Strand Turn

Details...

Beta strand

31 – 37

7

Beta strand

42 – 45

4

Beta strand

50 – 60

11

Beta strand

63 – 68

6

Beta strand

78 – 83

6

Helix

84 – 86

3

Beta strand

88 – 93

6

Helix

98 – 101

4

Beta strand

103 – 110

8

Beta strand

115 – 125

11

Beta strand

136 – 139

4

Beta strand

144 – 146

3

Beta strand

148 – 150

3

Beta strand

152 – 154

3

Beta strand

157 – 159

3

Beta strand

165 – 170

6

Turn

177 – 179

3

Beta strand

180 – 186

7

Beta strand

192 – 194

3

Helix

199 – 201

3

Beta strand

203 – 211

9

Beta strand

214 – 217

4

Beta strand

221 – 225

5

Sequences

	Sequence		Length	Mass (Da)
	A2A8L5 [UniParc]. Last modified February 20, 2007. Version 1. Checksum: 903FF6814F0BC914	FASTA	1,898	211,489
	10 20 30 40 50 60 MAPEPAPGRR MVPLVPALVM LGLMAGAHGD SKPVFVKVPE DQTGLSGGVA SFVCQATGEP 70 80 90 100 110 120 KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR DEAIYECTAT NSLGEINTSA 130 140 150 160 170 180 KLSVLEEDQL PSGFPTIDMG PQLKVVEKGR TATMLCAAGG NPDPEISWFK DFLPVDPAAS 190 200 210 220 230 240 NGRIKQLRSG ALQIESSEES DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS 250 260 270 280 290 300 QEVMPGGSVN LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV MRSANYTCVA 310 320 330 340 350 360 ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNTEPVSFY GIQYRAAGTD 370 380 390 400 410 420 GPFQEVDGVA STRYSIGGLS PFSEYAFRVL AVNSIGRGPP SEAVRARTGE QAPSSPPRRV 430 440 450 460 470 480 QARMLSASTM LVQWEPPEEP NGLVRGYRVY YTPDSRRPLS AWHKHNTDAG LLTTVGSLLP 490 500 510 520 530 540 GITYSLRVLA FTAVGDGPPS PTIQVKTQQG VPAQPADFQA NAESDTRIQL SWLLPPQERI 550 560 570 580 590 600 VKYELVYWAA EDEGQQHKVT FDPTSSYTLE DLKPDTLYHF QLAARSDLGV GVFTPTVEAR 610 620 630 640 650 660 TAQSTPSAPP QKVTCVSTGS TTVRVSWVPP PADSRNGIIT QYSVAYEAVD GEDRKRHVVD 670 680 690 700 710 720 GISREHSSWD LLGLEKWTEY RVWVRAHTDV GPGPESSPVL VRTDEDVPSG PPRKVEVEPL 730 740 750 760 770 780 NSTAVHVSWK LPVPNKQHGQ IRGYQVTYVR LENGEPRGQP IIQDVMLAEA QETTISGLTP 790 800 810 820 830 840 ETTYSITVAA YTTKGDGARS KPKVVTTTGA VPGRPTMMVS TTAMHTALLQ WHPPKELPGE 850 860 870 880 890 900 LLGYRLQYRR ADEARPNTID FGKDDQHFTV TGLHKGATYV FRLAAKNRAG PGEEFEKEIT 910 920 930 940 950 960 TPEDVPSGFP QNLRVTGLTT STTELTWDPP VLAERNGHIT NYTVVYRDIN SQLELQNVTN 970 980 990 1000 1010 1020 DTHLTLLGLK PDTTYDIKVR AHTSKGAGPL SPSIQSRTMP VEQVFAKNFR VAAAMKTSVL 1030 1040 1050 1060 1070 1080 LSWEVPDSYK SAVPFKILYN GQSVEVDGHS MRKLIADLQP NTEYSFVLMN RGSSAGGLQH 1090 1100 1110 1120 1130 1140 LVSIRTAPDL LPQKPLPASA FIEDGRFSLS MPQVQDPSLV RWFYIVVVPI DRVGGNLLAP 1150 1160 1170 1180 1190 1200 RWNTPEELEL DELLEAIEQG EEKQRRRRRQ AERLKPYVAA QVDVLPDTFT LGDKKSYRGF 1210 1220 1230 1240 1250 1260 YNRPLSPDLS YQCFVLASLK EPMDQKRYAS SPYSDEIVVQ VTPAQQQEEP EMLWVTGPVL 1270 1280 1290 1300 1310 1320 AVILIILIVI AILLFKRKRT HSPSSKDEQS IGLKDSLLAH SSDPVEMRRL NYQTPGMRDH 1330 1340 1350 1360 1370 1380 PPIPITDLAD NIERLKANDG LKFSQEYESI DPGQQFTWEN SNSEVNKPKN RYANVIAYDH 1390 1400 1410 1420 1430 1440 SRVLLTSIDG VPGSDYINAN YIDGYRKQNA YIATQGPLPE TMGDFWRMVW EQRTATVVMM 1450 1460 1470 1480 1490 1500 TRLEEKSRVK CDQYWPVRGT ETYGLIQVTL VDTVELATYT MRTFALHKSG SSEKRELRQF 1510 1520 1530 1540 1550 1560 QFMAWPDHGV PEYPTPILAF LRRVKACNPL DAGPMVVHCS AGVGRTGCFI VIDAMLERMK 1570 1580 1590 1600 1610 1620 HEKTVDIYGH VTCMRSQRNY MVQTEDQYVF IHEALLEAAM CGHTEVLARN LYAHIQKLGQ 1630 1640 1650 1660 1670 1680 VPPGESVTAM ELEFKLLANS KAHTSRFVSA NLPCNKFKNR LVNIMPYELT RVCLQPIRGV 1690 1700 1710 1720 1730 1740 EGSDYINASF LDGYRQQKAY IATQGPLAES TEDFWRMLWE HNSTIIVMLT KLREMGREKC 1750 1760 1770 1780 1790 1800 HQYWPAERSA RYQYFVVDPM AEYNMPQYIL REFKVTDARD GQSRTIRQFQ FTDWPEQGVP 1810 1820 1830 1840 1850 1860 KTGEGFIDFI GQVHKTKEQF GQDGPITVHC SAGVGRTGVF ITLSIVLERM RYEGVVDMFQ 1870 1880 1890 TVKTLRTQRP AMVQTEDQYQ LCYRAALEYL GSFDHYAT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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." Terszowski G., Jankowski A., Hendriks W.J.A.J., Rolink A.G., Kisielow P. Eur. J. Immunol. 31:832-840(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Thymus.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." 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. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 370-1898. Strain: FVB/N. Tissue: Mammary tumor.
[4]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-721; ASN-936; ASN-941 AND ASN-960, MASS SPECTROMETRY.
[5]	"The immunoglobulin-like domains 1 and 2 of the protein tyrosine phosphatase LAR adopt an unusual horseshoe-like conformation." Biersmith B.H., Hammel M., Geisbrecht E.R., Bouyain S. J. Mol. Biol. 408:616-627(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-226, HEPARIN-BINDING REGION, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF300943 mRNA. Translation: AAG40194.1.
AL807774, AL626764 Genomic DNA. Translation: CAM17264.1.
AL626764, AL807774 Genomic DNA. Translation: CAM27382.1.
BC057166 mRNA. Translation: AAH57166.1.

