P10586 (PTPRF_HUMAN) 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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1907 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). Ref.13 The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Ref.13
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subunit structure	Interacts with GRIP1 By similarity. Interacts with PPFIA1, PPFIA2 and PPFIA3. Interacts with INSR. Ref.8 Ref.9
Subcellular location	Membrane; Single-pass type I membrane protein.
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.
Sequence caution	The sequence BAD66835.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA68754.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
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 Traceable author statement PubMed 7665159. Source: ProtInc transmembrane receptor protein tyrosine phosphatase signaling pathway Traceable author statement Ref.8. Source: ProtInc
Cellular_component	integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	heparin binding Inferred from electronic annotation. Source: UniProtKB-KW transmembrane receptor protein tyrosine phosphatase activity Traceable author statement Ref.8. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P10586-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P10586-2)

The sequence of this isoform differs from the canonical sequence as follows:
     772-780: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Potential

Chain

30 – 1907

1878

Receptor-type tyrosine-protein phosphatase F

PRO_0000025432

Regions

Topological domain

30 – 1263

1234

Extracellular Potential

Transmembrane

1264 – 1284

21

Helical; Potential

Topological domain

1285 – 1907

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 – 815

108

Fibronectin type-III 5

Domain

817 – 910

94

Fibronectin type-III 6

Domain

915 – 1008

94

Fibronectin type-III 7

Domain

1011 – 1095

85

Fibronectin type-III 8

Domain

1352 – 1607

256

Tyrosine-protein phosphatase 1

Domain

1639 – 1898

260

Tyrosine-protein phosphatase 2

Region

68 – 77

10

Heparin-binding By similarity

Region

1548 – 1554

7

Substrate binding By similarity

Sites

Active site

1548

1

Phosphocysteine intermediate Probable

Active site

1839

1

Phosphocysteine intermediate By similarity

Binding site

1516

1

Substrate By similarity

Binding site

1592

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...) Potential

Glycosylation

959

1

N-linked (GlcNAc...) Ref.11

Glycosylation

966

1

N-linked (GlcNAc...) Ref.10 Ref.11

Disulfide bond

54 ↔ 107

By similarity

Disulfide bond

156 ↔ 207

By similarity

Disulfide bond

253 ↔ 298

By similarity

Natural variations

Alternative sequence

772 – 780

9

Missing in isoform 2.

VSP_036617

Natural variant

412

1

A → V.
Corresponds to variant rs1065775 [ dbSNP | Ensembl ].

VAR_054766

Natural variant

450

1

Y → C.
Corresponds to variant rs3748796 [ dbSNP | Ensembl ].

VAR_020299

Natural variant

562

1

D → N.
Corresponds to variant rs3748800 [ dbSNP | Ensembl ].

VAR_020300

Experimental info

Mutagenesis

1548

1

C → S: Loss of activity. Ref.13

Sequence conflict

646

1

Y → H in CAA68754. Ref.1

Sequence conflict

1421

1

I → T in AAH48768. Ref.5

Secondary structure

1

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1907

Helix Strand Turn

Details...

