ID A0A226EGI2_FOLCA Unreviewed; 613 AA.
AC A0A226EGI2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Myotubularin-related protein 9 {ECO:0000313|EMBL:OXA56682.1};
GN ORFNames=Fcan01_08278 {ECO:0000313|EMBL:OXA56682.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA56682.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA56682.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA56682.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA56682.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000256|ARBA:ARBA00007471}.
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:OXA56682.1}.
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DR EMBL; LNIX01000003; OXA56682.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226EGI2; -.
DR STRING; 158441.A0A226EGI2; -.
DR OMA; ILKCKDF; -.
DR Proteomes; UP000198287; Unassembled WGS sequence.
DR CDD; cd13211; PH-GRAM_MTMR9; 1.
DR CDD; cd14536; PTP-MTMR9; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR PANTHER; PTHR10807:SF73; LD06050P; 1.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR Pfam; PF21098; PH-GRAM_MTMR6-like; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000198287}.
FT DOMAIN 125..523
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 575..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 533..560
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 577..599
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 613 AA; 69876 MW; 51575E5CA66B37DC CRC64;
MEFIELIKVP KVDNVTMRRN ALPTVEGGTL CITSHHLILS SRKDGEEELW LLHRNIDLVE
RKPLTLGGGS LVIKCKDFSV IHLDIVGSED FNNAADSIEA LSNVDAQHLM YAFFYRPMYS
IVEDGWTAFS TEAEFSKLIL QSENEWRISH INRDYSVCKS YPKTVVVPKS IPDEEILVAA
TFRQGGRFPV LCFRHENGAV LLRAGEPLVG PSGRRCKEDE RLINAILTIG KRGYIIDTRS
QTLAQTARTK GGGVELEIYY PQWRRIHKPI DRHYTLLDSL SKLLEACSDT NCTMDKWLSR
LDASGWLTNV RETLNCACVV AQCLDQESNS VLIHGGDGVD LTLAVTSLTQ IILNPDCRSI
RGFEALIERE WLQGGYPFRT RHSKSAFAYS LSNVKNQRKA YAPSFLLFSQ NGDVHADPSC
GFLLFIDCVW QIYNQFPFSF EFSEQFLMTL VQHSYASQFG TFLCDNVCER EELHLMTKTV
SLWSHVNRPD IMQSYMNPVY EPNPCVIWPS VHPISLQLWN GMYLKGIIDQ SSMKKTWNTI
AELKENEKEL KKEAIKLRKY LLDLHQSRHS IQRKLSEATI DDNPTSDDCV NFQHTEDSSS
ESPGDIDHPL KYQ
//
