ID L5MA98_MYODS Unreviewed; 1405 AA.
AC L5MA98;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Tensin-like C1 domain-containing phosphatase {ECO:0000313|EMBL:ELK35306.1};
GN ORFNames=MDA_GLEAN10015465 {ECO:0000313|EMBL:ELK35306.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK35306.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000256|ARBA:ARBA00007881}.
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DR EMBL; KB102468; ELK35306.1; -; Genomic_DNA.
DR eggNOG; KOG1930; Eukaryota.
DR eggNOG; KOG2283; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR CDD; cd20887; C1_TNS2; 1.
DR CDD; cd01213; PTB_tensin; 1.
DR CDD; cd09927; SH2_Tensin_like; 1.
DR Gene3D; 2.60.40.1110; -; 1.
DR Gene3D; 3.30.60.20; -; 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 Gene3D; 3.30.505.10; SH2 domain; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR013625; PTB.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR035012; Tensin-like_SH2.
DR InterPro; IPR014020; Tensin_C2-dom.
DR InterPro; IPR029023; Tensin_phosphatase.
DR InterPro; IPR033929; Tensin_PTB.
DR PANTHER; PTHR45734; TENSIN; 1.
DR PANTHER; PTHR45734:SF1; TENSIN-2; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF10409; PTEN_C2; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM01326; PTEN_C2; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF55550; SH2 domain; 1.
DR PROSITE; PS51182; C2_TENSIN; 1.
DR PROSITE; PS51181; PPASE_TENSIN; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 31..79
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 122..294
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 299..425
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1136..1243
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..918
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..976
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1051
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1089
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1405 AA; 152608 MW; E63EF1E8169BCA15 CRC64;
MKSSGPVERL LRALGRRDSS RATSRPRKAE PHSFREKIFR KKPPVCAVCK VTIDGTGVSC
RVCKVATHRK CEAKVTSSCQ ALPPAELRRS TAPVRRIEHL GSTKSLNHSK QRSTLPRSFS
LDPLMERRWD LDLTYVTERI LAAAFPARPD EERHRSHLRE LAHVLQSKHR DKYLFFNLSE
KRHDLTRLNP KVQDFGWPEL HAPPLDKLCS ICKAMETWLS ADPQHVVVLY CKGSKSKLGV
IVSAYMHYSK ISAGADQALA TLTMRKFCED KVAAELQPSQ RRYINYFSGL LSGSIRMNSS
PLFLHYVLVP VLPAFEPGTG FQPFLKIYQS MQLVYTSGIY HIAGPGPQQL CISLEPALLL
KGDVMVTCYH KGGRGTDRTL VFRVQFHTCT IHGPRLTFPK DQLDEAWTDE RFPFQASVEF
IFSSSPEKIK GNIPRNDPTV TVDYNTAEPA VRWDSYENFN QHHEDSSLTH TRGPLDGSPY
AQVQRAPRQT PPAPSPELPP APLLSISSDS GHSSTLTTEP AAESPGRPPP TAAERQELDR
LLGGCGVAGG GRGAGRETAI LDDEEQPPTS GGAHIGTYSG HRPPLSRHCS CRQGYREPFG
VPNGGYYQPE GTLERRRLAY GYEGPAQGYA EASVEKRRLC RSLSEGPYPY PPELGKPASG
DFGYRSPGYR EVVILEEPGL PALCSCPACQ EKLALPTTAL YGLRLEREAG EGWASDASKP
LLHPVRPGHP LPLLVPACGH HHAPIPDYSC LKPPKAGEEG HEGCPYPMCP EGRYGHPGYP
ALVTYGYGGA VPSYCPAYGR VPHSCGSAGE GRGYPNPGAH SPRAGSISPG SPPYPPSRKL
SYEIPAEEGG DRYPLPSHLA PAGPLTSAES PEPASWREGP SRHSTLPRSP RDAPCSTSSE
MSGPSTPLHT SSPVQGKEST RRQDTRSPPL APTQRLSPGE ALLPVSQGGA EKPPELPARS
GLEPPAPSPL SPTSTPSSPN DWPQERSPGG RSDSGSPRGP VPTTLPGLRH APWQGLREPP
DSPDGSPLTP VPTQMPWLVA SPEPPQSSPT PAFPVAASYD LNGPTQPPLP EKRHLPGPGQ
QPGPWGPEQA SPPARGTSHH VTFAPQLPDN TPQPPEPPLQ ESQSNVKFVQ DTSKFWYKPH
LSRDQAIALL KDKDPGAFLI RDSHSFQGAY GLALKVATPP PSAQPWKGDP LEQLVRHFLI
ETGPKGVKIK GCPSEPYFGS LSALVSQHSI SPLSLPCCLR IPSKDPLEET PEIPVPANMS
TAADLLRQGA ACSVLYLTSV ETESLTGPQA VARASSAALG CSPRPTPAVV HFKVSAQGIT
LTDNQRKLFF RRHYPVNSIT FSSTDPQDRR WTNPDGTTSK IFGFVAKKPG SPWENVCHLF
AELDPDQPAG AIVTFITKVL LGQRK
//