Beta strand

31 – 37

7

Beta strand

42 – 45

4

Beta strand

50 – 60

11

Beta strand

63 – 68

6

Turn

75 – 77

3

Beta strand

78 – 83

6

Helix

84 – 86

3

Beta strand

88 – 93

6

Helix

98 – 101

4

Beta strand

103 – 111

9

Beta strand

114 – 125

12

Helix

127 – 129

3

Beta strand

136 – 139

4

Beta strand

144 – 147

4

Beta strand

152 – 154

3

Beta strand

157 – 159

3

Beta strand

165 – 170

6

Helix

177 – 179

3

Beta strand

183 – 186

4

Beta strand

192 – 194

3

Helix

199 – 201

3

Beta strand

203 – 211

9

Beta strand

214 – 217

4

Beta strand

221 – 226

6

Beta strand

323 – 331

9

Beta strand

334 – 340

7

Beta strand

348 – 356

9

Beta strand

371 – 378

8

Beta strand

384 – 392

9

Beta strand

404 – 407

4

Beta strand

610 – 616

7

Beta strand

618 – 628

11

Beta strand

639 – 652

14

Beta strand

657 – 659

3

Beta strand

667 – 673

7

Beta strand

679 – 688

10

Beta strand

699 – 702

4

Beta strand

825 – 830

6

Beta strand

835 – 841

7

Beta strand

852 – 859

8

Beta strand

866 – 871

6

Beta strand

876 – 880

5

Beta strand

887 – 896

10

Beta strand

899 – 909

11

Beta strand

920 – 923

4

Beta strand

925 – 927

3

Beta strand

935 – 937

3

Beta strand

950 – 957

8

Beta strand

963 – 971

9

Beta strand

984 – 987

4

Helix

1334 – 1344

11

Turn

1347 – 1349

3

Helix

1350 – 1358

9

Helix

1368 – 1371

4

Turn

1373 – 1375

3

Helix

1376 – 1378

3

Turn

1388 – 1390

3

Turn

1401 – 1404

4

Beta strand

1407 – 1413

7

Beta strand

1416 – 1423

8

Turn

1428 – 1430

3

Helix

1431 – 1440

10

Beta strand

1445 – 1448

4

Beta strand

1452 – 1454

3

Beta strand

1466 – 1472

7

Beta strand

1475 – 1484

10

Beta strand

1486 – 1497

12

Beta strand

1503 – 1511

9

Beta strand

1516 – 1518

3

Helix

1524 – 1536

13

Beta strand

1544 – 1553

10

Helix

1554 – 1571

18

Helix

1576 – 1584

9

Helix

1594 – 1610

17

Helix

1617 – 1619

3

Helix

1620 – 1627

8

Helix

1638 – 1644

7

Turn

1645 – 1647

3

Turn

1657 – 1660

4

Helix

1662 – 1667

6

Turn

1677 – 1679

3

Turn

1690 – 1693

4

Beta strand

1696 – 1700

5

Beta strand

1703 – 1705

3

Beta strand

1709 – 1712

4

Helix

1717 – 1719

3

Helix

1720 – 1729

10

Beta strand

1734 – 1737

4

Beta strand

1741 – 1743

3

Beta strand

1746 – 1749

4

Beta strand

1755 – 1757

3

Beta strand

1759 – 1761

3

Beta strand

1764 – 1773

10

Beta strand

1775 – 1786

12

Turn

1787 – 1789

3

Beta strand

1792 – 1800

9

Beta strand

1805 – 1807

3

Helix

1813 – 1828

16

Beta strand

1835 – 1844

10

Helix

1845 – 1862

18

Beta strand

1863 – 1865

3

Helix

1867 – 1874

8

Turn

1875 – 1877

3

Helix

1885 – 1897

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 24, 2009. Version 2. Checksum: 4A7C14A2090EA88F	FASTA	1,907	212,879
	10 20 30 40 50 60 MAPEPAPGRT MVPLVPALVM LGLVAGAHGD SKPVFIKVPE DQTGLSGGVA SFVCQATGEP 70 80 90 100 110 120 KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR DEAIYECTAT NSLGEINTSA 130 140 150 160 170 180 KLSVLEEEQL PPGFPSIDMG PQLKVVEKAR TATMLCAAGG NPDPEISWFK DFLPVDPATS 190 200 210 220 230 240 NGRIKQLRSG ALQIESSEES DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS 250 260 270 280 290 300 QEVMPGGSVN LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV VRSANYTCVA 310 320 330 340 350 360 ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNSEPVTYY GIQYRAAGTE 370 380 390 400 410 420 GPFQEVDGVA TTRYSIGGLS PFSEYAFRVL AVNSIGRGPP SEAVRARTGE QAPSSPPRRV 430 440 450 460 470 480 QARMLSASTM LVQWEPPEEP NGLVRGYRVY YTPDSRRPPN AWHKHNTDAG LLTTVGSLLP 490 500 510 520 530 540 GITYSLRVLA FTAVGDGPPS PTIQVKTQQG VPAQPADFQA EVESDTRIQL