MILK1_HUMAN
ID MILK1_HUMAN Reviewed; 863 AA.
AC Q8N3F8; Q5TI16; Q7RTP5; Q8N3N8; Q9BVL9; Q9BY92; Q9UH43; Q9UH44; Q9UH45;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=MICAL-like protein 1;
DE AltName: Full=Molecule interacting with Rab13;
DE Short=MIRab13;
GN Name=MICALL1; Synonyms=KIAA1668, MIRAB13;
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 [MRNA], FUNCTION IN ENDOCYTOSIS, INTERACTION WITH
RP RAB13, SUBCELLULAR LOCATION, AND DOMAIN.
RC TISSUE=Uterine adenocarcinoma;
RX PubMed=21795389; DOI=10.1091/mbc.e11-01-0030;
RA Abou-Zeid N., Pandjaitan R., Sengmanivong L., David V., Le Pavec G.,
RA Salamero J., Zahraoui A.;
RT "MICAL-like1 mediates epidermal growth factor receptor endocytosis.";
RL Mol. Biol. Cell 22:3431-3441(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-863, AND VARIANT SER-519.
RC TISSUE=Melanoma;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-863.
RC TISSUE=Brain;
RX PubMed=11258795; DOI=10.1093/dnares/8.1.1;
RA Hirosawa M., Nagase T., Murahashi Y., Kikuno R., Ohara O.;
RT "Identification of novel transcribed sequences on human chromosome 22 by
RT expressed sequence tag mapping.";
RL DNA Res. 8:1-9(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 514-863.
RC TISSUE=Choriocarcinoma;
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 GENE STRUCTURE.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-309; THR-318;
RP THR-467; SER-471; SER-484 AND SER-486, AND IDENTIFICATION BY MASS
RP 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP FUNCTION IN ENDOCYTIC RECYCLING, INTERACTION WITH EHD1; EHD3 AND RAB8A,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF 425-ASN--PHE-427; 633-ASN--PHE-635
RP AND 721-MET--PHE-726.
RX PubMed=19864458; DOI=10.1091/mbc.e09-06-0535;
RA Sharma M., Giridharan S.S., Rahajeng J., Naslavsky N., Caplan S.;
RT "MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor
RT recycling.";
RL Mol. Biol. Cell 20:5181-5194(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP FUNCTION IN ENDOCYTOSIS, AND INTERACTION WITH DPYSL2.
RX PubMed=20801876; DOI=10.1074/jbc.c110.166066;
RA Rahajeng J., Giridharan S.S., Naslavsky N., Caplan S.;
RT "Collapsin response mediator protein-2 (Crmp2) regulates trafficking by
RT linking endocytic regulatory proteins to dynein motors.";
RL J. Biol. Chem. 285:31918-31922(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-467; THR-469; SER-470;
RP SER-471; SER-484; SER-486 AND SER-578, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP INTERACTION WITH ARF6 AND RAB35, AND SUBCELLULAR LOCATION.
RX PubMed=21951725; DOI=10.1111/j.1600-0854.2011.01294.x;
RA Rahajeng J., Giridharan S.S., Cai B., Naslavsky N., Caplan S.;
RT "MICAL-L1 is a tubular endosomal membrane hub that connects Rab35 and Arf6
RT with Rab8a.";
RL Traffic 13:82-93(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-391; THR-467;
RP SER-471; SER-484; SER-486; SER-578 AND SER-621, AND IDENTIFICATION BY MASS
RP 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 [17]
RP FUNCTION IN MEMBRANE TUBULATION, LIPID-BINDING, HOMOOLIGOMERIZATION,
RP INTERACTION WITH EHD1 AND PACSIN2, AND MUTAGENESIS OF 385-PRO--PRO-387 AND
RP 480-PRO--PRO-483.
RX PubMed=23596323; DOI=10.1091/mbc.e13-01-0026;
RA Giridharan S.S., Cai B., Vitale N., Naslavsky N., Caplan S.;
RT "Cooperation of MICAL-L1, syndapin2, and phosphatidic acid in tubular
RT recycling endosome biogenesis.";
RL Mol. Biol. Cell 24:1776-1790(2013).
RN [18]
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).
RN [19]
RP STRUCTURE BY NMR OF 419-433 IN COMPLEX WITH EHD1, AND MUTAGENESIS OF
RP 428-GLU--GLU-430.
