ID A0A3Q2LL24_HORSE Unreviewed; 1202 AA.
AC A0A3Q2LL24;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 2.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN Name=MTMR4 {ECO:0000313|Ensembl:ENSECAP00000042291.2,
GN ECO:0000313|VGNC:VGNC:20427};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000042291.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000042291.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000042291.2,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000042291.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000042291.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1-D-myo-inositol-3-
CC phosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:42328, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:65221, ChEBI:CHEBI:78934;
CC Evidence={ECO:0000256|ARBA:ARBA00023732};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-
CC phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol) + phosphate; Xref=Rhea:RHEA:12316, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57880, ChEBI:CHEBI:58088; EC=3.1.3.64;
CC Evidence={ECO:0000256|ARBA:ARBA00001291};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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DR AlphaFoldDB; A0A3Q2LL24; -.
DR Ensembl; ENSECAT00000034463.3; ENSECAP00000042291.2; ENSECAG00000018106.4.
DR VGNC; VGNC:20427; MTMR4.
DR GeneTree; ENSGT00940000158976; -.
DR Proteomes; UP000002281; Chromosome 11.
DR Bgee; ENSECAG00000018106; Expressed in cerebellum and 24 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphate phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR CDD; cd15733; FYVE_MTMR4; 1.
DR CDD; cd14587; PTP-MTMR4; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR046978; MTMR4_FYVE.
DR InterPro; IPR030590; MTMR4_PTP.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF64; MYOTUBULARIN-RELATED PROTEIN 4; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00064; FYVE; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00091}.
FT DOMAIN 159..576
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 382..426
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 1121..1181
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT REGION 832..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..873
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 413
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 326..329
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 351..352
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
FT BINDING 413..419
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1202 AA; 134265 MW; 75325F5A09B2F84A CRC64;
MGEEGPPSLE YIQAKDLFPP KELVKEEENL QVPFTVLQGE GVEFLGRATD ALIAISNYRL
HIKFKDSVIN FALPLKVPLR MIDSVESRDM FQLHIACKDS KVVRCHFSTF KQCQEWLSRL
SRATARPAKP EDLFAFAYHA WCLGLTEEDQ HTHLCQPGEH IRCRQEAELV RMGFDLQNVW
RVSHINSNYK LCPSYPQKLL VPVWITDKEL ENVASFRSWK RIPVVVYRHL RNGAAIARCS
QPEISWWGWR NADDEYLVTS IAKACALDPG TRATGGSLST GNSDASEACD TDFDSSLTAC
SGVESTAAPQ KLLILDARSY TAAVANRAKG GGCECEEYYP NCEVVFMGMA NIHAIRNSFQ
YLRAVCSQMP DPSNWLSALE STKWLQHLSV MLKAAVLVAN TVDREGRPVL VHCSDGWDRT
PQIVALAKIL LDPYYRTLEG FQVLVESDWL DFGHKFGDRC GHQENAEDQN EQCPVFLQWL
DSVHQLLKQF PCLFEFNEAF LVKLVQHTYS CLYGTFLANN PCEREKRNIY KRTCSVWALL
RAGNKNFHNF LYTPGSDMVL HPVCHVRALH LWTAVYLPAS SPCTLGEENM DLYLSPVAQS
QEFSGRSLER LPKTRSMDDL LSACDTSSPL TRTSSDPNLN NHCQEARVGL EPWHSNPEGS
EATFVESGVG GPQQPVAEMS LLPPLPSSQK DYLNSKPFKS HKSCSPSYKL LNTAVPQKMK
SNTSDPGIKV LEETKAPAPD LCAQNELGRT LDGTEEPPEH CPEREAVGAL SKVISSKCDG
ICDFPESFRD SLTGTPQQAH LDSVLGVPSR CAPNHSLGTL CDPPSTTCQT PLDPSTDFLS
QDSPGSVASI SHQEKPSSVP DLIHGEEDTG KRGNNRNGQL LENPRFGKVP LELARKPISQ
SQISEYSFLG SNWDSFQGMV TSFPSGETTP RRLLSYGCCS KRSSSKQMRA VGPCFGGQWA
QREGVKSPVC SSHSNGHCTG PGGKNNRMWL SGHPKQVSNT KPVPLSCPSP VPPLYLDDDG
LPFPTDVIQH RLRQIEAGYK QEVEQLRRQV RELQMRLDIR HCCAPPAEPP MDYEDDFTCL
KESDGSDTED FGSDHSEDCL SEASWEPVDK KETEVTRWVP DHMASHCYNC DCEFWLAKRR
HHCRNCGNVF CATCCHLKLP IPDQQLYDPV LVCNSCYEHI QVSRARELMS QHLKKPIATA
SS
//
