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   27-MAR-2024, entry version 145.
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   GlyGen; O88902; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O88902; -.
DR   PhosphoSitePlus; O88902; -.
DR   jPOST; O88902; -.
DR   PaxDb; 10116-ENSRNOP00000052992; -.
DR   UCSC; RGD:619892; rat.
DR   AGR; RGD:619892; -.
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:0016311; P:dephosphorylation; IEA:InterPro.
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: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   CDD; cd14539; PTP-N23; 1.
DR   CDD; cd09234; V_HD-PTP_like; 1.
DR   Gene3D; 1.20.120.560; alix/aip1 in complex with the ypdl late domain; 1.
DR   Gene3D; 1.20.140.50; alix/aip1 like domains; 1.
DR   Gene3D; 1.25.40.280; alix/aip1 like domains; 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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; PCD6 INTERACTING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR23030:SF30; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 23; 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; (Phosphotyrosine protein) phosphatases II; 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
//