MTMR6_MOUSE
ID MTMR6_MOUSE Reviewed; 617 AA.
AC Q8VE11; L8AZD2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Myotubularin-related protein 6 {ECO:0000305};
DE AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase {ECO:0000305};
DE EC=3.1.3.95 {ECO:0000250|UniProtKB:Q9Y217};
DE AltName: Full=Phosphatidylinositol-3-phosphate phosphatase {ECO:0000305};
DE EC=3.1.3.64 {ECO:0000250|UniProtKB:Q9Y217};
GN Name=Mtmr6 {ECO:0000312|MGI:MGI:2145637};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH MTMR9 AND RAB1B,
RP TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=23188820; DOI=10.1074/jbc.m112.395087;
RA Mochizuki Y., Ohashi R., Kawamura T., Iwanari H., Kodama T., Naito M.,
RA Hamakubo T.;
RT "Phosphatidylinositol 3-phosphatase myotubularin-related protein 6 (MTMR6)
RT is regulated by small GTPase Rab1B in the early secretory and autophagic
RT pathways.";
RL J. Biol. Chem. 288:1009-1021(2013).
RN [2] {ECO:0000312|EMBL:BAC36259.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC36259.1}, and
RC NOD {ECO:0000312|EMBL:BAE32884.1};
RC TISSUE=Dendritic cell {ECO:0000312|EMBL:BAE32884.1}, and
RC Embryonic head {ECO:0000312|EMBL:BAC36259.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000312|EMBL:EDL36118.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000312|EMBL:AAH20019.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH20019.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH20019.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH MTMR9.
RX PubMed=12890864; DOI=10.1073/pnas.1333958100;
RA Mochizuki Y., Majerus P.W.;
RT "Characterization of myotubularin-related protein 7 and its binding
RT partner, myotubularin-related protein 9.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9768-9773(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF
RP 336-CYS--ARG-342.
RX PubMed=24591580; DOI=10.1073/pnas.1311029111;
RA Maekawa M., Terasaka S., Mochizuki Y., Kawai K., Ikeda Y., Araki N.,
RA Skolnik E.Y., Taguchi T., Arai H.;
RT "Sequential breakdown of 3-phosphorylated phosphoinositides is essential
RT for the completion of macropinocytosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E978-E987(2014).
CC -!- FUNCTION: Phosphatase that acts on lipids with a phosphoinositol
CC headgroup. Dephosphorylates phosphatidylinositol 3-phosphate
CC (PtdIns(3)P) and phosphatidylinositol 3,5-bisphosphate. Binds with high
CC affinity to phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) but
CC also to phosphatidylinositol 3-phosphate (PtdIns(3)P),
CC phosphatidylinositol 4-phosphate (PtdIns(4)P), and phosphatidylinositol
CC 5-phosphate (PtdIns(5)P), phosphatidic acid and phosphatidylserine (By
CC similarity). Negatively regulates ER-Golgi protein transport (By
CC similarity). Probably in association with MTMR9, plays a role in the
CC late stages of macropinocytosis by dephosphorylating
CC phosphatidylinositol 3-phosphate in membrane ruffles (PubMed:24591580).
CC Acts as a negative regulator of KCNN4/KCa3.1 channel activity in CD4(+)
CC T-cells possibly by decreasing intracellular levels of
CC phosphatidylinositol 3-phosphate. Negatively regulates proliferation of
CC reactivated CD4(+) T-cells. In complex with MTMR9, negatively regulates
CC DNA damage-induced apoptosis. The formation of the MTMR6-MTMR9 complex
CC stabilizes both MTMR6 and MTMR9 protein levels (By similarity).
CC {ECO:0000250|UniProtKB:A0A0G2JXT6, ECO:0000250|UniProtKB:Q9Y217,
CC ECO:0000269|PubMed:24591580}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC bisphosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:39019,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57795,
CC ChEBI:CHEBI:57923; EC=3.1.3.95;
CC Evidence={ECO:0000250|UniProtKB:Q9Y217};
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:0000250|UniProtKB:Q9Y217};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-inositol-3,5-
CC bisphosphate) + H2O = 1,2-dioctanoyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-5-phosphate) + phosphate; Xref=Rhea:RHEA:45632,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:78911,
CC ChEBI:CHEBI:85342; Evidence={ECO:0000250|UniProtKB:Q9Y217};
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:0000250|UniProtKB:Q9Y217};
CC -!- ACTIVITY REGULATION: Allosterically activated by phosphatidylserine
CC and/or phosphatidylinositol 4-phosphate (PtdIns(4)P), and
CC phosphatidylinositol 5-phosphate (PtdIns(5)P) (By similarity).
