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Protein

MICAL-like protein 1

Gene

Micall1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. On endosome membranes, may act as a downstream effector of Rab proteins recruiting cytosolic proteins to regulate membrane tubulation. May be involved in a late step of receptor-mediated endocytosis regulating for instance endocytosed-EGF receptor trafficking. Alternatively, may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. May indirectly play a role in neurite outgrowth.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
MICAL-like protein 1
Alternative name(s):
Molecule interacting with Rab13
Short name:
MIRab13
Gene namesi
Name:Micall1
Synonyms:D15Mit260, Kiaa1668, Mirab13
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:105870. Micall1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 870870MICAL-like protein 1PRO_0000075849Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei291 – 2911PhosphoserineBy similarity
Modified residuei305 – 3051PhosphoserineBy similarity
Modified residuei311 – 3111PhosphothreonineCombined sources
Modified residuei314 – 3141PhosphothreonineCombined sources
Modified residuei477 – 4771PhosphothreonineCombined sources
Modified residuei479 – 4791PhosphothreonineBy similarity
Modified residuei480 – 4801PhosphoserineBy similarity
Modified residuei481 – 4811PhosphoserineCombined sources
Modified residuei494 – 4941PhosphoserineCombined sources
Modified residuei496 – 4961PhosphoserineCombined sources
Modified residuei747 – 7471PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BGT6.
MaxQBiQ8BGT6.
PaxDbiQ8BGT6.
PRIDEiQ8BGT6.

PTM databases

iPTMnetiQ8BGT6.
PhosphoSiteiQ8BGT6.

Expressioni

Gene expression databases

BgeeiQ8BGT6.
GenevisibleiQ8BGT6. MM.

Interactioni

Subunit structurei

Homooligomer (Probable). Interacts (via NPF1 motif) with EHD1 (via EH domain); the interaction is direct and probably recruits EHD1 to membranes. Interacts with EHD3 (via EH domain). Interacts with RAB35 (GTP-bound form); the interaction is direct and probably recruits MICALL1 to membranes. Interacts with ACAP2; the interaction is indirect through RAB35. Interacts with RAB8A (GTP-bound form); regulates RAB8A association with recycling endosomes. Interacts with RAB13 (GTP-bound form). Interacts with ARF6 (GTP-bound form). Interacts with PACSIN2 (via the SH3 domain). Interacts with DPYSL2.Curated2 Publications

GO - Molecular functioni

  • identical protein binding Source: MGI
  • Rab GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi205096. 1 interaction.
IntActiQ8BGT6. 1 interaction.
MINTiMINT-4101902.
STRINGi10090.ENSMUSP00000042053.

Structurei

3D structure databases

ProteinModelPortaliQ8BGT6.
SMRiQ8BGT6. Positions 8-115, 153-229.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 105104CHPROSITE-ProRule annotationAdd
BLAST
Domaini163 – 22664LIM zinc-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni659 – 870212RAB-binding domain (RBD); mediates the interaction with RAB13 and RAB35 and intramolecular interaction with the CH domainBy similarityAdd
BLAST
Regioni707 – 870164Necessary and sufficient to associate with tubular recycling endosome membranes, mediate phosphatidic acid-binding and membrane tubulationBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili689 – 72234Sequence analysisAdd
BLAST
Coiled coili806 – 84035Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi421 – 4233NPF1
Motifi640 – 6423NPF2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi277 – 558282Pro-richAdd
BLAST

Domaini

Probably exists in a closed and an opened conformation due to interaction of the C-terminal RAB-binding domain (RBD) with the N-terminal CH (calponin-homology) domain. The conformational change is regulated by RAB13 and may modulate MICALL1 interactions with functional partners (By similarity).By similarity

Sequence similaritiesi

Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
Contains 1 LIM zinc-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, LIM domain

