MILK2_HUMAN
ID MILK2_HUMAN Reviewed; 904 AA.
AC Q8IY33; D3YTD2; Q7RTP4; Q7Z655; Q8TEQ4; Q9H5F9;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=MICAL-like protein 2;
DE AltName: Full=Junctional Rab13-binding protein;
DE AltName: Full=Molecule interacting with CasL-like 2;
DE Short=MICAL-L2;
GN Name=MICALL2; Synonyms=JRAB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC TISSUE=Brain cortex, and Small intestine;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 [7]
RP IDENTIFICATION.
RX PubMed=12110185; DOI=10.1016/s0092-8674(02)00794-8;
RA Terman J.R., Mao T., Pasterkamp R.J., Yu H.-H., Kolodkin A.L.;
RT "MICALs, a family of conserved flavoprotein oxidoreductases, function in
RT plexin-mediated axonal repulsion.";
RL Cell 109:887-900(2002).
RN [8]
RP INTERACTION WITH RAB13.
RX PubMed=16525024; DOI=10.1091/mbc.e05-09-0826;
RA Terai T., Nishimura N., Kanda I., Yasui N., Sasaki T.;
RT "JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the
RT endocytic recycling of occludin.";
RL Mol. Biol. Cell 17:2465-2475(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-494; SER-649; SER-658 AND
RP SER-660, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP INTERACTION WITH FLNA.
RX PubMed=23890175; DOI=10.1111/gtc.12078;
RA Sakane A., Alamir Mahmoud Abdallah A., Nakano K., Honda K., Kitamura T.,
RA Imoto I., Matsushita N., Sasaki T.;
RT "Junctional Rab13-binding protein (JRAB) regulates cell spreading via
RT filamins.";
RL Genes Cells 18:810-822(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-143; SER-153;
RP SER-249; SER-294; SER-494; SER-504; SER-598 AND SER-649, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-153 AND THR-644, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Effector of small Rab GTPases which is involved in junctional
CC complexes assembly through the regulation of cell adhesion molecules
CC transport to the plasma membrane and actin cytoskeleton reorganization.
CC Regulates the endocytic recycling of occludins, claudins and E-cadherin
CC to the plasma membrane and may thereby regulate the establishment of
CC tight junctions and adherens junctions. In parallel, may regulate actin
CC cytoskeleton reorganization directly through interaction with F-actin
CC or indirectly through actinins and filamins. Most probably involved in
CC the processes of epithelial cell differentiation, cell spreading and
CC neurite outgrowth (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with RAB13 (GTP-bound form); competes with RAB8A and
CC is involved in tight junctions assembly. Interacts with RAB8A; competes
CC with RAB13 and is involved in E-cadherin endocytic recycling (By
CC similarity). Interacts with RAB8B (By similarity). Interacts
CC (preferentially in opened conformation) with ACTN1 and ACTN4;
CC stimulated by RAB13 activation (By similarity). Interacts (via
CC calponin-homology (CH) domain) with the filamins FLNA, FLNB and FLNC
CC (via actin-binding domain). {ECO:0000250, ECO:0000269|PubMed:16525024,
CC ECO:0000269|PubMed:23890175}.
CC -!- INTERACTION:
CC Q8IY33; P12814: ACTN1; NbExp=6; IntAct=EBI-2555563, EBI-351710;
CC Q8IY33; P35609: ACTN2; NbExp=7; IntAct=EBI-2555563, EBI-77797;
CC Q8IY33; Q08043: ACTN3; NbExp=3; IntAct=EBI-2555563, EBI-2880652;
CC Q8IY33; O43707: ACTN4; NbExp=3; IntAct=EBI-2555563, EBI-351526;
CC Q8IY33; Q01850: CDR2; NbExp=3; IntAct=EBI-2555563, EBI-1181367;
CC Q8IY33; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-2555563, EBI-10303987;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cell junction, tight junction {ECO:0000250}.
CC Recycling endosome {ECO:0000250}. Cell projection {ECO:0000250}.
