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MTMRD_XENLA
ID   MTMRD_XENLA             Reviewed;        1873 AA.
AC   Q6NTN5;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Myotubularin-related protein 13;
DE   AltName: Full=Inactive phosphatidylinositol 3-phosphatase 13 {ECO:0000305};
DE   AltName: Full=SET-binding factor 2;
GN   Name=sbf2; Synonyms=mtmr13;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Guanine nucleotide exchange factor (GEF) which may activate
CC       Rab small GTPases (By similarity). Promotes the exchange of GDP to GTP,
CC       converting inactive GDP-bound Rab proteins into their active GTP-bound
CC       form (By similarity). Acts as an adapter for the phosphatase mtmr2 (By
CC       similarity). {ECO:0000250|UniProtKB:E9PXF8,
CC       ECO:0000250|UniProtKB:Q86WG5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86WG5}.
CC       Membrane {ECO:0000250|UniProtKB:Q86WG5}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q86WG5}. Note=Associated with membranes.
CC       {ECO:0000250|UniProtKB:Q86WG5}.
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC       receptor class myotubularin subfamily. {ECO:0000305}.
CC   -!- CAUTION: Although it belongs to the non-receptor class myotubularin
CC       subfamily, lacks the conserved active site cysteine residue at position
CC       1439 in the dsPTPase catalytic loop, suggesting that it has no
CC       phosphatase activity. {ECO:0000305}.
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DR   EMBL; BC068924; AAH68924.1; -; mRNA.
DR   RefSeq; NP_001084507.1; NM_001091038.1.
DR   AlphaFoldDB; Q6NTN5; -.
DR   SMR; Q6NTN5; -.
DR   MaxQB; Q6NTN5; -.
DR   PRIDE; Q6NTN5; -.
DR   DNASU; 414452; -.
DR   GeneID; 414452; -.
DR   KEGG; xla:414452; -.
DR   CTD; 414452; -.
DR   Xenbase; XB-GENE-1004473; sbf2.L.
DR   OrthoDB; 45015at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 414452; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0019208; F:phosphatase regulator activity; IEA:InterPro.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR   CDD; cd13339; PH-GRAM_MTMR13; 1.
DR   Gene3D; 2.30.29.30; -; 2.
DR   Gene3D; 3.40.50.11500; -; 1.
DR   InterPro; IPR001194; cDENN_dom.
DR   InterPro; IPR005112; dDENN_dom.
DR   InterPro; IPR043153; DENN_C.
DR   InterPro; IPR004182; GRAM.
DR   InterPro; IPR030567; MTMR13.
DR   InterPro; IPR037823; MTMR13_PH-GRAM.
DR   InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR   InterPro; IPR030564; Myotubularin_fam.
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   InterPro; IPR005113; uDENN_dom.
DR   PANTHER; PTHR10807; PTHR10807; 1.
DR   PANTHER; PTHR10807:SF4; PTHR10807:SF4; 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   Pfam; PF03456; uDENN; 1.
DR   SMART; SM00801; dDENN; 1.
DR   SMART; SM00799; DENN; 1.
DR   SMART; SM00568; GRAM; 1.
DR   SMART; SM00233; PH; 1.
DR   SMART; SM00800; uDENN; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   PROSITE; PS50211; DENN; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Cytoplasm; Guanine-nucleotide releasing factor; Membrane;
KW   Reference proteome.
