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Database: UniProt
Entry: A0A3Q3H1N1_9LABR
LinkDB: A0A3Q3H1N1_9LABR
Original site: A0A3Q3H1N1_9LABR 
ID   A0A3Q3H1N1_9LABR        Unreviewed;      1204 AA.
AC   A0A3Q3H1N1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE            EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN   Name=PTPN21 {ECO:0000313|Ensembl:ENSLBEP00000037944.1};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000037944.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000037944.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649}.
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DR   AlphaFoldDB; A0A3Q3H1N1; -.
DR   Ensembl; ENSLBET00000039508.1; ENSLBEP00000037944.1; ENSLBEG00000028296.1.
DR   GeneTree; ENSGT00940000155613; -.
DR   OrthoDB; 3108587at2759; -.
DR   Proteomes; UP000261660; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13188; FERM_C_PTPN14_PTPN21; 1.
DR   CDD; cd17192; FERM_F1_PTPN21; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR   InterPro; IPR035963; FERM_2.
DR   InterPro; IPR019748; FERM_central.
DR   InterPro; IPR019747; FERM_CS.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018979; FERM_N.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR014392; PTP_non-rcpt_14/21.
DR   InterPro; IPR041782; PTPN14/21_FERM_C.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR45706; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR   PANTHER; PTHR45706:SF3; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 21; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF00102; Y_phosphatase; 1.
DR   PIRSF; PIRSF000934; Tyr-Ptase_nr14; 1.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SMART; SM00194; PTPc; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261660}.
FT   DOMAIN          23..308
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          927..1197
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1108..1188
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          397..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          667..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          700..719
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          757..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          828..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          889..912
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..428
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..692
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..717
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..779
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        837..855
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        897..912
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1138
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000934-1"
SQ   SEQUENCE   1204 AA;  137118 MW;  01F2E83FD6E3B46E CRC64;
     MPLPFGFKLK RTRRYTVSSK SCLVTRIQLL NGEFVEFTLS VESTGQECLE AVAQRLELRE
     ITFFSLWYFN KQNQQRWIDL EKPLKKQLDK YGLEPTVYFG VVFYIPSVNQ LQQEITRYQY
     YLQLKKDVLE GRISCSLEQA VRLASLAVQA DFGDFNRYDS QEFLQKFVLF PIDWIQDERV
     LEEATQKVAL LYQSFRGLSA PEAEMLYMQE VEKMEGYGQE SYQAKDSTGT DVTLGSCLEG
     IFVKHKNGRP LLLFRWNEIN NMSHNRSFFA LELTNREESV QFQTEDMETS KYVCRMCLAR
     LKFYKINKSS LQSQATVVNP VRRRSSTRLS LPKPQGYMMP PPQMHYNGHF TEPYTSSQDN
     LYMNNQNGYY YHSQTSLDCP PLEYSSGGRL RNGSVYSAHS TSSLTNPQHY LQPSPMSSNP
     SITSDITRPD YIPSHRHSAL IPPSYRATPD YETVMRQKTR GPGGGMVLSQ EHRQSHSMRN
     LNIGNSYAYS RPDPLVYSQP EIRGEHGGAA QHLHYPFHLG SSFHSPSPYP YPTERRPVVG
     AVSVPELTNV QLQQAQEYPA PNIMRTQVYR PPPPYPYAHP RPANSTPDLS RHLYVSSSNP
     DLIITRRVHH SVQTFQEDSL PVAHSLQEVS EPLFSGPPQR HPYHAQKRNS IEIAGLAQSL
     EGMRVKERTL SSSAAESATP PPVLHSRQSQ GSQLDVFLER TKKEDRGGNK EGVQYGHKKS
     LSDATMLVHS SGEEEEFEED SGRHTPLSQD AAVTLPEQPT QPHHSLTSLS SLKNQQQTPI
     EPPPAYPIGS SLDPAVTSSL AYKVHPLIQE NEPLYLLSDL RQPRIMPSVS EGDLSGQAKQ
     KTKKDFKKRP VSDVPAGKKT VEGLPPPGMR KGARSEVKKM GPLKVAHLNG LSVSRQPMHD
     EIKDEPERAS NDERCKALEQ HMERGELLKE YESIPKRRPS GECNIALQPE SGDKNRFQDV
     MPYDDTRVEL VPTKENNTGY INASHVRITV SGQEWSYIAT QGPMSNTCQD FWQMVWEQGV
     SIIAMVTAEE ESGREKSFRY WPRLGSRHNT VTYGRFKITT RFRTESGCYA TTGLKIKHLL
     TGQERTVWHL QYTDWPDHGC PEDFKGFLTY LEEIQSVRRH TNSISDPKNT NLPVLVHCSA
     GVGRTGVVIL SEIMIACLEH NEALDVPKFL SRLRAQRMMM VQTLSQYTFI YKVIIEYLRN
     SRLI
//
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