CC Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytosol
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8IY33-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IY33-2; Sequence=VSP_009854, VSP_009855;
CC Name=3;
CC IsoId=Q8IY33-3; Sequence=VSP_009856;
CC Name=4;
CC IsoId=Q8IY33-4; Sequence=VSP_009857;
CC Name=5;
CC IsoId=Q8IY33-5; Sequence=VSP_009858;
CC -!- DOMAIN: Probably exists in a closed and an opened conformation due to
CC interaction of the C-terminal coiled-coil domain with an N-terminal
CC region including the calponin-homology (CH) and the LIM zinc-binding
CC domain. The conformational change is regulated by RAB13 (By
CC similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15667.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB84894.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL833704; CAD98087.1; -; mRNA.
DR EMBL; AK027124; BAB15667.1; ALT_INIT; mRNA.
DR EMBL; AK126808; BAC86702.1; -; mRNA.
DR EMBL; AK074068; BAB84894.1; ALT_INIT; mRNA.
DR EMBL; AC102953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471144; EAW87200.1; -; Genomic_DNA.
DR EMBL; BC037988; AAH37988.1; -; mRNA.
DR EMBL; BK000467; DAA01346.1; -; mRNA.
DR CCDS; CCDS5324.1; -. [Q8IY33-1]
DR RefSeq; NP_891554.1; NM_182924.3. [Q8IY33-1]
DR AlphaFoldDB; Q8IY33; -.
DR SMR; Q8IY33; -.
DR BioGRID; 122879; 22.
DR IntAct; Q8IY33; 18.
DR STRING; 9606.ENSP00000297508; -.
DR GlyGen; Q8IY33; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q8IY33; -.
DR PhosphoSitePlus; Q8IY33; -.
DR BioMuta; MICALL2; -.
DR DMDM; 46396456; -.
DR EPD; Q8IY33; -.
DR jPOST; Q8IY33; -.
DR MassIVE; Q8IY33; -.
DR MaxQB; Q8IY33; -.
DR PaxDb; Q8IY33; -.
DR PeptideAtlas; Q8IY33; -.
DR PRIDE; Q8IY33; -.
DR ProteomicsDB; 12799; -.
DR ProteomicsDB; 71097; -. [Q8IY33-1]
DR ProteomicsDB; 71098; -. [Q8IY33-2]
DR ProteomicsDB; 71099; -. [Q8IY33-3]
DR ProteomicsDB; 71100; -. [Q8IY33-4]
DR ProteomicsDB; 71101; -. [Q8IY33-5]
DR Antibodypedia; 24191; 84 antibodies from 20 providers.
DR DNASU; 79778; -.
DR Ensembl; ENST00000297508.8; ENSP00000297508.7; ENSG00000164877.19. [Q8IY33-1]
DR Ensembl; ENST00000413446.5; ENSP00000405415.1; ENSG00000164877.19. [Q8IY33-2]
DR GeneID; 79778; -.
DR KEGG; hsa:79778; -.
DR MANE-Select; ENST00000297508.8; ENSP00000297508.7; NM_182924.4; NP_891554.1.
DR UCSC; uc003skj.5; human. [Q8IY33-1]
DR CTD; 79778; -.
DR DisGeNET; 79778; -.
DR GeneCards; MICALL2; -.
DR HGNC; HGNC:29672; MICALL2.
DR HPA; ENSG00000164877; Low tissue specificity.
DR MalaCards; MICALL2; -.
DR neXtProt; NX_Q8IY33; -.
DR OpenTargets; ENSG00000164877; -.
DR PharmGKB; PA162395928; -.
DR VEuPathDB; HostDB:ENSG00000164877; -.
DR eggNOG; KOG0517; Eukaryota.
DR GeneTree; ENSGT00940000160222; -.
DR HOGENOM; CLU_015382_0_0_1; -.
DR InParanoid; Q8IY33; -.
DR OMA; SELMYKM; -.
DR OrthoDB; 377701at2759; -.
DR PhylomeDB; Q8IY33; -.
DR TreeFam; TF328311; -.
DR PathwayCommons; Q8IY33; -.
DR SignaLink; Q8IY33; -.
DR BioGRID-ORCS; 79778; 25 hits in 1075 CRISPR screens.
DR ChiTaRS; MICALL2; human.
DR GenomeRNAi; 79778; -.
DR Pharos; Q8IY33; Tbio.
DR PRO; PR:Q8IY33; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8IY33; protein.
DR Bgee; ENSG00000164877; Expressed in tibial nerve and 136 other tissues.
DR Genevisible; Q8IY33; HS.