RX PubMed=20106972; DOI=10.1074/jbc.m109.045666;
RA Kieken F., Sharma M., Jovic M., Giridharan S.S., Naslavsky N., Caplan S.,
RA Sorgen P.L.;
RT "Mechanism for the selective interaction of C-terminal Eps15 homology
RT domain proteins with specific Asn-Pro-Phe-containing partners.";
RL J. Biol. Chem. 285:8687-8694(2010).
RN [20]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-817.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Probable lipid-binding protein with higher affinity for
CC phosphatidic acid, a lipid enriched in recycling endosome membranes. On
CC endosome membranes, may act as a downstream effector of Rab proteins
CC recruiting cytosolic proteins to regulate membrane tubulation. May be
CC involved in a late step of receptor-mediated endocytosis regulating for
CC instance endocytosed-EGF receptor trafficking. Alternatively, may
CC regulate slow endocytic recycling of endocytosed proteins back to the
CC plasma membrane. May indirectly play a role in neurite outgrowth.
CC {ECO:0000269|PubMed:19864458, ECO:0000269|PubMed:20801876,
CC ECO:0000269|PubMed:21795389, ECO:0000269|PubMed:23596323}.
CC -!- SUBUNIT: Homooligomer (Probable). Interacts (via NPF1 motif) with EHD1
CC (via EH domain); the interaction is direct and probably recruits EHD1
CC to membranes. Interacts with EHD3 (via EH domain). Interacts with RAB35
CC (GTP-bound form); the interaction is direct and probably recruits
CC MICALL1 to membranes. Interacts with ACAP2; the interaction is indirect
CC through RAB35. Interacts with RAB8A (GTP-bound form); regulates RAB8A
CC association with recycling endosomes. Interacts with RAB13 (GTP-bound
CC form). Interacts with ARF6 (GTP-bound form). Interacts with PACSIN2
CC (via the SH3 domain). Interacts with DPYSL2.
CC {ECO:0000269|PubMed:19864458, ECO:0000269|PubMed:20106972,
CC ECO:0000269|PubMed:20801876, ECO:0000269|PubMed:21795389,
CC ECO:0000269|PubMed:21951725, ECO:0000269|PubMed:23596323, ECO:0000305}.
CC -!- INTERACTION:
CC Q8N3F8; Q9H4M9: EHD1; NbExp=12; IntAct=EBI-1056885, EBI-490691;
CC Q8N3F8; Q9NZN3: EHD3; NbExp=5; IntAct=EBI-1056885, EBI-2870749;
CC Q8N3F8; Q15286: RAB35; NbExp=2; IntAct=EBI-1056885, EBI-722275;
CC Q8N3F8; Q5ZXN6: ankX; Xeno; NbExp=2; IntAct=EBI-1056885, EBI-26359852;
CC Q8N3F8; O02675: DPYSL2; Xeno; NbExp=2; IntAct=EBI-1056885, EBI-8783505;
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane; Peripheral membrane
CC protein. Late endosome membrane. Note=Localization to late endosomes is
CC actin-dependent. Association to tubular recycling endosomes is
CC regulated by RAB35 and ARF6.
CC -!- DOMAIN: Probably exists in a closed and an opened conformation due to
CC interaction of the C-terminal RAB-binding domain (RBD), also described
CC as bivalent Mical/EHBP Rab binding (bMERB) domain, with the N-terminal
CC calponin-homology (CH) domain. The conformational change is regulated
CC by RAB13 and may modulate MICALL1 interactions with functional
CC partners. {ECO:0000269|PubMed:21795389}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD39036.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ496196; CAD42713.1; -; mRNA.
DR EMBL; CR456437; CAG30323.1; -; mRNA.
DR EMBL; AL022311; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL834373; CAD39036.1; ALT_FRAME; mRNA.
DR EMBL; AL833860; CAD38718.1; -; mRNA.
DR EMBL; AB051455; BAB33338.1; -; mRNA.
DR EMBL; BC001090; AAH01090.2; -; mRNA.
DR EMBL; BK000466; DAA01345.1; -; mRNA.
DR CCDS; CCDS13961.1; -.
DR RefSeq; NP_203744.1; NM_033386.3.
DR PDB; 2KSP; NMR; -; B=419-433.
DR PDBsum; 2KSP; -.