Phylogenomic databases

eggNOGiENOG410IG9K. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118856.
HOGENOMiHOG000290690.
HOVERGENiHBG052475.
InParanoidiQ8BGT6.
KOiK19948.
OMAiEGYRGVD.
OrthoDBiEOG7X3QR0.
TreeFamiTF328311.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
2.10.110.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR022735. DUF3585.
IPR028563. MICAL-L1.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR11915:SF323. PTHR11915:SF323. 3 hits.
PfamiPF00307. CH. 1 hit.
PF12130. DUF3585. 1 hit.
PF00412. LIM. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 1 hit.
SM00132. LIM. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS50021. CH. 1 hit.
PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BGT6-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGPRGALLA WCRRQCEGYR GVDIRDLSSS FRDGLAFCAI LHRHRPDLLD
60 70 80 90 100
FQSLSKENVF ENNRLAFEVA EKELGIPALL DPNDMVSMSV PDCLSIMTYV
110 120 130 140 150
SQYYNHFTSS GQAAASPPKP GKDPAPPSPT STSPAVQPGE EAQGDDLSPD
160 170 180 190 200
SLSEQGKQQP PSSACAACGQ RVHLVQRYLA EGRLYHRHCF RCRQCSSTLV
210 220 230 240 250
PGSYSSGPEE GTFVCAERCT RLGPGSRSGT RLLSQQRQQP AAAEAKDAED
260 270 280 290 300
NDPSLSVAAV AEADRLQASS EVQFHTPTKP PLPSKPQELA SPPGGRPTPA
310 320 330 340 350
PRKASESSAL TPPTPRPRSS LQQDGTVEQS VSSGLVNGRL QEPPVPKPRG
360 370 380 390 400
TPKLSERMAA PRKDPPWITL VQTEPKKKPA PQPPSSGPGP LSQAYRQVED
410 420 430 440 450
GGLEEQTQKS SGTEPEPKPY NPFEEEEEEE GEPAPPVPSP SLAPPVPSPS
460 470 480 490 500
PAPPVPSPAP APSEATPKSL HPWYGITPTS SPKTKKRPAP RAPSASPLAI
510 520 530 540 550
HASRLSHSEP PSATPSPALS VESLSSESSS HTANAEPLEP PAVPKSSSDP
560 570 580 590 600
AVHVPGTPGT SGNSVTPSAN SSLSSSGELG QPSGEQMLQA RTKGSAGTHS
610 620 630 640 650
TKPFSGATPT PFLLAGDRNP APPVGSASPQ LQIKSSCKEN PFNRKPSPSA
660 670 680 690 700
SPTVRKATKG AKPVRPPAPG HGFPLIKRKV QADQYIPEED IYGEMDNIER
710 720 730 740 750
QLDALEHSGV LLEEKLRGGA NEGSEDDMLV DWFKLIHEKH LLVRRESELI
760 770 780 790 800
YVFKQQNLEQ RQADVEFELR CLLNKPEKDW TDEDRAREKV LMQELMTLIE
810 820 830 840 850
QRDAIVNCLD EDRQREEEED KMLETMIKKK DFQREAESDS KKKGKFKTIK
860 870
VLKFLGNKRE AKSKAPGDKS
Length:870
Mass (Da):94,079
Last modified:July 27, 2011 - v3
Checksum:i774D9009CF5CD994
GO
Isoform 2 (identifier: Q8BGT6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-357: Missing.

Show »
Length:513
Mass (Da):55,721
Checksum:i70CD36ACA49CB061
GO
Isoform 3 (identifier: Q8BGT6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     113-133: AAASPPKPGKDPAPPSPTSTS → GERGPSPSGRLPWAVYFFAEQ
     134-870: Missing.

Note: No experimental confirmation available.
Show »
Length:133
Mass (Da):14,995
Checksum:i57E16294FAE64D2A
GO

Sequence cautioni

The sequence BAC98229.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti588 – 5903LQA → PQV in BAC98229 (PubMed:14621295).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 357357Missing in isoform 2. 1 PublicationVSP_009851Add
BLAST
Alternative sequencei113 – 13321AAASP…PTSTS → GERGPSPSGRLPWAVYFFAE Q in isoform 3. 1 PublicationVSP_009852Add
BLAST
Alternative sequencei134 – 870737Missing in isoform 3. 1 PublicationVSP_009853Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129419 mRNA. Translation: BAC98229.1. Different initiation.
AK031386 mRNA. No translation available.
AK076763 mRNA. Translation: BAC36472.1.
AK077217 mRNA. Translation: BAC36689.1.
AL589670 Genomic DNA. No translation available.
CCDSiCCDS49667.1. [Q8BGT6-1]
RefSeqiNP_803412.1. NM_177461.1. [Q8BGT6-1]
XP_006521087.1. XM_006521024.1. [Q8BGT6-2]
UniGeneiMm.196480.