DR GO; GO:0005923; C:bicellular tight junction; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; ISS:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0042805; F:actinin binding; IEA:Ensembl.
DR GO; GO:0031005; F:filamin binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0030041; P:actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; HMP:ParkinsonsUK-UCL.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR022735; bMERB_dom.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR028563; MICAL-L.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR23167:SF53; PTHR23167:SF53; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF12130; DUF3585; 1.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00132; LIM; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS51848; BMERB; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW Coiled coil; Cytoplasm; Cytoskeleton; Endosome; LIM domain; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Tight junction; Zinc.
FT CHAIN 1..904
FT /note="MICAL-like protein 2"
FT /id="PRO_0000075850"
FT DOMAIN 1..107
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 186..248
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 723..874
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 1..260
FT /note="Forms an intramolecular interaction with the C-
FT terminal coiled coil domain keeping the protein in a closed
FT conformation"
FT /evidence="ECO:0000250"
FT REGION 117..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..697
FT /note="Mediates targeting to the cell plasma membrane"
FT /evidence="ECO:0000250"
FT REGION 261..388
FT /note="Necessary and sufficient for interaction with
FT actinins"
FT /evidence="ECO:0000250"
FT REGION 698..807
FT /note="Forms an intramolecular interaction with the N-
FT terminal Calponin-homology and LIM zinc-binding domains-
FT containing region keeping the protein in a closed
FT conformation"
FT /evidence="ECO:0000250"
FT REGION 807..903
FT /note="Mediates interaction with RAB13 and is required for
FT transition from the closed to the opened conformation"
FT /evidence="ECO:0000250"
FT COILED 735..771
FT /evidence="ECO:0000255"
FT COMPBIAS 265..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..532
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..659
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..705
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18088087,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 644
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 649
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3TN34"
FT VAR_SEQ 1..570
FT /note="MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLINFSA
FT LKKENIYENNKLAFRVAEEHLGIPALLDAEDMVALKVPDRLSILTYVSQYYNYFHGRSP
FT IGGMAGVKRASEDSEEEPSGKKAPVQAAKLPSPAPARKPPLSPAQTNPVVQRRNEGAGG
FT PPPKTDQALAGSLVSSTCGVCGKHVHLVQRHLADGRLYHRSCFRCKQCSCTLHSGAYKA
FT TGEPGTFVCTSHLPAAASASPKLTGLVPRQPGAMGVDSRTSCSPQKAQEANKARPSAWE
FT PAAGNSPARASVPAAPNPAATSATSVHVRSPARPSESRLAPTPTEGKVRPRVTNSSPMG
FT WSSAAPCTAAAASHPAVPPSAPDPRPATPQGGGAPRVAAPQTTLSSSSTSAATVDPPAW
FT TPSASRTQQARNKFFQTSAVPPGTSLSGRGPTPSLVLSKDSSKEQARNFLKQALSALEE
