PTN23_RAT
ID PTN23_RAT Reviewed; 1499 AA.
AC O88902; Q9QZP8;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 23;
DE EC=3.1.3.48;
DE AltName: Full=His domain-containing protein tyrosine phosphatase;
DE Short=HD-PTP;
DE AltName: Full=Protein tyrosine phosphatase TD14;
DE Short=PTP-TD14;
DE Flags: Fragment;
GN Name=Ptpn23;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF CYS-1255, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9694860; DOI=10.1074/jbc.273.33.21077;
RA Cao L., Zhang L., Ruiz-Lozano P., Yang Q., Chien K.R., Graham R.M.,
RA Zhou M.;
RT "A novel putative protein-tyrosine phosphatase contains a BRO1-like domain
RT and suppresses Ha-ras-mediated transformation.";
RL J. Biol. Chem. 273:21077-21083(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1248-1499.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RA Nicolas G., Galand C., Malbert-Colas L., Lecomte M.-C.;
RT "Corrections in cDNA sequence of the rat protein tyrosine phosphatase TD14
RT (PTP-TD14): identification of a base insertion and a base deletion in the
RT sequence database.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=11095967; DOI=10.1006/bbrc.2000.3870;
RA Toyooka S., Ouchida M., Jitsumori Y., Tsukuda K., Sakai A., Nakamura A.,
RA Shimizu N., Shimizu K.;
RT "HD-PTP: a novel protein tyrosine phosphatase gene on human chromosome
RT 3p21.3.";
RL Biochem. Biophys. Res. Commun. 278:671-678(2000).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Plays a role in sorting of endocytic ubiquitinated cargos
CC into multivesicular bodies (MVBs) via its interaction with the ESCRT-I
CC complex (endosomal sorting complex required for transport I), and
CC possibly also other ESCRT complexes. May act as a negative regulator of
CC Ras-mediated mitogenic activity. Plays a role in ciliogenesis (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:9694860}.
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBUNIT: Interacts with GRAP2 and GRB2. Interacts with UBAP1 and CHMP4B
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Cytoplasmic vesicle {ECO:0000269|PubMed:9694860}. Endosome
CC {ECO:0000250}. Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC brain, testis and kidney, and lowest levels in skeletal muscle.
CC {ECO:0000269|PubMed:11095967, ECO:0000269|PubMed:9694860}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC62959.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC62959.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF077000; AAC62959.1; ALT_SEQ; mRNA.
DR EMBL; AF175208; AAF13172.1; -; mRNA.
DR PIR; T14355; T14355.
DR AlphaFoldDB; O88902; -.
DR SMR; O88902; -.
DR STRING; 10116.ENSRNOP00000052992; -.
DR iPTMnet; O88902; -.
DR PhosphoSitePlus; O88902; -.
DR jPOST; O88902; -.
DR PaxDb; O88902; -.
DR PRIDE; O88902; -.
DR UCSC; RGD:619892; rat.
DR RGD; 619892; Ptpn23.
DR eggNOG; KOG0789; Eukaryota.
DR eggNOG; KOG2220; Eukaryota.
DR InParanoid; O88902; -.
DR PhylomeDB; O88902; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0036064; C:ciliary basal body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISO:RGD.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0045022; P:early endosome to late endosome transport; ISO:RGD.
DR GO; GO:0032456; P:endocytic recycling; ISO:RGD.
DR GO; GO:0010633; P:negative regulation of epithelial cell migration; ISO:RGD.
DR GO; GO:1903393; P:positive regulation of adherens junction organization; ISO:RGD.
DR GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; ISO:RGD.
DR GO; GO:1903387; P:positive regulation of homophilic cell adhesion; ISO:RGD.
DR GO; GO:0061357; P:positive regulation of Wnt protein secretion; ISO:RGD.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; ISS:UniProtKB.
DR Gene3D; 1.25.40.280; -; 1.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR025304; ALIX_V_dom.
DR InterPro; IPR045251; BRO1-like.
DR InterPro; IPR004328; BRO1_dom.
DR InterPro; IPR038499; BRO1_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR23030; PTHR23030; 1.
DR Pfam; PF13949; ALIX_LYPXL_bnd; 1.
DR Pfam; PF03097; BRO1; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM01041; BRO1; 1.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51180; BRO1; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endosome; Hydrolase;
KW Methylation; Nucleus; Phosphoprotein; Protein phosphatase;
KW Protein transport; Reference proteome; Repeat; TPR repeat; Transport.