CC Interaction with MTMR9 increases catalytic activity towards
CC phosphatidylinositol 3,5-bisphosphate (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y217}.
CC -!- SUBUNIT: Homodimer (By similarity). Heterodimer (via C-terminus) with
CC MTMR9 (via C-terminus) (PubMed:23188820, PubMed:12890864). Interacts
CC with ALKBH4 (By similarity). Interacts with KCNN4 (By similarity).
CC Interacts (via GRAM domain) with RAB1B (in GDP-bound form); the
CC interaction regulates MTMR6 recruitment to the endoplasmic reticulum-
CC Golgi intermediate compartment (PubMed:23188820).
CC {ECO:0000250|UniProtKB:Q9Y217, ECO:0000269|PubMed:12890864,
CC ECO:0000269|PubMed:23188820}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24591580}.
CC Endoplasmic reticulum-Golgi intermediate compartment
CC {ECO:0000250|UniProtKB:Q9Y217}. Cell projection, ruffle membrane
CC {ECO:0000269|PubMed:24591580}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q9Y217}. Note=Localizes to ruffles during EGF-
CC induced macropinocytosis (PubMed:24591580). Colocalizes with MTMR9 to
CC the perinuclear region (By similarity). Partially localizes to the
CC endoplasmic reticulum (By similarity). Co-localizes with RAB1B to the
CC endoplasmic reticulum-Golgi intermediate compartment and to the peri-
CC Golgi region (By similarity). {ECO:0000250|UniProtKB:A0A0G2JXT6,
CC ECO:0000250|UniProtKB:Q9Y217, ECO:0000269|PubMed:24591580}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VE11-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VE11-2; Sequence=VSP_060069;
CC -!- TISSUE SPECIFICITY: Isoform 1: Ubiquitously expressed including in
CC heart, brain, spleen, lung, liver, muscle, kidney and testis (at
CC protein level) (PubMed:23188820). Isoform 2: Expressed in testis (at
CC protein level) (PubMed:23188820). {ECO:0000269|PubMed:23188820}.
CC -!- DOMAIN: The GRAM domain is required for cell membrane localization.
CC {ECO:0000269|PubMed:24591580}.
CC -!- DOMAIN: The C-terminus domain (aa 502-617) mediates interaction with
CC MTMR9. {ECO:0000269|PubMed:23188820}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000255}.
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DR EMBL; AB517623; BAM76259.1; -; mRNA.
DR EMBL; AK076218; BAC36259.1; -; mRNA.
DR EMBL; AK154859; BAE32884.1; -; mRNA.
DR EMBL; AC166113; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466535; EDL36118.1; -; Genomic_DNA.
DR EMBL; BC020019; AAH20019.1; -; mRNA.
DR CCDS; CCDS27176.1; -. [Q8VE11-1]
DR RefSeq; NP_659092.1; NM_144843.4. [Q8VE11-1]
DR RefSeq; XP_017171460.1; XM_017315971.1. [Q8VE11-2]
DR AlphaFoldDB; Q8VE11; -.
DR SMR; Q8VE11; -.
DR BioGRID; 230116; 9.
DR STRING; 10090.ENSMUSP00000022563; -.
DR iPTMnet; Q8VE11; -.
DR PhosphoSitePlus; Q8VE11; -.
DR EPD; Q8VE11; -.
DR jPOST; Q8VE11; -.
DR MaxQB; Q8VE11; -.
DR PaxDb; Q8VE11; -.
DR PRIDE; Q8VE11; -.
DR ProteomicsDB; 287638; -. [Q8VE11-1]
DR ProteomicsDB; 341414; -.
DR Antibodypedia; 22544; 143 antibodies from 24 providers.
DR DNASU; 219135; -.
