PTPRM_MOUSE
ID PTPRM_MOUSE Reviewed; 1452 AA.
AC P28828; E9QKU4; Q571L8;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Receptor-type tyrosine-protein phosphatase mu;
DE Short=Protein-tyrosine phosphatase mu;
DE Short=R-PTP-mu;
DE EC=3.1.3.48;
DE Flags: Precursor;
GN Name=Ptprm; Synonyms=Kiaa4044;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=1655529; DOI=10.1016/0014-5793(91)81241-y;
RA Gebbink M.F.B.G., van Etten I., Hateboer G., Suijkerbuijk R.,
RA Beijersbergen R., Geurts van Kessel A., Moolenaar W.H.;
RT "Cloning, expression and chromosomal localization of a new putative
RT receptor-like protein tyrosine phosphatase.";
RL FEBS Lett. 290:123-130(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-1452.
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Receptor protein-tyrosine phosphatase that mediates homotypic
CC cell-cell interactions and plays a role in adipogenic differentiation
CC via modulation of p120 catenin/CTNND1 phosphorylation. Promotes CTNND1
CC dephosphorylation and prevents its cytoplasmic localization where it
CC inhibits SLC2A4 membrane trafficking. In turn, SLC2A4 is directed to
CC the plasma membrane and performs its glucose transporter function.
CC {ECO:0000250|UniProtKB:P28827}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000250|UniProtKB:P28827};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P28827}.
CC -!- INTERACTION:
CC P28828; Q62470: Itga3; NbExp=3; IntAct=EBI-8539266, EBI-8398907;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P28827};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P28827}.
CC Note=Localizes in regions of cell-cell contact.
CC {ECO:0000250|UniProtKB:P28827}.
CC -!- TISSUE SPECIFICITY: Most abundant in lung, less in brain and heart.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC Receptor class 2B subfamily. {ECO:0000305}.
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DR EMBL; X58287; CAA41225.1; -; mRNA.
DR EMBL; AC109261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC139750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC163731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT030654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK220171; BAD90356.1; -; mRNA.
DR CCDS; CCDS28948.1; -.
DR PIR; S17670; S17670.
DR RefSeq; NP_033010.2; NM_008984.2.
DR AlphaFoldDB; P28828; -.
DR SMR; P28828; -.
DR BioGRID; 202502; 7.
DR IntAct; P28828; 4.
DR MINT; P28828; -.
DR STRING; 10090.ENSMUSP00000045603; -.
DR CarbonylDB; P28828; -.
DR GlyConnect; 2673; 1 N-Linked glycan (1 site).
DR GlyGen; P28828; 12 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P28828; -.
DR PhosphoSitePlus; P28828; -.
DR MaxQB; P28828; -.
DR PaxDb; P28828; -.
DR PeptideAtlas; P28828; -.
DR PRIDE; P28828; -.
DR ProteomicsDB; 301947; -.
DR Antibodypedia; 21926; 239 antibodies from 34 providers.
DR DNASU; 19274; -.
DR Ensembl; ENSMUST00000223982; ENSMUSP00000153662; ENSMUSG00000033278.
DR GeneID; 19274; -.
DR KEGG; mmu:19274; -.
DR UCSC; uc008dka.2; mouse.
DR CTD; 5797; -.
DR MGI; MGI:102694; Ptprm.
DR VEuPathDB; HostDB:ENSMUSG00000033278; -.
DR eggNOG; KOG4228; Eukaryota.
DR GeneTree; ENSGT00940000155020; -.
DR HOGENOM; CLU_001645_0_1_1; -.
DR InParanoid; P28828; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; P28828; -.
DR TreeFam; TF312900; -.
DR BioGRID-ORCS; 19274; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Ptprm; mouse.
DR PRO; PR:P28828; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P28828; protein.
DR Bgee; ENSMUSG00000033278; Expressed in left lung lobe and 263 other tissues.
DR ExpressionAtlas; P28828; baseline and differential.
DR Genevisible; P28828; MM.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:MGI.
DR GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0010596; P:negative regulation of endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0010842; P:retina layer formation; ISS:UniProtKB.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR GO; GO:0042311; P:vasodilation; IMP:MGI.
DR CDD; cd00063; FN3; 3.
DR CDD; cd06263; MAM; 1.
DR CDD; cd14633; R-PTPc-M-1; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 3.90.190.10; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR045911; R-PTP-mu_cat_rpt1.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF00629; MAM; 1.
DR Pfam; PF00102; Y_phosphatase; 2.
DR PRINTS; PR00020; MAMDOMAIN.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00060; FN3; 3.
DR SMART; SM00409; IG; 1.
DR SMART; SM00137; MAM; 1.
