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   27-MAR-2024, entry version 193.
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.ENSMUSP00000153662; -.
DR   CarbonylDB; P28828; -.
DR   GlyConnect; 2673; 1 N-Linked glycan (1 site).
DR   GlyCosmos; P28828; 12 sites, 1 glycan.
DR   GlyGen; P28828; 12 sites, 1 N-linked glycan (1 site).
DR   iPTMnet; P28828; -.
DR   PhosphoSitePlus; P28828; -.
DR   MaxQB; P28828; -.
DR   PaxDb; 10090-ENSMUSP00000045603; -.
DR   PeptideAtlas; P28828; -.
DR   ProteomicsDB; 301947; -.
DR   Pumba; P28828; -.
DR   Antibodypedia; 21926; 259 antibodies from 34 providers.
DR   DNASU; 19274; -.
DR   Ensembl; ENSMUST00000223982.2; ENSMUSP00000153662.2; ENSMUSG00000033278.11.
DR   GeneID; 19274; -.
DR   KEGG; mmu:19274; -.
DR   UCSC; uc008dka.2; mouse.
DR   AGR; MGI:102694; -.
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   OMA; XPMQETI; -.
DR   OrthoDB; 2875525at2759; -.
DR   PhylomeDB; P28828; -.
DR   TreeFam; TF312900; -.
DR   BioGRID-ORCS; 19274; 1 hit in 77 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 264 other cell types or tissues.
DR   ExpressionAtlas; P28828; baseline and differential.
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:0043232; C:intracellular non-membrane-bounded organelle; ISO:MGI.
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:0016791; F:phosphatase activity; 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   CDD; cd14635; R-PTPc-M-2; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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   PANTHER; PTHR24051:SF12; PROTEIN TYROSINE PHOSPHATASE, RECEPTOR TYPE, M; 1.
DR   PANTHER; PTHR24051; SUSHI DOMAIN-CONTAINING PROTEIN 1; 1.
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; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
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.
DR   Genevisible; P28828; MM.
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
//