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Database: UniProt
Entry: A0A3Q2VV35_HAPBU
LinkDB: A0A3Q2VV35_HAPBU
Original site: A0A3Q2VV35_HAPBU 
ID   A0A3Q2VV35_HAPBU        Unreviewed;      1169 AA.
AC   A0A3Q2VV35;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Tyrosine-protein phosphatase non-receptor type {ECO:0000256|PIRNR:PIRNR000934};
DE            EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000934};
GN   Name=PTPN21 {ECO:0000313|Ensembl:ENSHBUP00000015866.1};
OS   Haplochromis burtoni (Burton's mouthbrooder) (Chromis burtoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Haplochromis.
OX   NCBI_TaxID=8153 {ECO:0000313|Ensembl:ENSHBUP00000015866.1, ECO:0000313|Proteomes:UP000264840};
RN   [1] {ECO:0000313|Ensembl:ENSHBUP00000015866.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|PIRNR:PIRNR000934};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR000934}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649,
CC       ECO:0000256|PIRNR:PIRNR000934}.
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DR   AlphaFoldDB; A0A3Q2VV35; -.
DR   Ensembl; ENSHBUT00000033982.1; ENSHBUP00000015866.1; ENSHBUG00000017930.1.
DR   GeneTree; ENSGT00940000155613; -.
DR   OMA; TEWDYIA; -.
DR   Proteomes; UP000264840; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13188; FERM_C_PTPN14_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; 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, ECO:0000256|PIRNR:PIRNR000934};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW   ECO:0000256|PIRNR:PIRNR000934}; Hydrolase {ECO:0000256|PIRNR:PIRNR000934};
KW   Protein phosphatase {ECO:0000256|PIRNR:PIRNR000934};
KW   Reference proteome {ECO:0000313|Proteomes:UP000264840}.
FT   DOMAIN          23..305
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          893..1162
FT                   /note="Tyrosine-protein phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS50055"
FT   DOMAIN          1073..1153
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          312..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          394..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          668..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          727..758
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..842
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          857..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        394..425
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        727..742
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..821
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1103
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000934-1"
SQ   SEQUENCE   1169 AA;  133399 MW;  17D0C9FA79D64019 CRC64;
     MPLPFGLKLK RTRRYTVSSK SCLVTRIQLL NGEFVEFTLS VESTGQECLE AVAQRLELRE
     ITYFSLWYLN KQNQQRWIDL EKPLKKQLDK YGLEPTVYFG VVFYIPSVTQ LQQEITRYQY
     YLQLKKDVLE GRISCSLEQA IRLASLAVQA DFGDFNRYDS QEFLQKFELF PIDWIQDERV
     LEEAIQKVAL LYQGLPVPEA EMLYMQEVEK MEGYGQETFQ AKDNTGADVT LGSCLDGIFV
     KHKSERPLVL YRWHDINNMS HNRSFFALEL ANREESVQYQ TEDMETSKYV CRMCLARLKF
     YKINMSSLQP QPTVVNPVRR RSSTRVSLPK PQTYMMPPPQ MHYNGHFTEP YTSSQDNLYM
     NSQNGFYYHS QTSLDCSPLE YSSGGRLRNG SVYSAHSTSS LTNPQHYLQP SPMSSNPSIT
     SDITRPDYVP SHRHSALIPP SYRATPDYES VMRQKNRGAG GGMVLSQEHR QSHSMRNLNI
     GNSYAYSRPD PLVYSQPEIR GEHGGAAQHH HYPLHLGSSF HSPSPYPYPT ERRSVVGAVS
     VPELTNVQLQ QAQEYPAPNI MKTHVYRSPP PYPYAHPRPA NSTPDLSRHL YVSSSNPDLI
     ITRRVHHSVQ TFQEDSLPVA HSLQEVSEPL YSGPPQRQQY HAQKRNSIEI AGLAQSFEGI
     RVKERTASSS AAEMATPPPV LHGGRSQGSQ LNVFLEQKNP EDIEDIKEDV QYGHKKSLSD
     ATMLVHSSGE EEDFEDDSGR HTPLSQEPPP AYPIGSSLDP SITGTLTYKV HTLIHEREPL
     YLVSELQQPR IMPSVSEGDL SGQEKPRPKK DFKKRPVSDV PPGKKAVEGL PPAGMKKGAK
     SEVKKMGPLK VAHLNGLSIS RQPVHSEIKD EPERASNDER CKVLEQHMEK GEVLKEYESI
     PKRPRGEYTI AQLPESGDRN RFQDVLPYDD TRVELVPTKE NNTGYINASH IRVSLGGQEW
     NYIASQGPMS HTCQDFWQMV WEQGVSIIAM VTAEEESGRE KSFRYWPRLG SRHNTVTYGR
     FKITTRFRTE SGCYATTGLK IKHLLTQQER TVWHLQYTDW PDHGCPEDFK GFLTYLEEIQ
     SVRRHTNSIS DPKNSNQPVL VHCSAGVGRT GVVILSEIMI ACLEHNEPLD VPKHLLALRN
     QRMLMVQTLS QYTFVYRVLI QYLRNSRLI
//
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