MILK1_MOUSE
ID MILK1_MOUSE Reviewed; 870 AA.
AC Q8BGT6; E9QKJ4; Q8BJ60;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=MICAL-like protein 1;
DE AltName: Full=Molecule interacting with Rab13;
DE Short=MIRab13;
GN Name=Micall1; Synonyms=D15Mit260, Kiaa1668, Mirab13;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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]
RP INTERACTION WITH RAB8A.
RX PubMed=18094055; DOI=10.1091/mbc.e07-06-0551;
RA Yamamura R., Nishimura N., Nakatsuji H., Arase S., Sasaki T.;
RT "The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the
RT assembly of tight junctions and adherens junctions.";
RL Mol. Biol. Cell 19:971-983(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311; THR-314; THR-477;
RP SER-481; SER-494; SER-496 AND SER-747, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
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 [6]
RP FUNCTION IN NEURITE OUTGROWTH, AND INTERACTION WITH ACAP2; EHD1 AND RAB35.
RX PubMed=23572513; DOI=10.1242/jcs.117846;
RA Kobayashi H., Fukuda M.;
RT "Rab35 establishes the EHD1-association site by coordinating two distinct
RT effectors during neurite outgrowth.";
RL J. Cell Sci. 126:2424-2435(2013).
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:23572513}.
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:18094055, ECO:0000269|PubMed:23572513,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Late endosome membrane
CC {ECO:0000250}. Note=Localization to late endosomes is actin-dependent.
CC Association to tubular recycling endosomes is regulated by RAB35 and
CC ARF6 (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BGT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BGT6-2; Sequence=VSP_009851;
CC Name=3;
CC IsoId=Q8BGT6-3; Sequence=VSP_009852, VSP_009853;
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 partners
CC (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98229.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK129419; BAC98229.1; ALT_INIT; mRNA.
DR EMBL; AK031386; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK076763; BAC36472.1; -; mRNA.
DR EMBL; AK077217; BAC36689.1; -; mRNA.
DR EMBL; AL589670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49667.1; -. [Q8BGT6-1]
DR RefSeq; NP_803412.1; NM_177461.1. [Q8BGT6-1]
DR RefSeq; XP_006521087.1; XM_006521024.1. [Q8BGT6-2]
DR AlphaFoldDB; Q8BGT6; -.
DR SMR; Q8BGT6; -.
DR BioGRID; 205096; 6.
DR STRING; 10090.ENSMUSP00000042053; -.
DR iPTMnet; Q8BGT6; -.
DR PhosphoSitePlus; Q8BGT6; -.
DR EPD; Q8BGT6; -.
DR jPOST; Q8BGT6; -.
DR MaxQB; Q8BGT6; -.
DR PaxDb; Q8BGT6; -.
DR PeptideAtlas; Q8BGT6; -.
DR PRIDE; Q8BGT6; -.
DR ProteomicsDB; 295603; -. [Q8BGT6-1]
DR ProteomicsDB; 295604; -. [Q8BGT6-2]
DR ProteomicsDB; 295605; -. [Q8BGT6-3]
DR Antibodypedia; 26174; 144 antibodies from 21 providers.
DR Ensembl; ENSMUST00000040320; ENSMUSP00000042053; ENSMUSG00000033039. [Q8BGT6-1]
DR GeneID; 27008; -.
DR KEGG; mmu:27008; -.
DR UCSC; uc007wsm.2; mouse. [Q8BGT6-3]
DR UCSC; uc007wso.2; mouse. [Q8BGT6-1]
DR CTD; 85377; -.
DR MGI; MGI:105870; Micall1.
DR VEuPathDB; HostDB:ENSMUSG00000033039; -.
DR eggNOG; ENOG502QWQX; Eukaryota.
DR GeneTree; ENSGT00940000156057; -.
DR HOGENOM; CLU_015382_1_0_1; -.
DR InParanoid; Q8BGT6; -.
DR OMA; GHNKSTH; -.
DR OrthoDB; 377701at2759; -.
DR PhylomeDB; Q8BGT6; -.
DR TreeFam; TF328311; -.
DR BioGRID-ORCS; 27008; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Micall1; mouse.
DR PRO; PR:Q8BGT6; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8BGT6; protein.
DR Bgee; ENSMUSG00000033039; Expressed in ascending aorta and 223 other tissues.
