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B1AUH1 (PTPRU_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor-type tyrosine-protein phosphatase U

Short name=R-PTP-U
EC=3.1.3.48
Alternative name(s):
Ftp-1
Pancreatic carcinoma phosphatase 2
Short name=PCP-2
Protein-tyrosine phosphatase-lamda
Short name=PTP-lambda
Short name=PTPlambda
Receptor-type protein-tyrosine phosphatase psi
Short name=R-PTP-psi
Gene names
Name:Ptpru
Synonyms:Pcp2, Ptpf
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1446 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis By similarity.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Forms homooligomeric complexes which mediate cell homotypic adhesion Probable. Interacts (via the cytoplasmic juxtamembrane domain) with CTNNB1; may mediate interaction with the cadherin/catenin adhesion complex. Interacts with KIT By similarity. May interact with AP3B1 By similarity. Ref.2

Subcellular location

Cell junction By similarity. Cell membrane; Single-pass type I membrane protein By similarity.

Tissue specificity

Transcripts of different sizes are differentially expressed in a subset of tissues. Detected in brain, lung, skeletal muscle, heart, kidney and placenta. In brain; expressed in olfactory bulb, cerebral cortex, hippocampus and cerebellum. Ref.1 Ref.2 Ref.7

Developmental stage

Expressed throughout embryonic development. First detected at E7. Ref.2

Post-translational modification

The extracellular domain is proteolytically processed through cleavage within the fibronectin type-III 4 domain. Beside the 190 kDa full-length protein, proteolytic products of 100 kDa, 80 kDa and 73 kDa are observed By similarity.

N-glycosylated By similarity.

Phosphorylated on tyrosine residues upon activation of KIT with stem cell factor (SCF). The 73 kDa proteolytic product is not phosphorylated By similarity.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 2B subfamily.

Contains 4 fibronectin type-III domains.

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Contains 1 MAM domain.

Contains 2 tyrosine-protein phosphatase domains.

Sequence caution

The sequence AAH80736.1 differs from that shown. Reason: Erroneous termination at position 618. Translated as Arg.

The sequence AAH80736.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAE43351.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
   Biological processCell adhesion
Differentiation
   Cellular componentCell junction
Cell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionHydrolase
Protein phosphatase
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcanonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

homotypic cell-cell adhesion

Inferred from direct assay Ref.2. Source: MGI

negative regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

organ regeneration

Inferred from electronic annotation. Source: Ensembl

protein localization to cell surface

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell-cell junction

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionbeta-catenin binding

Inferred from physical interaction Ref.2. Source: MGI

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: B1AUH1-1)

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: B1AUH1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     774-783: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 14461428Receptor-type tyrosine-protein phosphatase U
PRO_0000371659

Regions

Topological domain19 – 749731Extracellular Potential
Transmembrane750 – 77021Helical; Potential
Topological domain771 – 1446676Cytoplasmic Potential
Domain25 – 188164MAM
Domain190 – 27586Ig-like C2-type
Domain288 – 38396Fibronectin type-III 1
Domain386 – 48499Fibronectin type-III 2
Domain485 – 591107Fibronectin type-III 3
Domain592 – 66877Fibronectin type-III 4
Domain888 – 1144257Tyrosine-protein phosphatase 1
Domain1176 – 1439264Tyrosine-protein phosphatase 2
Region771 – 887117Mediates interaction with CTNNB1
Region1085 – 10917Substrate binding By similarity

Sites

Active site10851Phosphocysteine intermediate By similarity
Active site13801Phosphocysteine intermediate By similarity
Binding site10531Substrate Potential
Binding site11291Substrate By similarity

Amino acid modifications

Modified residue8481Phosphoserine By similarity
Modified residue8531Phosphoserine By similarity
Glycosylation751N-linked (GlcNAc...) Potential
Glycosylation4101N-linked (GlcNAc...) Potential
Glycosylation6851N-linked (GlcNAc...) Potential
Disulfide bond210 ↔ 264 Potential

Natural variations

Alternative sequence774 – 78310Missing in isoform 2.
VSP_037086

Experimental info

Sequence conflict801A → T in AAB17895. Ref.2
Sequence conflict1581Y → F in AAB17895. Ref.2
Sequence conflict2651V → A in AAH80736. Ref.6
Sequence conflict3871P → S in AAH80736. Ref.6
Sequence conflict5061K → R in AAH80736. Ref.6
Sequence conflict11581K → R in AAB17895. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: CBF639D8150D0D0B