DR Ensembl; ENSMUST00000022563; ENSMUSP00000022563; ENSMUSG00000021987. [Q8VE11-1]
DR Ensembl; ENSMUST00000224366; ENSMUSP00000153403; ENSMUSG00000021987. [Q8VE11-2]
DR GeneID; 219135; -.
DR KEGG; mmu:219135; -.
DR UCSC; uc007ufa.2; mouse. [Q8VE11-1]
DR UCSC; uc033gri.1; mouse.
DR CTD; 9107; -.
DR MGI; MGI:2145637; Mtmr6.
DR VEuPathDB; HostDB:ENSMUSG00000021987; -.
DR eggNOG; KOG1089; Eukaryota.
DR GeneTree; ENSGT00940000158055; -.
DR HOGENOM; CLU_001839_3_2_1; -.
DR InParanoid; Q8VE11; -.
DR OMA; PNTDYMY; -.
DR OrthoDB; 824298at2759; -.
DR PhylomeDB; Q8VE11; -.
DR TreeFam; TF315197; -.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR BioGRID-ORCS; 219135; 10 hits in 77 CRISPR screens.
DR ChiTaRS; Mtmr6; mouse.
DR PRO; PR:Q8VE11; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8VE11; protein.
DR Bgee; ENSMUSG00000021987; Expressed in spermatocyte and 258 other tissues.
DR Genevisible; Q8VE11; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0106018; F:phosphatidylinositol-3,5-bisphosphate phosphatase activity; ISO:MGI.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; ISO:MGI.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; ISO:MGI.
DR CDD; cd13343; PH-GRAM_MTMR6; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR030581; MTMR6.
DR InterPro; IPR035998; MTMR6_PH-GRAM.
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 InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR PANTHER; PTHR10807; PTHR10807; 1.
DR PANTHER; PTHR10807:SF34; PTHR10807:SF34; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasm;
KW Endocytosis; Endoplasmic reticulum; Hydrolase; Lipid metabolism; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..617
FT /note="Myotubularin-related protein 6"
FT /id="PRO_0000367041"
FT DOMAIN 1..101
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 124..499
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT REGION 2..141
FT /note="Interaction with RAB1B"
FT /evidence="ECO:0000269|PubMed:23188820"
FT ACT_SITE 336
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q13614,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 248..251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 273..274
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 336..342
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT BINDING 382
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q13614"
FT MOD_RES 108
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y217"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y217"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y217"
FT VAR_SEQ 242
FT /note="K -> KHRMQSWWDTQKDIGRIIVRISSKIWNDEKIRESDERKR (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_060069"
FT MUTAGEN 336..342
FT /note="CSDGWDR->ASDGWDA: Probable loss of catalytic
FT activity. Loss of macropinocytosis."
FT /evidence="ECO:0000269|PubMed:24591580"
SQ SEQUENCE 617 AA; 70933 MW; EE699C578602A013 CRC64;
MEHIRTTKVE QVKLLDRFST NNKSLTGTLY LTATHLLFID AQQKETWILH HHIASVEKLA
LTTSGCPLVI QCKNFRIVHF IVPRERDCHD IYNSLLQLSK QAKYEDLYAF SYNPKQNDTE
RRNGWQLIDL AAEYERMGVP NANWQLSDAN REYKVCETYP RELYVPRTAS RPVIVGSSNF
RSKGRLPVLS YCRQGTEAAI CRCSQPLSGF SARCLEDEHL LQAISKANPG NRYMYVVDTR
PKLNAIANRA AGKGYENEDN YSNIRFQFVG IENIHVMRSS LQKLLEVNGS KGLSVNDFYS
GLESSGWLRH IKAVLDAAIF LAKAIVVENA SVLVHCSDGW DRTSQVCSLG SLLLDSYYRT
MKGFMVLIEK DWISFGHKFS ERCGHLDGDP REVSPVFTQF LECVWHLTQQ FPQAFEFNEA
FLLQIHEHIH SCQFGNFLGN CQKEREELRL KEKTYSLWPF LLDDKKKYLN PLYSSKSQRL
TVLEPNTASF NFKFWRNMYH QFDRTLHPRQ SVLSIIMNMN EQSKQLEEDI KDLEAKIKQC
KNGILTKELL HAVHPESPAL KTSLCLKEPS LLPVKDTLRA IEGSSPADNR YCDYAEEFSK
SEPTVVSLEY GVARMTC