DR AlphaFoldDB; Q8N3F8; -.
DR SMR; Q8N3F8; -.
DR BioGRID; 124504; 89.
DR CORUM; Q8N3F8; -.
DR IntAct; Q8N3F8; 32.
DR MINT; Q8N3F8; -.
DR STRING; 9606.ENSP00000215957; -.
DR GlyGen; Q8N3F8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N3F8; -.
DR PhosphoSitePlus; Q8N3F8; -.
DR BioMuta; MICALL1; -.
DR DMDM; 30173085; -.
DR EPD; Q8N3F8; -.
DR jPOST; Q8N3F8; -.
DR MassIVE; Q8N3F8; -.
DR MaxQB; Q8N3F8; -.
DR PaxDb; Q8N3F8; -.
DR PeptideAtlas; Q8N3F8; -.
DR PRIDE; Q8N3F8; -.
DR ProteomicsDB; 71798; -.
DR Antibodypedia; 26174; 144 antibodies from 21 providers.
DR DNASU; 85377; -.
DR Ensembl; ENST00000215957.10; ENSP00000215957.6; ENSG00000100139.14.
DR GeneID; 85377; -.
DR KEGG; hsa:85377; -.
DR MANE-Select; ENST00000215957.10; ENSP00000215957.6; NM_033386.4; NP_203744.1.
DR UCSC; uc003aui.4; human.
DR CTD; 85377; -.
DR DisGeNET; 85377; -.
DR GeneCards; MICALL1; -.
DR HGNC; HGNC:29804; MICALL1.
DR HPA; ENSG00000100139; Low tissue specificity.
DR MIM; 619563; gene.
DR neXtProt; NX_Q8N3F8; -.
DR OpenTargets; ENSG00000100139; -.
DR PharmGKB; PA162395891; -.
DR VEuPathDB; HostDB:ENSG00000100139; -.
DR eggNOG; ENOG502QWQX; Eukaryota.
DR GeneTree; ENSGT00940000156057; -.
DR HOGENOM; CLU_015382_1_0_1; -.
DR InParanoid; Q8N3F8; -.
DR OMA; GHNKSTH; -.
DR OrthoDB; 377701at2759; -.
DR PhylomeDB; Q8N3F8; -.
DR TreeFam; TF328311; -.
DR PathwayCommons; Q8N3F8; -.
DR SignaLink; Q8N3F8; -.
DR BioGRID-ORCS; 85377; 25 hits in 1077 CRISPR screens.
DR ChiTaRS; MICALL1; human.
DR EvolutionaryTrace; Q8N3F8; -.
DR GeneWiki; MICALL1; -.
DR GenomeRNAi; 85377; -.
DR Pharos; Q8N3F8; Tbio.
DR PRO; PR:Q8N3F8; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q8N3F8; protein.
DR Bgee; ENSG00000100139; Expressed in cervix squamous epithelium and 175 other tissues.
DR ExpressionAtlas; Q8N3F8; baseline and differential.
DR Genevisible; Q8N3F8; HS.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070300; F:phosphatidic acid binding; IDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IMP:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0097320; P:plasma membrane tubulation; IDA:UniProtKB.
DR GO; GO:0036010; P:protein localization to endosome; IMP:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IMP:UniProtKB.
DR GO; GO:0032458; P:slow endocytic recycling; IMP: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:SF44; PTHR23167:SF44; 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 3D-structure; Coiled coil; Endocytosis; Endosome; LIM domain; Membrane;
KW Metal-binding; Phosphoprotein; Protein transport; Reference proteome;
KW Transport; Zinc.