FASTA1,446162,494
        10         20         30         40         50         60 
MARAQALVLA LTFQFCAPET ETPAAGCTFE EASDPVVPCE FSQAQYDDFQ WEQVRIHPGT 

        70         80         90        100        110        120 
RTPEDLPHGA YLMVNASQHA PGQRAHIIFQ TLSENDTHCV QFSYFLYSRD GHSPGTLGVY 

       130        140        150        160        170        180 
VRVNGGPLGS AVWNMTGSHG RQWHQAELAV STFWPNEYQV LFEALISPDH KGYIGLDDIL 

       190        200        210        220        230        240 
LFSYPCAKAP HFSRLGDVEV NAGQNASFQC MAAGRAAEAE HFFLQRQSGV LVPAAGVRHI 

       250        260        270        280        290        300 
SHRRFLATFP LASVGRSEQD LYRCVSQAPR GAGVSNFAEL IVKEPPTPIA PPQLLRAGPT 

       310        320        330        340        350        360 
YLIIQLNTNS IIGDGPIVRK EIEYRMARGP WAEVHAVNLQ TYKLWHLDPD TEYEISVLLT 

       370        380        390        400        410        420 
RPGDGGTGRP GPPLISRTKC AEPTRAPKGL AFAEIQARQL TLQWEPLGYN VTRCHTYAVS 

       430        440        450        460        470        480 
LCYRYTLGGS HNQTIRECVK MERGASRYTI KNLLPFRNIH VRLILTNPEG RKEGKEVTFQ 

       490        500        510        520        530        540 
TDEDVPGGIA AESLTFTPLE DMIFLKWEEP QEPNGLITQY EISYQSIESS DPAVNVPGPR 

       550        560        570        580        590        600 
RTISKLRNET YHVFSNLHPG TTYLFSVRAR TSKGFGQAAL TEITTNISAP SFDYADMPSP 

       610        620        630        640        650        660 
LGESENTITV LLRPAQGRGA PISVYQVVVE EERPRRLRRE PGAQDCFSVP LTFETALARG 

       670        680        690        700        710        720 
LVHYFGAELA ASSLLEAMPF TVGDNQTYRG FWNPPLEPRK AYLIYFQAAS HLKGETRLNC 

       730        740        750        760        770        780 
IRIARKAACK ESKRPLEVSQ RSEEMGLILG ICAGGLAVLI LLLGAIIVII RKGRDRYAYS 

       790        800        810        820        830        840 
YYPKPVNMTK ATVNYRQEKT HMMSAVDRSF TDQSTLQEDE RLGLSFMDAP GYSPRGDQRS 

       850        860        870        880        890        900 
GGVTEASSLL GGSPRRPCGR KGSPYHTGQL HPAVRVADLL QHINQMKTAE GYGFKQEYES 

       910        920        930        940        950        960 
FFEGWDATKK KDKLKGGRQE PVSAYDRHHV KLHPMLADPD ADYISANYID GYHRSNHFIA 

       970        980        990       1000       1010       1020 
TQGPKPEMIY DFWRMVWQEQ CASIVMITKL VEVGRVKCSR YWPEDSDMYG DIKITLVKTE 

      1030       1040       1050       1060       1070       1080 
TLAEYVVRTF ALERRGYSAR HEVRQFHFTA WPEHGVPYHA TGLLAFIRRV KASTPPDAGP 

      1090       1100       1110       1120       1130       1140 
IVIHCSAGTG RTGCYIVLDV MLDMAECEGV VDIYNCVKTL CSRRVNMIQT EEQYIFIHDA 

      1150       1160       1170       1180       1190       1200 
ILEACLCGET TIPVNEFKAT YREMIRIDPQ SNSSQLREEF QTLNSVTPPL DVEECSIALL 

      1210       1220       1230       1240       1250       1260 
PRNRDKNRSM DVLPPDRCLP FLISSDGDPN NYINAALTDS YTRSAAFIVT LHPLQSTTPD 

      1270       1280       1290       1300       1310       1320 
FWRLVYDYGC TSIVMLNQLN QSNSAWPCLQ YWPEPGRQQY GLMEVEFVSG TANEDLVSRV 

      1330       1340       1350       1360       1370       1380 
FRVQNSSRLQ EGHLLVRHFQ FLRWSAYRDT PDSRKAFLHL LAEVDKWQAE SGDGRTVVHC 

      1390       1400       1410       1420       1430       1440 
LNGGGRSGTF CACATVLEMI RCHSLVDVFF AAKTLRNYKP NMVETMDQYH FCYDVALEYL 


EALELR 

« Hide

Isoform 2 [UniParc].