IPI

IPI00110264.

RefSeq

NP_035343.2. NM_011213.2.

UniGene

Mm.29855.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3PXH	X-ray	2.00	A	30-226	[»]

ProteinModelPortal

A2A8L5.

SMR

A2A8L5. Positions 30-1001, 1325-1893.

ModBase

Search...

Protein-protein interaction databases

IntAct

A2A8L5. 1 interaction.

PTM databases

PhosphoSite

A2A8L5.

Proteomic databases

PaxDb

A2A8L5.

PRIDE

A2A8L5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000049074; ENSMUSP00000039368; ENSMUSG00000033295.

GeneID

19268.

KEGG

mmu:19268.

UCSC

uc008ujq.1. mouse.

Organism-specific databases

CTD

5792.

MGI

MGI:102695. Ptprf.

Phylogenomic databases

eggNOG

COG5599.

GeneTree

ENSGT00590000082937.

HOGENOM

HOG000010250.

InParanoid

A2A8L5.

KO

K05695.

OMA

FTPTIEA.

OrthoDB

EOG4BG8V3.

Gene expression databases

ArrayExpress

A2A8L5.

Bgee

A2A8L5.

Genevestigator

A2A8L5.

Family and domain databases

Gene3D

2.60.40.10. 10 hits.

InterPro

IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]

Pfam

PF00041. fn3. 7 hits.
PF07679. I-set. 3 hits.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]

PRINTS

PR00700. PRTYPHPHTASE.

SMART

SM00060. FN3. 8 hits.
SM00409. IG. 1 hit.
SM00408. IGc2. 2 hits.
SM00194. PTPc. 2 hits.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 8 hits.

PROSITE

PS50853. FN3. 8 hits.
PS50835. IG_LIKE. 3 hits.
PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

NextBio

296150.

SOURCE

Search...

Entry information

Entry name

PTPRF_MOUSE

Accession

Primary (citable) accession number: A2A8L5
Secondary accession number(s): Q6PG86, Q9EQ17

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 20, 2007
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program