DR ExpressionAtlas; Q8BGT6; baseline and differential.
DR Genevisible; Q8BGT6; MM.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070300; F:phosphatidic acid binding; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISO:MGI.
DR GO; GO:0032456; P:endocytic recycling; ISS:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0031175; P:neuron projection development; IMP:UniProtKB.
DR GO; GO:0097320; P:plasma membrane tubulation; ISS:UniProtKB.
DR GO; GO:0036010; P:protein localization to endosome; ISS:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; ISS:UniProtKB.
DR GO; GO:0032458; P:slow endocytic recycling; 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: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 Alternative splicing; Coiled coil; Endocytosis; Endosome; LIM domain;
KW Membrane; Metal-binding; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Zinc.
FT CHAIN 1..870
FT /note="MICAL-like protein 1"
FT /id="PRO_0000075849"
FT DOMAIN 2..108
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 163..226
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 678..825
FT /note="bMERB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01195"
FT REGION 110..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 659..870
FT /note="Mediates the interaction with RAB13 and RAB35 and
FT intramolecular interaction with the CH domain"
FT /evidence="ECO:0000250"
FT REGION 707..870
FT /note="Necessary and sufficient to associate with tubular
FT recycling endosome membranes, mediate phosphatidic acid-
FT binding and membrane tubulation"
FT /evidence="ECO:0000250"
FT COILED 689..722
FT /evidence="ECO:0000255"
FT COILED 806..840
FT /evidence="ECO:0000255"
FT MOTIF 421..423
FT /note="NPF1"
FT MOTIF 640..642
FT /note="NPF2"
FT COMPBIAS 119..133
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..299
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..465
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 305
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 311
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 314
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 477
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 479
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3F8"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..357
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009851"
FT VAR_SEQ 113..133
FT /note="AAASPPKPGKDPAPPSPTSTS -> GERGPSPSGRLPWAVYFFAEQ (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009852"
FT VAR_SEQ 134..870
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009853"
FT CONFLICT 588..590
FT /note="LQA -> PQV (in Ref. 1; BAC98229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 870 AA; 94079 MW; 774D9009CF5CD994 CRC64;
MAGPRGALLA WCRRQCEGYR GVDIRDLSSS FRDGLAFCAI LHRHRPDLLD FQSLSKENVF
ENNRLAFEVA EKELGIPALL DPNDMVSMSV PDCLSIMTYV SQYYNHFTSS GQAAASPPKP
GKDPAPPSPT STSPAVQPGE EAQGDDLSPD SLSEQGKQQP PSSACAACGQ RVHLVQRYLA
EGRLYHRHCF RCRQCSSTLV PGSYSSGPEE GTFVCAERCT RLGPGSRSGT RLLSQQRQQP
AAAEAKDAED NDPSLSVAAV AEADRLQASS EVQFHTPTKP PLPSKPQELA SPPGGRPTPA
PRKASESSAL TPPTPRPRSS LQQDGTVEQS VSSGLVNGRL QEPPVPKPRG TPKLSERMAA
PRKDPPWITL VQTEPKKKPA PQPPSSGPGP LSQAYRQVED GGLEEQTQKS SGTEPEPKPY
NPFEEEEEEE GEPAPPVPSP SLAPPVPSPS PAPPVPSPAP APSEATPKSL HPWYGITPTS
SPKTKKRPAP RAPSASPLAI HASRLSHSEP PSATPSPALS VESLSSESSS HTANAEPLEP
PAVPKSSSDP AVHVPGTPGT SGNSVTPSAN SSLSSSGELG QPSGEQMLQA RTKGSAGTHS
TKPFSGATPT PFLLAGDRNP APPVGSASPQ LQIKSSCKEN PFNRKPSPSA SPTVRKATKG
AKPVRPPAPG HGFPLIKRKV QADQYIPEED IYGEMDNIER QLDALEHSGV LLEEKLRGGA
NEGSEDDMLV DWFKLIHEKH LLVRRESELI YVFKQQNLEQ RQADVEFELR CLLNKPEKDW
TDEDRAREKV LMQELMTLIE QRDAIVNCLD EDRQREEEED KMLETMIKKK DFQREAESDS
KKKGKFKTIK VLKFLGNKRE AKSKAPGDKS