FT AGAPAPGRPSPATAAVPSSQPKTEAPQASPLAKPLQSSSPRVLGLPSRMEPPAPLSTSS
FT TSQASALPPAGRRNLAESSGVGRVGAGSRPKPEAPMAKGKSTTLTQ -> MALSSWAQG
FT TSWAAKGFSRSFSLAEFSLLKPRAGSCRTQEPRKPADGQPWLRCSPCTGGQRIWVHGAH
FT PATSPPIRQKGKLRPRGRESFPQGHTAQESQLGAPPLTPCPVLLMPPGRLAVGVSEGGV
FT AMGRWQGEAQPPLQTPHSQHSFLTPRPLASHP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009856"
FT VAR_SEQ 1..48
FT /note="MAAIRALQQWCRQQCEGYRDVNICNMTTSFRDGLAFCAILHRHRPDLI ->
FT MFLSSR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_009854"
FT VAR_SEQ 29..240
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_009858"
FT VAR_SEQ 571..904
FT /note="DMSTSLQEGQEDGPAGWRANLKPVDRRSPAERTLKPKEPRALAEPRAGEAPR
FT KVSGSFAGSVHITLTPVRPDRTPRPASPGPSLPARSPSPPRRRRLAVPASLDVCDNWLR
FT PEPPGQEARVQSWKEEEKKPHLQGKPGRPLSPANVPALPGETVTSPVRLHPDYLSPEEI
FT QRQLQDIERRLDALELRGVELEKRLRAAEGDDAEDSLMVDWFWLIHEKQLLLRQESELM
FT YKSKAQRLEEQQLDIEGELRRLMAKPEALKSLQERRREQELLEQYVSTVNDRSDIVDSL
FT DEDRLREQEEDQMLRDMIEKLGLQRKKSKFRLSKIWSPKSKSSPSQ -> GE (in
FT isoform 4)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_009857"
FT VAR_SEQ 656..904
FT /note="ARSPSPPRRRRLAVPASLDVCDNWLRPEPPGQEARVQSWKEEEKKPHLQGKP
FT GRPLSPANVPALPGETVTSPVRLHPDYLSPEEIQRQLQDIERRLDALELRGVELEKRLR
FT AAEGDDAEDSLMVDWFWLIHEKQLLLRQESELMYKSKAQRLEEQQLDIEGELRRLMAKP
FT EALKSLQERRREQELLEQYVSTVNDRSDIVDSLDEDRLREQEEDQMLRDMIEKLGLQRK
FT KSKFRLSKIWSPKSKSSPSQ -> GPPPHPAAGDWPSLPASTFVTTGFGRSPLARKPEC
FT RAGRRRRRNLTFRANQGDPCPRPMSLLCLARR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_009855"
FT VARIANT 480
FT /note="A -> P (in dbSNP:rs12540098)"
FT /id="VAR_034071"
FT VARIANT 519
FT /note="P -> L (in dbSNP:rs4075307)"
FT /id="VAR_034072"
FT VARIANT 623
FT /note="K -> R (in dbSNP:rs61287564)"
FT /id="VAR_061356"
FT VARIANT 711
FT /note="L -> V (in dbSNP:rs11980797)"
FT /id="VAR_050159"
FT CONFLICT 255
FT /note="L -> M (in Ref. 1; CAD98087)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="S -> L (in Ref. 2; BAB15667)"
FT /evidence="ECO:0000305"
FT CONFLICT 706
FT /note="K -> R (in Ref. 2; BAB15667)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 904 AA; 97502 MW; A2C360EDDEFFA2EF CRC64;
MAAIRALQQW CRQQCEGYRD VNICNMTTSF RDGLAFCAIL HRHRPDLINF SALKKENIYE
NNKLAFRVAE EHLGIPALLD AEDMVALKVP DRLSILTYVS QYYNYFHGRS PIGGMAGVKR
ASEDSEEEPS GKKAPVQAAK LPSPAPARKP PLSPAQTNPV VQRRNEGAGG PPPKTDQALA
GSLVSSTCGV CGKHVHLVQR HLADGRLYHR SCFRCKQCSC TLHSGAYKAT GEPGTFVCTS
HLPAAASASP KLTGLVPRQP GAMGVDSRTS CSPQKAQEAN KARPSAWEPA AGNSPARASV
PAAPNPAATS ATSVHVRSPA RPSESRLAPT PTEGKVRPRV TNSSPMGWSS AAPCTAAAAS
HPAVPPSAPD PRPATPQGGG APRVAAPQTT LSSSSTSAAT VDPPAWTPSA SRTQQARNKF
FQTSAVPPGT SLSGRGPTPS LVLSKDSSKE QARNFLKQAL SALEEAGAPA PGRPSPATAA
VPSSQPKTEA PQASPLAKPL QSSSPRVLGL PSRMEPPAPL STSSTSQASA LPPAGRRNLA
ESSGVGRVGA GSRPKPEAPM AKGKSTTLTQ DMSTSLQEGQ EDGPAGWRAN LKPVDRRSPA
ERTLKPKEPR ALAEPRAGEA PRKVSGSFAG SVHITLTPVR PDRTPRPASP GPSLPARSPS
PPRRRRLAVP ASLDVCDNWL RPEPPGQEAR VQSWKEEEKK PHLQGKPGRP LSPANVPALP
GETVTSPVRL HPDYLSPEEI QRQLQDIERR LDALELRGVE LEKRLRAAEG DDAEDSLMVD
WFWLIHEKQL LLRQESELMY KSKAQRLEEQ QLDIEGELRR LMAKPEALKS LQERRREQEL
LEQYVSTVND RSDIVDSLDE DRLREQEEDQ MLRDMIEKLG LQRKKSKFRL SKIWSPKSKS
SPSQ