Genome annotation databases

EnsembliENSMUST00000040320; ENSMUSP00000042053; ENSMUSG00000033039. [Q8BGT6-1]
GeneIDi27008.
KEGGimmu:27008.
UCSCiuc007wsm.2. mouse. [Q8BGT6-3]
uc007wso.2. mouse. [Q8BGT6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129419 mRNA. Translation: BAC98229.1. Different initiation.
AK031386 mRNA. No translation available.
AK076763 mRNA. Translation: BAC36472.1.
AK077217 mRNA. Translation: BAC36689.1.
AL589670 Genomic DNA. No translation available.
CCDSiCCDS49667.1. [Q8BGT6-1]
RefSeqiNP_803412.1. NM_177461.1. [Q8BGT6-1]
XP_006521087.1. XM_006521024.1. [Q8BGT6-2]
UniGeneiMm.196480.

3D structure databases

ProteinModelPortaliQ8BGT6.
SMRiQ8BGT6. Positions 8-115, 153-229.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205096. 1 interaction.
IntActiQ8BGT6. 1 interaction.
MINTiMINT-4101902.
STRINGi10090.ENSMUSP00000042053.

PTM databases

iPTMnetiQ8BGT6.
PhosphoSiteiQ8BGT6.

Proteomic databases

EPDiQ8BGT6.
MaxQBiQ8BGT6.
PaxDbiQ8BGT6.
PRIDEiQ8BGT6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040320; ENSMUSP00000042053; ENSMUSG00000033039. [Q8BGT6-1]
GeneIDi27008.
KEGGimmu:27008.
UCSCiuc007wsm.2. mouse. [Q8BGT6-3]
uc007wso.2. mouse. [Q8BGT6-1]

Organism-specific databases

CTDi85377.
MGIiMGI:105870. Micall1.
RougeiSearch...

Phylogenomic databases

eggNOGiENOG410IG9K. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118856.
HOGENOMiHOG000290690.
HOVERGENiHBG052475.
InParanoidiQ8BGT6.
KOiK19948.
OMAiEGYRGVD.
OrthoDBiEOG7X3QR0.
TreeFamiTF328311.

Miscellaneous databases

ChiTaRSiMicall1. mouse.
PROiQ8BGT6.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BGT6.
GenevisibleiQ8BGT6. MM.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
2.10.110.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR022735. DUF3585.
IPR028563. MICAL-L1.
IPR001781. Znf_LIM.
[Graphical view]
PANTHERiPTHR11915:SF323. PTHR11915:SF323. 3 hits.
PfamiPF00307. CH. 1 hit.
PF12130. DUF3585. 1 hit.
PF00412. LIM. 1 hit.
[Graphical view]
SMARTiSM00033. CH. 1 hit.
SM00132. LIM. 1 hit.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS50021. CH. 1 hit.
PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Embryonic tail.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The interaction of JRAB/MICAL-L2 with Rab8 and Rab13 coordinates the assembly of tight junctions and adherens junctions."
    Yamamura R., Nishimura N., Nakatsuji H., Arase S., Sasaki T.
    Mol. Biol. Cell 19:971-983(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RAB8A.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-311; THR-314; THR-477; SER-481; SER-494; SER-496 AND SER-747, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas and Spleen.
  6. "Rab35 establishes the EHD1-association site by coordinating two distinct effectors during neurite outgrowth."
    Kobayashi H., Fukuda M.
    J. Cell Sci. 126:2424-2435(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEURITE OUTGROWTH, INTERACTION WITH ACAP2; EHD1 AND RAB35.

Entry informationi

Entry nameiMILK1_MOUSE
AccessioniPrimary (citable) accession number: Q8BGT6
Secondary accession number(s): E9QKJ4, Q8BJ60
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.