FT CHAIN <1..1499
FT /note="Tyrosine-protein phosphatase non-receptor type 23"
FT /id="PRO_0000094779"
FT DOMAIN 1..219
FT /note="BRO1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00526"
FT REPEAT 75..108
FT /note="TPR 1"
FT REPEAT 199..232
FT /note="TPR 2"
FT REPEAT 788..789
FT /note="1"
FT REPEAT 790..791
FT /note="2"
FT REPEAT 792..793
FT /note="3"
FT REPEAT 794..795
FT /note="4"
FT REPEAT 796..797
FT /note="5"
FT REPEAT 798..799
FT /note="6"
FT REPEAT 800..801
FT /note="7"
FT REPEAT 802..803
FT /note="8"
FT REPEAT 804..805
FT /note="9"
FT REPEAT 806..807
FT /note="10"
FT REPEAT 808..809
FT /note="11"
FT REPEAT 810..811
FT /note="12"
FT REPEAT 812..813
FT /note="13"
FT REPEAT 814..815
FT /note="14"
FT REPEAT 816..817
FT /note="15"
FT REPEAT 818..819
FT /note="16"
FT REPEAT 820..821
FT /note="17"
FT REPEAT 822..823
FT /note="18"
FT REPEAT 824..825
FT /note="19"
FT REPEAT 826..827
FT /note="20"
FT DOMAIN 1055..1315
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 536..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..993
FT /note="His"
FT REGION 718..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 788..827
FT /note="20 X 2 AA approximate tandem repeats of P-Q"
FT REGION 1322..1351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1381..1499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 278..305
FT /evidence="ECO:0000255"
FT COILED 377..464
FT /evidence="ECO:0000255"
FT COILED 506..537
FT /evidence="ECO:0000255"
FT COMPBIAS 553..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..752
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..842
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..971
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1432
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1438..1477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1255
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000305"
FT MOD_RES 785
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3S7"
FT MOD_RES 985
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3S7"
FT MOD_RES 986
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3S7"
FT MOD_RES 994
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3S7"
FT MOD_RES 1478
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3S7"
FT MUTAGEN 1255
FT /note="C->S: Abolishes suppressive effect on Ha-ras induced
FT transformation."
FT /evidence="ECO:0000269|PubMed:9694860"
FT CONFLICT 1280
FT /note="R -> G (in Ref. 2; AAF13172)"
FT /evidence="ECO:0000305"
FT NON_TER 1
SQ SEQUENCE 1499 AA; 163454 MW; 9F9BF8C8DE517123 CRC64;
LNVNLMLGQA QECLLEKSML DNRKSFLVAR ISAQVVDYYK EACRALENPD TASLLGRIQK
DWKKLVQMKI YYFAAVAHLH MGKQAEEQQK FGERVAYFQS ALDKLNEAIK LAKGQPDTVQ
DALRFAMDVI GGKYNSAKKD NDFIYHEAVP ALDTLQPVKG APLVKPLPVN PTDPAVTGPD
IFAKLVPMAA HEASSLYSEE KAKLLREMLA KIEDKNEVLD QFMDSMQLDP DTVDNLDAYN
HIPPQLMEKC AALSVRPDTV KNLVQSMQVL SGVFTDVEAS LKDIRDLLEE DELQEQKLQE
TLGQAGAGPG PSVTKAELGE VRREWAKYTE VHEKASFTNS ELHRAMNLHV GNLRLLSGPL
DQVRAALPTP ALTPEDKAVL QNLKRILAKV QEMRDQRVSL EQQLRELIQK DDITASLVTT
DHSEMKKLFE EQLKKYDQLK VYLEQNLAAQ DNVLRALTEA NVQYAAVRRV LSELDQKWNS
TLQTLVASYE AYEDLMKKSQ EGKDFYADLE SKVAALLERA QSLCRAQEAA RQQLLDRELK
KKAPPPRPTA PKPLLSRREE GEAAEAGDQP EELRSLPPDM MAGPRLPDPF LGTAAPLHFS
PGPFPGSTGP ATHYLSGPLP PGTYSGPTQL MQPRAAVPMA PGPVLYPAPV YTSELGLVPR
SSPQHGIVSS PYAGVGPPQP IVGLPSAPPP QFSGPELAMD VRPATTTVDS VQAPISSHMA
LRPGPAPAPP QPCFPVPQPV PQSVPQPQPL PTPYTYSIGT KQHLTGPLPQ HHFPPGIPTS
FPAPRIGPQP PPQLQPQPQP QPQPQPPPQP QPQPQPQPQP QPQPQPQRPV FGPQPTQQPL
PFQHPHLFPS QAPGILTPPP PYPFTPQPGV LGQPPPTRHT QLYPGPPPDT LPPHSGALPF
PSPGPPHPHP TLAYGPAPSP RPLGPQATPV SIRGPPPANQ PAPSPHLVPS PAPSPGPGPV
PSRPPTAEPP PCLRRGAAAA DLLSSSPESQ HGGTQPPGGG QPLLQPTKVD AAERPTAQAL
RLIEQDPYEH PERLQKLQQE LESFRGQLGD AGALDAVWRE LQEAQEHDAR GRSIAIARCY
SLKNRHQDVM PYDSNRVVLR SGKDDYINAS CVEGLSPYCP PLVATQRPLP GTAADFWLMV
HEQKVSVIVM LVSEAEMEKQ KVARYFPIER GQPMVHGALS VALSSVRTTD THVERVLSLQ
FRDQSLKRSL VHLHFPTWPE LGLPDSPGNL LRFIQEVHAH YLHQRPLHTP IVVHCSSGVG
RTGAFALLYA AVQEVEAGSR IPELPQLVRR MRQQRKHMLQ EKLHLKFCHE ALVRHVEQVL
QRHGVPPPGK PVASMSVSQK SHLPQDSQDL VLGGDVPISS IQATIAKLSI RPLGGLDSPA
ASLPSLVEPP GLPPASLPEP TPAPPSSPPP PSSPLPEPPQ PEEEPSVPEA PSLGPPSSSL
ELLASLTPEA FSLDSSLRGK QRMSKQNFLQ AHNGQGLRAA QPTDDPLSLL DPLWTLNKT
