ID W8B070_CERCA Unreviewed; 1838 AA.
AC W8B070;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 08-NOV-2023, entry version 48.
DE SubName: Full=Myotubularin-related protein 13 {ECO:0000313|EMBL:JAB86571.1};
GN Name=MTMRD {ECO:0000313|EMBL:JAB86571.1};
OS Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC Tephritidae; Ceratitis; Ceratitis.
OX NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB86571.1};
RN [1] {ECO:0000313|EMBL:JAB86571.1}
RP NUCLEOTIDE SEQUENCE.
RA Geib S.;
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB86571.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA Calla B., Hall B., Hou S., Geib S.M.;
RT "A genomic perspective to assessing quality of mass-reared SIT flies used
RT in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT California.";
RL BMC Genomics 15:98-98(2014).
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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; GAMC01019984; JAB86571.1; -; mRNA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd13208; PH-GRAM_MTMR5_MTMR13; 1.
DR CDD; cd01235; PH_Sbf1_hMTMR5; 1.
DR CDD; cd14534; PTP-MTMR5-like; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 3.40.50.11500; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001194; cDENN_dom.
DR InterPro; IPR005112; dDENN_dom.
DR InterPro; IPR043153; DENN_C.
DR InterPro; IPR004182; GRAM.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR022096; SBF1/SBF2.
DR InterPro; IPR037516; Tripartite_DENN.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF109; SET DOMAIN BINDING FACTOR, ISOFORM A; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF02141; DENN; 1.
DR Pfam; PF02893; GRAM; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF12335; SBF2; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00801; dDENN; 1.
DR SMART; SM00799; DENN; 1.
DR SMART; SM00568; GRAM; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR PROSITE; PS50211; DENN; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..319
FT /note="UDENN"
FT /evidence="ECO:0000259|PROSITE:PS50211"
FT DOMAIN 993..1510
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT DOMAIN 1636..1684
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1734..1838
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 1150..1191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1170..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1838 AA; 208541 MW; 6BE333E65CECAB7B CRC64;
MYAPKCLVLI SRLDYADTFK NCLGTIYTVY IENLPYTLEN LIGNILGCIQ VPPAGGPQVR
FSIGAGDKQS LQPPQSPSLP VTGTAVYFIF KQLGIKNVLI LLCAVMTENK ILFHSKSYSH
LTESCKALVS LMYPFRYTHV YIPILPAPLT EVLSTPTPFI MGIHSSLVSE ITDLLDVIVV
DLDGGMVTIP ESLSPPVPIL PSPLWEQTQE LLTMILFPNL SQADLAFPSL EKPTNYPKSD
AIIDKELRAI FMRLFAQLLQ GYRSCLTIIR IHPKPVITFH KAGFLGARDL IESEFLFRVL
DSMFFTTFVN ERGPPWRSSD AWDELYSSMN EILKSEAQNK NLIPTHIQEL GKILFENECP
NQQIYAQKVL RPPDGSFHRI HQPSFPRISN EKVELIINDG MRKNCISHRL TVLRNQMRII
PMGPRLPEVL DVRPAVLNSA RRLEVLKTCV AYIFENKIAD ARKLVPAVMR TLKHRDARLI
LCRELFGYVH GNKAILDHQQ FDLVIKFMNK TIQNSTGVDE YTVAAALLPM STIFCRKLST
GIVQFAYTCI QDHPIWKNLQ FWESTFYQDV QTQIKALYMQ RRRQIESNKE SNIVLDDVPL
EEPTALEITA EQMRKSPALE EDKKNELAQS EESTLYSQAI HYANRMVSLL IPPDVNAVGP
KPKQSFRLDD NQSVSNSIMG SHSLSEHSDE GFEENDALEV GGAVGKIVSR FIDRVCTEGG
VTSEHIRNLH DMVPGVVHMH IEMLESVYLE SKRHPHVQKP KIQTPCLLPG EEIVTDHLRC
YLMPDGREDD TQSWIPAEGA LFLTNYRIVF KGSPCDPLAC EQTIIRAFPI SSLLKEKKIS
VLYLSHLDQT LPEGLQLRSS TFQLMKIAFD TEVTPEMIET FRKILTKARH PIDEFEHFAF
QSYGTIMHGT APSKTKEKYS TLKGFAKKTI LRKFKQKAPT KRKLVTSTLD FDTLGPSTEA
IDTHSLDDEL EDDEFETNTD TMPRVLTAKD VERMRERSYV RDWKRLGFDD AQNGFRITTV
NANYSLCRSY PALLVAPLQI NDAALLHLGR CYKSQRIPVV TWRHRNGALL IRGALPHSKS
VIGMLKNSTG SNTMSHDVAN YHEQDKYISA LIDSMPKNIS LALAQYNLTG MNLSMNSLFL
NASDESSYLN RGDTSLTPEV NRKHKSALTA GSDGKSNNWT DSLKPKSNTI KNNSSVSAAT
AAYRKLRLYV LGEKSQTKSG INADLCAEFI AVDYADYRQS RIAFKKLMRA CLPSNTTNDA
DQTFAKSVEQ SEWLQQISSL LQLSGAVVDL MDLQESSVML SLEDGWDITA QISSIAQLCL
DPYYRTMEGF RVLIEKDWIA FGHRFAHRSN LKPTHGNSSI AFAPTFLQFL DAVYQIQKQF
PMAFEFNEFY VRFLAYHMVS CRFRTFLFDC EVERFDLGIA SVEDKRGSLS TKHHLLGNTG
SDDEGVYPMD VRSKAQSSVN FNRIGHSIFD YIERQHAKTQ IFYNFMYCVR DDVLRPQSSL
PALDLWPYYT NEELAQGPPY DLELTNADDE IDLSELRGKR IVVSAGYDNI EKSNPNAFVC
LLSDVRQAET ERGYLPQKWL QVWDQLEVPQ MEELTRKSSL SSILLQSHGK LAHKRSTLEI
LMKGRLSGYQ DKFFHPHRFE KHPYTTPTNC NHCTKLLWGP VGYRCMDCGN SYHEKCTEVS
LKNCTKYKAV DGVVPPNVNI SQGDTSSIAS SAATTARTSS HHFYNQFSSN VAENRTHEGH
LYKRGALLKG WKQRWFVLDS IKHQLRYYDS GEDSQCKGVI ELAEVQSVTT AQPAQIGTKR
IDEKGFFDLK TNRRTYNFYA VNANLAQEWI EKIQACLQ
//