DR SMART; SM00194; PTPc; 2.
DR SMART; SM00404; PTPc_motif; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
DR PROSITE; PS50853; FN3; 3.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS00740; MAM_1; 1.
DR PROSITE; PS50060; MAM_2; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; Hydrolase;
KW Immunoglobulin domain; Membrane; Phosphoprotein; Protein phosphatase;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1452
FT /note="Receptor-type tyrosine-protein phosphatase mu"
FT /id="PRO_0000025449"
FT TOPO_DOM 21..742
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 743..764
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 765..1452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..184
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 186..277
FT /note="Ig-like C2-type"
FT DOMAIN 284..379
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 382..480
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 481..587
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 589..671
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 900..1154
FT /note="Tyrosine-protein phosphatase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT DOMAIN 1186..1448
FT /note="Tyrosine-protein phosphatase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT ACT_SITE 1095
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 1389
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 1063
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1095..1101
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 1139
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28827"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 406
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 598
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 27..36
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 96..182
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 206..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 1384
FT /note="R -> P (in Ref. 1; CAA41225)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1452 AA; 163653 MW; A1170FC67A41AF1D CRC64;
MRTLGTCLVT LAGLLLTAAG ETFSGGCLFD EPYSTCGYSQ ADEDDFNWEQ VNTLTKPTSD
PWMPSGSFML VNTSGKPEGQ RAHLLLPQLK ENDTHCIDFH YFVSSKSNAA PGLLNVYVKV
NNGPLGNPIW NISGDPTRTW HRAELAISTF WPNFYQVIFE VVTSGHQGYL AIDEVKVLGH
PCTRTPHFLR IQNVEVNAGQ FATFQCSAIG RTVAGDRLWL QGIDVRDAPL KEIKVTSSRR
FIASFNVVNT TKRDAGKYRC MICTEGGVGI SNYAELVVKE PPVPIAPPQL ASVGATYLWI
QLNANSINGD GPIVAREVEY CTASGSWNDR QPVDSTSYKI GHLDPDTEYE ISVLLTRPGE
GGTGSPGPAL RTRTKCADPM RGPRKLEVVE VKSRQITIRW EPFGYNVTRC HSYNLTVHYG
YQVGGQEQVR EEVSWDTDNS HPQHTITNLS PYTNVSVKLI LMNPEGRKES QELTVQTDED
LPGAVPTESI QGSAFEEKIF LQWREPTQTY GVITLYEITY KAVSSFDPEI DLSNQSGRVS
KLGNETHFLF FGLYPGTTYS FTIRASTAKG FGPPATNQFT TKISAPSMPA YEFETPLNQT
DNTVTVMLKP AQSRGAPVSV YQIVVEEERP RRTKKTTEIL KCYPVPIHFQ NASILNSQYY
FAAEFPADSL QAAQPFTIGD NKTYNGYWNT PLLPHKSYRI YYQAASRANG ETKIDCVRVA
TKGAVTPKPV PEPEKQTDHT VKIAGVIAGI LLFVIIFLGV VLVMKKRKLA KKRKETMSST
RQEMTVMVNS MDKSYAEQGT NCDEAFSFMG THNLNGRSVS SPSSFTMKTN TLSTSVPNSY
YPDETHTMAS DTSSLAQPHT YKKREAADVP YQTGQLHPAI RVADLLQHIT QMKCAEGYGF
KEEYESFFEG QSAPWDSAKK DENRMKNRYG NIIAYDHSRV RLQMLEGDNN SDYINGNYID
GYHRPNHYIA TQGPMQETIY DFWRMVWHEN TASIIMVTNL VEVGRVKCCK YWPDDTEIYK
DIKVTLIDTE LLAEYVIRTF AVEKRGIHEI REIRQFHFTG WPDHGVPYHA TGLLGFVRQV
KSKSPPNAGP LVVHCSAGAG RTGCFIVIDI MLDMAEREGV VDIYNCVREL RSRRVNMVQT
EEQYVFIHDA ILEACLCGDT SIPASQVRSL YYDMNKLDPQ TNSSQIKEEF RTLNMVTPTL
RVEDCSIALL PRNHEKNRCM DILPPDRCLP FLITIDGESS NYINAALMDS YKQPSAFIVT
QHPLPNTVKD FWRLVLDYHC TSVVMLNDVD PAQLCPQYWP ENGVHRHGPI QVEFVSADLE
EDIISRIFRI YNASRPQDGH RMVQQFQFLG WPMYRDTPVS KRSFLKLIRQ VDKWQEEYNG
GEGRTVVHCL NGGGRSGTFC AISIVCEMLR HQRTVDVFHA VKTLRNNKPN MVDLLDQYKF
CYEVALEYLN SG