FT CHAIN 1..863
FT /note="MICAL-like protein 1"
FT /id="PRO_0000075848"
FT DOMAIN 2..108
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 162..225
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 671..818
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 119..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..863
FT /note="Mediates the interaction with RAB13 and RAB35 and
FT intramolecular interaction with the CH domain"
FT /evidence="ECO:0000269|PubMed:21795389,
FT ECO:0000269|PubMed:21951725"
FT REGION 700..863
FT /note="Necessary and sufficient to associate with tubular
FT recycling endosome membranes, mediate phosphatidic acid-
FT binding and membrane tubulation"
FT COILED 682..711
FT /evidence="ECO:0000255"
FT COILED 785..830
FT /evidence="ECO:0000255"
FT MOTIF 425..427
FT /note="NPF1"
FT MOTIF 633..635
FT /note="NPF2"
FT COMPBIAS 145..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 497..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 318
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 467
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 469
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 621
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGT6"
FT VARIANT 519
FT /note="A -> S (in dbSNP:rs9610875)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_018262"
FT VARIANT 583
FT /note="P -> L (in dbSNP:rs2272829)"
FT /id="VAR_020258"
FT VARIANT 685
FT /note="H -> R (in dbSNP:rs34834842)"
FT /id="VAR_050158"
FT VARIANT 817
FT /note="E -> K (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036192"
FT MUTAGEN 385..387
FT /note="PLP->ALA: No effect on interaction with PACSIN2.
FT Loss of interaction with PACSIN2; when associated with 480-
FT A--A-483."
FT /evidence="ECO:0000269|PubMed:23596323"
FT MUTAGEN 425..427
FT /note="NPF->APA: Partial loss of interaction with EHD1.
FT Complete loss of interaction with EHD1; when associated
FT with 633-A--A-635."
FT /evidence="ECO:0000269|PubMed:19864458"
FT MUTAGEN 428..430
FT /note="EEE->AAA: Strongly reduces interaction with EHD1."
FT /evidence="ECO:0000269|PubMed:20106972"
FT MUTAGEN 480..483
FT /note="PRAP->ARAA: No effect on interaction with PACSIN2.
FT Loss of interaction with PACSIN2; when associated with 385-
FT A--A-387."
FT /evidence="ECO:0000269|PubMed:23596323"
FT MUTAGEN 633..635
FT /note="NPF->APA: No effect on interaction with EHD1.
FT Complete loss of interaction with EHD1; when associated
FT with 425-A--A-427."
FT /evidence="ECO:0000269|PubMed:19864458"
FT MUTAGEN 721..726
FT /note="MLVDWF->AAAAAA: Altered association with membranes."
FT /evidence="ECO:0000269|PubMed:19864458"
FT CONFLICT 137
FT /note="P -> S (in Ref. 5; BAB33338)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="F -> Y (in Ref. 4; CAD39036)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 863 AA; 93441 MW; 755E3B57C6037292 CRC64;
MAGPRGALLA WCRRQCEGYR GVEIRDLSSS FRDGLAFCAI LHRHRPDLLD FDSLSKDNVF
ENNRLAFEVA EKELGIPALL DPNDMVSMSV PDCLSIMTYV SQYYNHFCSP GQAGVSPPRK
GLAPCSPPSV APTPVEPEDV AQGEELSSGS LSEQGTGQTP SSTCAACQQH VHLVQRYLAD
GRLYHRHCFR CRRCSSTLLP GAYENGPEEG TFVCAEHCAR LGPGTRSGTR PGPFSQPKQQ
HQQQLAEDAK DVPGGGPSSS APAGAEADGP KASPEARPQI PTKPRVPGKL QELASPPAGR
PTPAPRKASE STTPAPPTPR PRSSLQQENL VEQAGSSSLV NGRLHELPVP KPRGTPKPSE
GTPAPRKDPP WITLVQAEPK KKPAPLPPSS SPGPPSQDSR QVENGGTEEV AQPSPTASLE
SKPYNPFEEE EEDKEEEAPA APSLATSPAL GHPESTPKSL HPWYGITPTS SPKTKKRPAP
RAPSASPLAL HASRLSHSEP PSATPSPALS VESLSSESAS QTAGAELLEP PAVPKSSSEP
AVHAPGTPGN PVSLSTNSSL ASSGELVEPR VEQMPQASPG LAPRTRGSSG PQPAKPCSGA
TPTPLLLVGD RSPVPSPGSS SPQLQVKSSC KENPFNRKPS PAASPATKKA TKGSKPVRPP
APGHGFPLIK RKVQADQYIP EEDIHGEMDT IERRLDALEH RGVLLEEKLR GGLNEGREDD
MLVDWFKLIH EKHLLVRRES ELIYVFKQQN LEQRQADVEY ELRCLLNKPE KDWTEEDRAR
EKVLMQELVT LIEQRNAIIN CLDEDRQREE EEDKMLEAMI KKKEFQREAE PEGKKKGKFK
TMKMLKLLGN KRDAKSKSPR DKS
