ID A0A151PHB4_ALLMI Unreviewed; 939 AA.
AC A0A151PHB4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Tyrosine-protein phosphatase {ECO:0000256|PIRNR:PIRNR000927};
DE EC=3.1.3.48 {ECO:0000256|PIRNR:PIRNR000927};
GN ORFNames=Y1Q_0022680 {ECO:0000313|EMBL:KYO48491.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO48491.1};
RN [1] {ECO:0000313|EMBL:KYO48491.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO48491.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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:PIRNR000927};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR000927}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class subfamily. {ECO:0000256|ARBA:ARBA00009649,
CC ECO:0000256|PIRNR:PIRNR000927}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO48491.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKHW03000190; KYO48491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151PHB4; -.
DR STRING; 8496.A0A151PHB4; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
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; cd13189; FERM_C_PTPN4_PTPN3_like; 1.
DR CDD; cd17193; FERM_F1_PTPN3; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd14600; PTPc-N3; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.42.10; -; 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; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR041783; PTPN3/4_FERM_C.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR012151; Tyr_Pase_non-rcpt_typ-3/4.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR45706; TYROSINE-PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR45706:SF5; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 3; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000927; Tyr-Ptase_nr3; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 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; PS50106; PDZ; 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:PIRNR000927};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212,
KW ECO:0000256|PIRNR:PIRNR000927}; Hydrolase {ECO:0000256|PIRNR:PIRNR000927};
KW Protein phosphatase {ECO:0000256|PIRNR:PIRNR000927};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525}.
FT DOMAIN 43..326
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT DOMAIN 535..607
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 672..927
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS50055"
FT DOMAIN 845..918
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 374..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 868
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000927-1"
FT BINDING 837
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
FT BINDING 868..874
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
FT BINDING 912
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000927-2"
SQ SEQUENCE 939 AA; 107459 MW; D45BC9669A25BA47 CRC64;
MIDMLQPTGY SEIVMNSRLR ALSGRINNVR SSELPKEKTR SEIICNVHFL DGSIQSFKVN
KQDTGQILLD MAYNHLGVTE KEYFGLQQNE EAVDSPRWLE MSKPIKKQLK GGFPCTLHFR
VRFFIPDPNT LQEEKTRHLF FLQLKTAILE GRLTCPLNSA VVLASYAVQA QLGDFNSTEH
HSGYLSNFYF LPDQNKDFLI KVESLHEQHS GLKQSEAESC YINIARTLEF YGVELHSGRD
LHNLDLMIGI ASGGIAVYRK FICTSFYPWA NILKISFKRK KFFIQQRQKH NETREHIVAF
NMLNYRACKN LWKSCVEHHT FFQAKSLPHE NKIFSHYWTL GSRNLTKSVN NQYCRKVIGG
MVWNPSMRRS LSVEHLETKS LPSRSPPVTP NWRSPRLRHE IRKPRHSSVD NLTNEITYIT
ETEDVFYTYK VSPTSKDSDS EVSQNRSPRR RSPEQESSKN ILGNSPSQSC LTHTSPNTST
QSPSGVGNTS GSYPLDGADQ QFSETYDNVT KGSTSEDSSQ YYCDRNEVID GDLLSVHITP
DEDGKFGFNL KGGVDQKMPL VVSRITPGSP ADKCIPKLNE GDQIVLINGR DISEHTHDQV
VMFIKASRES HTRELALLVK RKVVKHFVET KSEDEADSQN FQESILSTCS EYGDTLEESM
EQLKKGLENG TVLTQFEQLY RKKPGLAVTC AKVPQNMDKN RYKDVLPYDA TRIILQGDED
YINANYVTME IPSAGIVNRY IATQGPLPHT CAHFWQVVWD HRLTLIIMLT TLTERGRTKC
HQYWPDPPEI MEYGNFRVKC QSEDCTIAYV FREMVLTNIE TEQEHIVTHL QYVAWPDHGV
PDDSTDFLEF VNCMRPKRVK NEPVLVHCSA GIGRTGVLVT METALCLIER NQPVYPLDIV
RKMRDQRAMM VQTSSQYKFV CEAILRVYKE GLVRPLDSS
//