Checksum: 8D406DE4948643FF
Show »

FASTA1,436161,158

References

« Hide 'large scale' references
[1]"Molecular cloning of a novel receptor-type protein tyrosine phosphatase from murine fetal liver."
Yoneya T., Yamada Y., Kakeda M., Osawa M., Arai E., Hayashi K., Nishi N., Inoue H., Nishikawa M.
Gene 194:241-247(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
Tissue: Fetal liver.
[2]"A novel protein-tyrosine phosphatase related to the homotypically adhering kappa and mu receptors."
Cheng J., Wu K., Armanini M., O'Rourke N., Dowbenko D., Lasky L.A.
J. Biol. Chem. 272:7264-7277(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), HOMOOLIGOMERIZATION, INTERACTION WITH CTNNB1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PROTEOLYTIC PROCESSING.
Tissue: Lung.
[3]"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. expand/collapse author list , 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.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1286 (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Kidney.
[6]"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 1-911 (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Embryo.
[7]"Genomic structure and alternative splicing of murine R2B receptor protein tyrosine phosphatases (PTPkappa, mu, rho and PCP-2)."
Besco J., Popesco M.C., Davuluri R.V., Frostholm A., Rotter A.
BMC Genomics 5:14-14(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D88187 mRNA. Translation: BAA23475.1.
U55057 mRNA. Translation: AAB17895.1.
AL670959 Genomic DNA. Translation: CAM27391.1.
AL670959 Genomic DNA. Translation: CAM27392.1.
CH466552 Genomic DNA. Translation: EDL30128.1.
AK052720 mRNA. Translation: BAE43351.1. Sequence problems.
BC080736 mRNA. Translation: AAH80736.1. Sequence problems.
CCDSCCDS18714.1. [B1AUH1-2]
CCDS38896.1. [B1AUH1-1]
RefSeqNP_001076588.1. NM_001083119.2. [B1AUH1-1]
NP_035344.2. NM_011214.2. [B1AUH1-2]
UniGeneMm.4860.

3D structure databases

ProteinModelPortalB1AUH1.
SMRB1AUH1. Positions 22-591, 871-1440.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEB1AUH1.

Protocols and materials databases

DNASU19273.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030741; ENSMUSP00000030741; ENSMUSG00000028909. [B1AUH1-1]
ENSMUST00000105987; ENSMUSP00000101607; ENSMUSG00000028909. [B1AUH1-2]
GeneID19273.
KEGGmmu:19273.
UCSCuc008vaa.1. mouse. [B1AUH1-1]
uc008vab.1. mouse. [B1AUH1-2]

Organism-specific databases

CTD10076.
MGIMGI:1321151. Ptpru.

Phylogenomic databases

eggNOGCOG5599.
GeneTreeENSGT00640000091300.
HOGENOMHOG000049029.
InParanoidQ66JV9.
KOK16662.
OMALTDSYTR.
OrthoDBEOG70KGNP.
PhylomeDBB1AUH1.
TreeFamTF312900.

Gene expression databases

ArrayExpressB1AUH1.
BgeeB1AUH1.
GenevestigatorB1AUH1.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
3.90.190.10. 2 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR000998. MAM_dom.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00041. fn3. 2 hits.
PF00629. MAM. 1 hit.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSPR00020. MAMDOMAIN.
PR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 3 hits.
SM00409. IG. 1 hit.
SM00137. MAM. 1 hit.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 2 hits.
SSF49899. SSF49899. 1 hit.
SSF52799. SSF52799. 2 hits.
PROSITEPS50853. FN3. 3 hits.
PS50060. MAM_2. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio296166.
PROB1AUH1.
SOURCESearch...

Entry information

Entry namePTPRU_MOUSE
AccessionPrimary (citable) accession number: B1AUH1
Secondary accession number(s): O35564 expand/collapse secondary AC list , P70125, Q3V312, Q66JV9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: April 8, 2008
Last modified: July 9, 2014
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot