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P28828 (PTPRM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=Protein-tyrosine phosphatase mu
Short name=R-PTP-mu
EC=3.1.3.48
Gene names
Name:Ptprm
Synonyms:Kiaa4044
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1452 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in cell-cell adhesion through homophilic interactions. May play a key role in signal transduction and growth control.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

Most abundant in lung, less in brain and heart.

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.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentMembrane
   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_processhomophilic cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of endothelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of endothelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of vasodilation

Inferred from mutant phenotype PubMed 15706045. Source: MGI

protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from sequence or structural similarity. Source: UniProtKB

retina layer formation

Inferred from sequence or structural similarity. Source: UniProtKB

retinal ganglion cell axon guidance

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcell-cell adherens junction

Inferred from sequence or structural similarity. Source: UniProtKB

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioncadherin binding

Inferred from sequence or structural similarity. Source: UniProtKB

transmembrane receptor protein tyrosine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 14521432Receptor-type tyrosine-protein phosphatase mu
PRO_0000025449

Regions

Topological domain21 – 742722Extracellular Potential
Transmembrane743 – 76422Helical; Potential
Topological domain765 – 1452688Cytoplasmic Potential
Domain22 – 184163MAM
Domain186 – 27792Ig-like C2-type
Domain284 – 37996Fibronectin type-III 1
Domain382 – 48099Fibronectin type-III 2
Domain481 – 587107Fibronectin type-III 3
Domain589 – 67183Fibronectin type-III 4
Domain900 – 1154255Tyrosine-protein phosphatase 1
Domain1186 – 1448263Tyrosine-protein phosphatase 2
Region1095 – 11017Substrate binding By similarity

Sites

Active site10951Phosphocysteine intermediate By similarity
Active site13891Phosphocysteine intermediate By similarity
Binding site10631Substrate By similarity
Binding site11391Substrate By similarity

Amino acid modifications

Modified residue8211Phosphoserine By similarity
Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation921N-linked (GlcNAc...) Potential
Glycosylation1311N-linked (GlcNAc...) Potential
Glycosylation2491N-linked (GlcNAc...) Potential
Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation4141N-linked (GlcNAc...) Potential
Glycosylation4541N-linked (GlcNAc...) Potential
Glycosylation5341N-linked (GlcNAc...) Potential
Glycosylation5441N-linked (GlcNAc...) Potential
Glycosylation5981N-linked (GlcNAc...) Potential
Glycosylation6511N-linked (GlcNAc...) Potential
Glycosylation6811N-linked (GlcNAc...) Potential
Disulfide bond27 ↔ 36 By similarity
Disulfide bond96 ↔ 182 By similarity
Disulfide bond206 ↔ 260 By similarity

Experimental info

Sequence conflict13841R → P in CAA41225. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P28828 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: A1170FC67A41AF1D

FASTA1,452163,653
        10         20         30         40         50         60 
MRTLGTCLVT LAGLLLTAAG ETFSGGCLFD EPYSTCGYSQ ADEDDFNWEQ VNTLTKPTSD 

        70         80         90        100        110        120 
PWMPSGSFML VNTSGKPEGQ RAHLLLPQLK ENDTHCIDFH YFVSSKSNAA PGLLNVYVKV 

       130        140        150        160        170        180 
NNGPLGNPIW NISGDPTRTW HRAELAISTF WPNFYQVIFE VVTSGHQGYL AIDEVKVLGH 

       190        200        210        220        230        240 
PCTRTPHFLR IQNVEVNAGQ FATFQCSAIG RTVAGDRLWL QGIDVRDAPL KEIKVTSSRR 

       250        260        270        280        290        300 
FIASFNVVNT TKRDAGKYRC MICTEGGVGI SNYAELVVKE PPVPIAPPQL ASVGATYLWI 

       310        320        330        340        350        360 
QLNANSINGD GPIVAREVEY CTASGSWNDR QPVDSTSYKI GHLDPDTEYE ISVLLTRPGE 

       370        380        390        400        410        420 
GGTGSPGPAL RTRTKCADPM RGPRKLEVVE VKSRQITIRW EPFGYNVTRC HSYNLTVHYG 

       430        440        450        460        470        480 
YQVGGQEQVR EEVSWDTDNS HPQHTITNLS PYTNVSVKLI LMNPEGRKES QELTVQTDED 

       490        500        510        520        530        540 
LPGAVPTESI QGSAFEEKIF LQWREPTQTY GVITLYEITY KAVSSFDPEI DLSNQSGRVS 

       550        560        570        580        590        600 
KLGNETHFLF FGLYPGTTYS FTIRASTAKG FGPPATNQFT TKISAPSMPA YEFETPLNQT 

       610        620        630        640        650        660 
DNTVTVMLKP AQSRGAPVSV YQIVVEEERP RRTKKTTEIL KCYPVPIHFQ NASILNSQYY 

       670        680        690        700        710        720 
FAAEFPADSL QAAQPFTIGD NKTYNGYWNT PLLPHKSYRI YYQAASRANG ETKIDCVRVA 

       730        740        750        760        770        780 
TKGAVTPKPV PEPEKQTDHT VKIAGVIAGI LLFVIIFLGV VLVMKKRKLA KKRKETMSST 

       790        800        810        820        830        840 
RQEMTVMVNS MDKSYAEQGT NCDEAFSFMG THNLNGRSVS SPSSFTMKTN TLSTSVPNSY 

       850        860        870        880        890        900 
YPDETHTMAS DTSSLAQPHT YKKREAADVP YQTGQLHPAI RVADLLQHIT QMKCAEGYGF 

       910        920        930        940        950        960 
KEEYESFFEG QSAPWDSAKK DENRMKNRYG NIIAYDHSRV RLQMLEGDNN SDYINGNYID 

       970        980        990       1000       1010       1020 
GYHRPNHYIA TQGPMQETIY DFWRMVWHEN TASIIMVTNL VEVGRVKCCK YWPDDTEIYK 

      1030       1040       1050       1060       1070       1080 
DIKVTLIDTE LLAEYVIRTF AVEKRGIHEI REIRQFHFTG WPDHGVPYHA TGLLGFVRQV 

      1090       1100       1110       1120       1130       1140 
KSKSPPNAGP LVVHCSAGAG RTGCFIVIDI MLDMAEREGV VDIYNCVREL RSRRVNMVQT 

      1150       1160       1170       1180       1190       1200 
EEQYVFIHDA ILEACLCGDT SIPASQVRSL YYDMNKLDPQ TNSSQIKEEF RTLNMVTPTL 

      1210       1220       1230       1240       1250       1260 
RVEDCSIALL PRNHEKNRCM DILPPDRCLP FLITIDGESS NYINAALMDS YKQPSAFIVT 

      1270       1280       1290       1300       1310       1320 
QHPLPNTVKD FWRLVLDYHC TSVVMLNDVD PAQLCPQYWP ENGVHRHGPI QVEFVSADLE 

      1330       1340       1350       1360       1370       1380 
EDIISRIFRI YNASRPQDGH RMVQQFQFLG WPMYRDTPVS KRSFLKLIRQ VDKWQEEYNG 

      1390       1400       1410       1420       1430       1440 
GEGRTVVHCL NGGGRSGTFC AISIVCEMLR HQRTVDVFHA VKTLRNNKPN MVDLLDQYKF 

      1450 
CYEVALEYLN SG 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, expression and chromosomal localization of a new putative receptor-like protein tyrosine phosphatase."
Gebbink M.F.B.G., van Etten I., Hateboer G., Suijkerbuijk R., Beijersbergen R., Geurts van Kessel A., Moolenaar W.H.
FEBS Lett. 290:123-130(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
[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. 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.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-1452.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58287 mRNA. Translation: CAA41225.1.
AC109261 Genomic DNA. No translation available.
AC139750 Genomic DNA. No translation available.
AC154596 Genomic DNA. No translation available.
AC163731 Genomic DNA. No translation available.
CT030654 Genomic DNA. No translation available.
AK220171 mRNA. Translation: BAD90356.1.
PIRS17670.
RefSeqNP_033010.2. NM_008984.2.
UniGeneMm.311809.

3D structure databases

ProteinModelPortalP28828.
SMRP28828. Positions 22-588, 877-1451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP28828. 1 interaction.
MINTMINT-129906.

PTM databases

PhosphoSiteP28828.

Proteomic databases

PaxDbP28828.
PRIDEP28828.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000037974; ENSMUSP00000045603; ENSMUSG00000033278.
GeneID19274.
KEGGmmu:19274.
UCSCuc008dka.2. mouse.

Organism-specific databases

CTD5797.
MGIMGI:102694. Ptprm.
RougeSearch...

Phylogenomic databases

eggNOGCOG5599.
GeneTreeENSGT00640000091300.
HOGENOMHOG000049029.
HOVERGENHBG062785.
KOK05693.
OMAHKSYRIY.
OrthoDBEOG70KGNP.
TreeFamTF312900.

Gene expression databases

ArrayExpressP28828.
BgeeP28828.
CleanExMM_PTPRM.
GenevestigatorP28828.

Family and domain databases

Gene3D2.60.40.10. 4 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013151. Immunoglobulin.
IPR000998. MAM_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00041. fn3. 2 hits.
PF00047. ig. 1 hit.
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.
PROSITEPS50853. FN3. 3 hits.
PS50835. IG_LIKE. 1 hit.
PS00740. MAM_1. 1 hit.
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

NextBio296172.
PROP28828.
SOURCESearch...

Entry information

Entry namePTPRM_MOUSE
AccessionPrimary (citable) accession number: P28828
Secondary accession number(s): E9QKU4, Q571L8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 133 of the entry and version 2 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