FT   CHAIN           1..1873
FT                   /note="Myotubularin-related protein 13"
FT                   /id="PRO_0000094946"
FT   DOMAIN          7..171
FT                   /note="uDENN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT   DOMAIN          190..323
FT                   /note="cDENN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT   DOMAIN          325..426
FT                   /note="dDENN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT   DOMAIN          869..955
FT                   /note="GRAM"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          1105..1613
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT   DOMAIN          1767..1871
FT                   /note="PH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT   REGION          1064..1102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1064..1080
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1087..1101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1873 AA;  210866 MW;  46D9D716D1716FDA CRC64;
     MARLADYFIV VGYDHEKTGS EGFGKIIQRF PMTDWSDTPF PQGIELFCQP GGWQLSRERK
     QPTFFIVVLT DIDSDRHYCA CLTFYEAEIN LQGTKREHSE TEEEDSGLIQ PAQVFAPKSL
     VLVSRLDYPE IFRACLGLIY TVYIDSLNVS LENLVSNLVT CIVPCAGGSQ KLFSLGAGDR
     QLIQTPLHDS LPVTGTSVAL LFQQLGIQNV LSLFCAVLTE NKVLFHSSSF QRLGDACRAL
     EALIYPLKYS YPYIPILPAQ LLEVLSSPTP FIIGVHSVFC SEIHDLLDVI IADLDGGTIK
     IPECIHLSPI PEPLLHQTQA ALSLVLHPDL EVADNAFAPL RTPVPHIKLL DKEVRAVFLR
     LFAQIFQGYR SCLQLIRIHA EPIIHFHKAA FLGQRGLIEN DFLTKVLSGM SFAGFVSERG
     PPYRPCDLFD ELVSFEVERI KDDDQNDTHK ILKHIRELAE QLFKNENPNP HMAFQKVPKP
     TEGSHLRVHI LPFSKMNDLK VQELIQEGLN KNQNSILSPR AEKKCVVPAG SPVVSIVDKA
     SSVFNSARRL EVVRNCIMYI FENKTLETEK TLPAALRALK GKAARQCLTE ELALHVQQNR
     SMLNHQQFDY IVRMMNCALQ DCSGSEEYTI ASQLLPLATA FCRKLSAAVS QFAYTCVQDH
     GVWANQQFWE TTFYNDVQNQ VRSLYLTTKN GNQGASEPKE NGVDSGNPER TVMDLAAEQL
     RLWPTLSKET QQELIQSEES TVFSQAIHFA NLMVYLLVPL DTSKNKLLRT SATGDWESGS
     NSIVTNSIAG SVAESYDTES GFEDSENDIA NSVVRFITRF IDKVCTESGV TQDHIKSLHC
     MIPGIVAMHI ETLEAVHRES RRLPPIKKPK IMRPALLPGE EFVCEALRVL LDPDGREEAT
     GGMLGGPHIL PAEGALFLTT YRIIFKGTPH DALVGEQTVI RSVPIASITR EKKINVQNQL
     HQNMQEGLQI RSATFQLIKV AFDEEVSAEM VDLFKKQLMK FRYPLSIFSA FAFAAGQTAP
     PIILPKQKEK NTSFRTISKT IVKGAKRAGK MTIGRQYAAK KKTGTILEER GSRSGGNEDD
     DISVSDDNEL PSGTLKPSEK STMEQLVERA CFRDYQRLAL GTISNSSTRF KSEHFRVTAL
     NRMHSLCRSY PGLLVVPQSV QDSSLQKVAR CYRHNRLPVV SWKNAKTNAV LLRGGGFHGK
     TVVGLFKSQN THTAAPASSL ESSSSIEQEK YLQALLNAIS VHYKMNGNST LTVRPTLALS
     PGSDRKSSRM SSVVKHVVPS HVDGSLSHSF ARGGVWASLR SSNRLITTQT PLIDVGARLV
     GKDLQTTYTD HSALQSQLLK RQAALYIFGE KSQLRGFKFD FALNCEFVPV EFGDIRQVKT
     SFKKLMRACV PSSNPTDSES TFLKAMGESE WFLQIHRIIQ LSVIISELME SGSSVMICLE
     DGWDITTQVV SLVQILGDPF YRTLEGFRML IEKEWLSFGH KFSQRSNLSP SSQGTGFVPI
     FLQFLDCVHQ IHNQYPTEFE FNRYYLKFLA YHHVSNRFKT FLLDSDYERL EHGTLFEDKG
     DKHSRRGICI WEYIERIHKK KTVFFNYLFA PTELEALKPS ANISTLRKWE YYMEETLASG
     PSYDWIITPS RFNASDETDS GEEAQQQGKR KIVWPCYDDV QKVQPDAITH LMNEIERLEI
     KLNQTSERWQ LLWERAKVKL KENAKKENNN PASLVSANLQ SYQKRSMVHL PDSGLGDEQN
     LNASPSNGVD RRTATLYNHF TSKNEENRSY EGILYKRGAL LKGWKPRWFV LDITKHQLRY
     YDSGEDTSCK GYIDLADVET VVPAAPTIGA PKHANEKAFF DVKTSKRVYN FCAQDAQSAQ
     LWMDKIQNCI SDA
 
 
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