SWLLPPQERI 550 560 570 580 590 600 IMYELVYWAA EDEDQQHKVT FDPTSSYTLE DLKPDTLYRF QLAARSDMGV GVFTPTIEAR 610 620 630 640 650 660 TAQSTPSAPP QKVMCVSMGS TTVRVSWVPP PADSRNGVIT QYSVAYEAVD GEDRGRHVVD 670 680 690 700 710 720 GISREHSSWD LVGLEKWTEY RVWVRAHTDV GPGPESSPVL VRTDEDVPSG PPRKVEVEPL 730 740 750 760 770 780 NSTAVHVYWK LPVPSKQHGQ IRGYQVTYVR LENGEPRGLP IIQDVMLAEA QWRPEESEDY 790 800 810 820 830 840 ETTISGLTPE TTYSVTVAAY TTKGDGARSK PKIVTTTGAV PGRPTMMIST TAMNTALLQW 850 860 870 880 890 900 HPPKELPGEL LGYRLQYCRA DEARPNTIDF GKDDQHFTVT GLHKGTTYIF RLAAKNRAGL 910 920 930 940 950 960 GEEFEKEIRT PEDLPSGFPQ NLHVTGLTTS TTELAWDPPV LAERNGRIIS YTVVFRDINS 970 980 990 1000 1010 1020 QQELQNITTD TRFTLTGLKP DTTYDIKVRA WTSKGSGPLS PSIQSRTMPV EQVFAKNFRV 1030 1040 1050 1060 1070 1080 AAAMKTSVLL SWEVPDSYKS AVPFKILYNG QSVEVDGHSM RKLIADLQPN TEYSFVLMNR 1090 1100 1110 1120 1130 1140 GSSAGGLQHL VSIRTAPDLL PHKPLPASAY IEDGRFDLSM PHVQDPSLVR WFYIVVVPID 1150 1160 1170 1180 1190 1200 RVGGSMLTPR WSTPEELELD ELLEAIEQGG EEQRRRRRQA ERLKPYVAAQ LDVLPETFTL 1210 1220 1230 1240 1250 1260 GDKKNYRGFY NRPLSPDLSY QCFVLASLKE PMDQKRYASS PYSDEIVVQV TPAQQQEEPE 1270 1280 1290 1300 1310 1320 MLWVTGPVLA VILIILIVIA ILLFKRKRTH SPSSKDEQSI GLKDSLLAHS SDPVEMRRLN 1330 1340 1350 1360 1370 1380 YQTPGMRDHP PIPITDLADN IERLKANDGL KFSQEYESID PGQQFTWENS NLEVNKPKNR 1390 1400 1410 1420 1430 1440 YANVIAYDHS RVILTSIDGV PGSDYINANY IDGYRKQNAY IATQGPLPET MGDFWRMVWE 1450 1460 1470 1480 1490 1500 QRTATVVMMT RLEEKSRVKC DQYWPARGTE TCGLIQVTLL DTVELATYTV RTFALHKSGS 1510 1520 1530 1540 1550 1560 SEKRELRQFQ FMAWPDHGVP EYPTPILAFL RRVKACNPLD AGPMVVHCSA GVGRTGCFIV 1570 1580 1590 1600 1610 1620 IDAMLERMKH EKTVDIYGHV TCMRSQRNYM VQTEDQYVFI HEALLEAATC GHTEVPARNL 1630 1640 1650 1660 1670 1680 YAHIQKLGQV PPGESVTAME LEFKLLASSK AHTSRFISAN LPCNKFKNRL VNIMPYELTR 1690 1700 1710 1720 1730 1740 VCLQPIRGVE GSDYINASFL DGYRQQKAYI ATQGPLAEST EDFWRMLWEH NSTIIVMLTK 1750 1760 1770 1780 1790 1800 LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTIRQFQF 1810 1820 1830 1840 1850 1860 TDWPEQGVPK TGEGFIDFIG QVHKTKEQFG QDGPITVHCS AGVGRTGVFI TLSIVLERMR 1870 1880 1890 1900 YEGVVDMFQT VKTLRTQRPA MVQTEDQYQL CYRAALEYLG SFDHYAT
	Isoform 2 [UniParc]. Checksum: 5138123452E59A4E	FASTA	1,898	211,687
	10 20 30 40 50 60 MAPEPAPGRT MVPLVPALVM LGLVAGAHGD SKPVFIKVPE DQTGLSGGVA SFVCQATGEP 70 80 90 100 110 120 KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR DEAIYECTAT NSLGEINTSA 130 140 150 160 170 180 KLSVLEEEQL PPGFPSIDMG PQLKVVEKAR TATMLCAAGG NPDPEISWFK DFLPVDPATS 190 200 210 220 230 240 NGRIKQLRSG ALQIESSEES DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS 250 260 270 280 290 300 QEVMPGGSVN LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV VRSANYTCVA 310 320 330 340 350 360 ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNSEPVTYY GIQYRAAGTE 370 380 390 400 410 420 GPFQEVDGVA TTRYSIGGLS PFSEYAFRVL AVNSIGRGPP SEAVRARTGE QAPSSPPRRV 430 440 450 460 470 480 QARMLSASTM LVQWEPPEEP NGLVRGYRVY YTPDSRRPPN AWHKHNTDAG LLTTVGSLLP 490 500 510 520 530 540 GITYSLRVLA FTAVGDGPPS PTIQVKTQQG VPAQPADFQA EVESDTRIQL SWLLPPQERI 550 560 570 580 590 600 IMYELVYWAA EDEDQQHKVT FDPTSSYTLE DLKPDTLYRF QLAARSDMGV GVFTPTIEAR 610 620 630 640 650 660 TAQSTPSAPP QKVMCVSMGS TTVRVSWVPP PADSRNGVIT QYSVAYEAVD GEDRGRHVVD 670 680 690 700 710 720 GISREHSSWD LVGLEKWTEY RVWVRAHTDV GPGPESSPVL VRTDEDVPSG PPRKVEVEPL 730 740 750 760 770 780 NSTAVHVYWK LPVPSKQHGQ IRGYQVTYVR LENGEPRGLP IIQDVMLAEA QETTISGLTP 790 800 810 820 830 840 ETTYSVTVAA YTTKGDGARS KPKIVTTTGA VPGRPTMMIS TTAMNTALLQ WHPPKELPGE 850 860 870 880 890 900 LLGYRLQYCR ADEARPNTID FGKDDQHFTV TGLHKGTTYI FRLAAKNRAG LGEEFEKEIR 910 920 930 940 950 960 TPEDLPSGFP QNLHVTGLTT STTELAWDPP VLAERNGRII SYTVVFRDIN SQQELQNITT 970 980 990 1000 1010 1020 DTRFTLTGLK PDTTYDIKVR AWTSKGSGPL SPSIQSRTMP VEQVFAKNFR VAAAMKTSVL 1030 1040 1050 1060 1070 1080 LSWEVPDSYK SAVPFKILYN GQSVEVDGHS MRKLIADLQP NTEYSFVLMN RGSSAGGLQH 1090 1100 1110 1120 1130 1140 LVSIRTAPDL LPHKPLPASA YIEDGRFDLS MPHVQDPSLV RWFYIVVVPI DRVGGSMLTP 1150 1160 1170 1180 1190 1200 RWSTPEELEL DELLEAIEQG GEEQRRRRRQ AERLKPYVAA QLDVLPETFT LGDKKNYRGF 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 SNLEVNKPKN RYANVIAYDH 1390 1400 1410 1420 1430 1440 SRVILTSIDG VPGSDYINAN YIDGYRKQNA YIATQGPLPE TMGDFWRMVW EQRTATVVMM 1450 1460 1470 1480 1490 1500 TRLEEKSRVK CDQYWPARGT ETCGLIQVTL LDTVELATYT VRTFALHKSG SSEKRELRQF 1510 1520 1530 1540 1550 1560 QFMAWPDHGV PEYPTPILAF LRRVKACNPL DAGPMVVHCS AGVGRTGCFI VIDAMLERMK 1570 1580 1590 1600 1610 1620 HEKTVDIYGH VTCMRSQRNY MVQTEDQYVF IHEALLEAAT CGHTEVPARN LYAHIQKLGQ 1630 1640 1650 1660 1670 1680 VPPGESVTAM ELEFKLLASS KAHTSRFISA 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]	"A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen." Streuli M., Krueger N.X., Hall L.R., Schlossman S.F., Saito H. J. Exp. Med. 168:1523-1530(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Tonsil.
[2]	"Alternative splice variants encoding unstable protein domains exist in the human brain." Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K. J. Mol. Biol. 343:1207-1220(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Brain.
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORM 2). Tissue: Retinoblastoma.
[6]	"A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila." Streuli M., Krueger N.X., Tsai A.Y.M., Saito H. Proc. Natl. Acad. Sci. U.S.A. 86:8698-8702(1989) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[7]	"Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR." Streuli M., Krueger N.X., Thai T., Tang M., Saito H. EMBO J. 9:2399-2407(1990) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS.
[8]	"Functional association between the insulin receptor and the transmembrane protein-tyrosine phosphatase LAR in intact cells." Ahmad F., Goldstein B.J. J. Biol. Chem. 272:448-457(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH INSR.
[9]	"Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins." Serra-Pages C., Medley Q.G., Tang M., Hart A., Streuli M. J. Biol. Chem. 273:15611-15620(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPFIA1; PPFIA2 AND PPFIA3.
[10]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-966, MASS SPECTROMETRY. Tissue: Plasma.
[11]	"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-959 AND ASN-966, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Crystal structure of the tandem phosphatase domains of RPTP LAR." Nam H.J., Poy F., Krueger N.X., Saito H., Frederick C.A. Cell 97:449-457(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1334-1897, FUNCTION, MUTAGENESIS OF CYS-1548.
[14]	"Solution structures of FN3 domains of human receptor-type tyrosine-protein phosphatase F." RIKEN structural genomics initiative (RSGI) Submitted (AUG-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 319-415 AND 596-1010.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00815 mRNA. Translation: CAA68754.1. Different initiation.
AB177857 mRNA. Translation: BAD66835.1. Different initiation.
AL583862, AC092815 Genomic DNA. Translation: CAI14894.1.
AL583862, AC092815 Genomic DNA. Translation: CAI14895.1.
CH471059 Genomic DNA. Translation: EAX07086.1.
CH471059 Genomic DNA. Translation: EAX07087.1.
CH471059 Genomic DNA. Translation: EAX07088.1.
CH471059 Genomic DNA. Translation: EAX07089.1.
BC048768 mRNA. Translation: AAH48768.1.

IPI

IPI00107831.
IPI00465186.

PIR

TDHULK. S03841.

RefSeq

NP_002831.2. NM_002840.3.
NP_569707.2. NM_130440.2.

UniGene

Hs.272062.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1LAR	X-ray	2.00	A/B	1334-1897	[»]
2DJU	NMR	-	A	319-411	[»]
2DN7	NMR	-	A	821-914	[»]
2EDX	NMR	-	A	596-716	[»]
2EDY	NMR	-	A	915-1010	[»]
2YD5	X-ray	2.20	A	29-231	[»]
2YD8	X-ray	2.05	A	29-231	[»]

ProteinModelPortal

P10586.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1189049.

STRING

9606.ENSP00000353030.

PTM databases

PhosphoSite

P10586.

Polymorphism databases

DMDM

226709091.

Proteomic databases

PaxDb

P10586.

PRIDE

P10586.

Protocols and materials databases

DNASU

5792.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000359947; ENSP00000353030; ENSG00000142949.
ENST00000372413; ENSP00000361490; ENSG00000142949.
ENST00000372414; ENSP00000361491; ENSG00000142949.
ENST00000438120; ENSP00000398822; ENSG00000142949.

GeneID

5792.

KEGG

hsa:5792.

UCSC

uc001cjr.3. human.
uc001cjs.3. human.

Organism-specific databases

CTD

5792.

GeneCards

GC01P043990.

HGNC

HGNC:9670. PTPRF.

HPA

HPA012710.

MIM

179590. gene.

neXtProt

NX_P10586.

PharmGKB

PA34015.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5599.

HOVERGEN

HBG053758.

InParanoid

P10586.

KO

K05695.

OMA

FTPTIEA.

OrthoDB

EOG4BG8V3.

Enzyme and pathway databases

SignaLink

P10586.

Gene expression databases

ArrayExpress

P10586.

Bgee

P10586.

CleanEx

HS_PTPRF.

Genevestigator

P10586.

GermOnline

ENSG00000142949. Homo sapiens.

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.
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.
SM00408. IGc2. 3 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

BindingDB

P10586.

ChEMBL

CHEMBL3521.

ChiTaRS

PTPRF. human.

EvolutionaryTrace

P10586.

GenomeRNAi

5792.

NextBio

22550.

PMAP-CutDB

Q5T022.

SOURCE

Search...

Entry information

Entry name

PTPRF_HUMAN

Accession

Primary (citable) accession number: P10586
Secondary accession number(s): D3DPX6 , D3DPX7, Q5T021, Q5T022, Q5W9G2, Q86WS0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	March 24, 2009
Last modified:	May 29, 2013
This is version 163 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.