Q8VDP3 (MICA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein-methionine sulfoxide oxidase MICAL1
EC=1.14.13.-

Alternative name(s):
Molecule interacting with CasL protein 1
Short name=MICAL-1
NEDD9-interacting protein with calponin homology and LIM domains

Gene names

Name:	Mical1
Synonyms:	Mical, Nical

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1048 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin. Acts by modifying actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization. Acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments By similarity. Also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L; acts by antagonizing STK38 and STK38L activation by MST1/STK4. Ref.4
Catalytic activity	[protein]-methionine + NADPH + O2 = [protein]-methionine-sulfoxide + NADP+ + H2O.
Cofactor	FAD.
Subunit structure	Associates with the SH3 domain of NEDD9. Interacts with VIM and PLXNA3. Interacts with RAB1B By similarity. Interacts with STK38 and STK38L. Ref.4
Subcellular location	Cytoplasm By similarity. Cytoplasm › cytoskeleton By similarity.
Domain	The C-terminal coiled coil part contains the plexin-interacting region.
Sequence similarities	Belongs to the Mical family. Contains 1 CH (calponin-homology) domain. Contains 1 LIM zinc-binding domain.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing
Domain	Coiled coil LIM domain
Ligand	Actin-binding FAD Flavoprotein Metal-binding NADP Zinc
Molecular function	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament depolymerization Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of apoptotic process Inferred from mutant phenotype Ref.4. Source: UniProtKB negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from mutant phenotype Ref.4. Source: UniProtKB negative regulation of protein phosphorylation Inferred from mutant phenotype Ref.4. Source: UniProtKB
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	FAD binding Inferred from sequence or structural similarity. Source: UniProtKB SH3 domain binding Inferred from sequence or structural similarity. Source: UniProtKB actin binding Inferred from sequence or structural similarity. Source: UniProtKB oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen Inferred from sequence or structural similarity. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Stk38	Q91VJ4	9	EBI-4394891,EBI-2527046
Stk38l	A4GW50	2	EBI-4394891,EBI-4404035	From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8VDP3-1)

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.

Isoform 2 (identifier: Q8VDP3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     87-159: Missing.

Isoform 3 (identifier: Q8VDP3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     192-192: S → D

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1048

1048

Protein-methionine sulfoxide oxidase MICAL1

PRO_0000075843

Regions

Domain

507 – 608

102

CH

Domain

681 – 743

63

LIM zinc-binding

Nucleotide binding

95 – 123

29

FAD

Region

1 – 489

489

Monooxygenase domain

Coiled coil

847 – 867

21

Potential

Coiled coil

906 – 949

44

Potential

Coiled coil

974 – 1031

58

Potential

Sites

Binding site

95

1

FAD

Binding site

114

1

FAD

Binding site

116

1

FAD

Binding site

121

1

FAD

Binding site

123

1

FAD

Binding site

393

1

FAD

Amino acid modifications

Modified residue

616

1

Phosphoserine By similarity

Natural variations

Alternative sequence

87 – 159

73

Missing in isoform 2.

VSP_042591

Alternative sequence

192

1

S → D in isoform 3.

VSP_042592

Experimental info

Sequence conflict

871

1

P → H in BAE35027. Ref.1

Secondary structure

1

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1048

Helix Strand Turn

Details...

Helix

9 – 19

11

Helix

23 – 37

15

Helix

44 – 53

10

Turn

58 – 60

3

Helix

61 – 71

11

Helix

74 – 79

6

Turn

80 – 84

5

Beta strand

86 – 90

5

Helix

94 – 105

12

Beta strand

109 – 115

7

Beta strand

124 – 126

3

Helix

129 – 136

8

Turn

137 – 139

3

Helix

140 – 143

4

Turn

145 – 148

4

Beta strand

154 – 156

3

Helix

157 – 170

14

Beta strand

174 – 178

5

Beta strand

180 – 185

6

Beta strand

194 – 200

7

Helix

204 – 207

4

Beta strand

211 – 216

6

Beta strand

228 – 233

6

Beta strand

238 – 245

8

Helix

250 – 253

4

Turn

263 – 266

4

Helix

269 – 277

9

Beta strand

281 – 298

18

Helix

300 – 305

6

Beta strand

308 – 311

4

Helix

316 – 319

4

Turn

322 – 324

3

Helix

327 – 341

15

Turn

342 – 346

5

Beta strand

357 – 359

3

Beta strand

361 – 365

5

Beta strand

367 – 373

7

Beta strand

375 – 381

7

Beta strand

384 – 390

7

Helix

392 – 394

3

Helix

400 – 402

3

Helix

405 – 424

20

Helix

429 – 440

12

Helix

441 – 445

5

Turn

448 – 450

3

Helix

455 – 457

3

Helix

462 – 464

3

Beta strand

466 – 468

3

Helix

476 – 482

7

Beta strand

483 – 485

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: C31A392A4AE222FC	FASTA	1,048	116,785
	10 20 30 40 50 60 MASPASTNPA HDHFETFVQA QLCQDVLSSF QGLCRALGVE SGGGLSQYHK IKAQLNYWSA 70 80 90 100 110 120 KSLWAKLDKR ASQPVYQQGQ ACTNTKCLVV GAGPCGLRAA VELALLGARV VLVEKRIKFS 130 140 150 160 170 180 RHNVLHLWPF TIHDLRALGA KKFYGRFCTG TLDHISIRQL QLLLLKVALL LGVEIHWGVK 190 200 210 220 230 240 FTGLQPPPRK GSGWRAQLQP NPPAQLASYE FDVLISAAGG KFVPEGFTIR EMRGKLAIGI 250 260 270 280 290 300 TANFVNGRTV EETQVPEISG VARIYNQKFF QSLLKATGID LENIVYYKDE THYFVMTAKK 310 320 330 340 350 360 QCLLRLGVLR QDLSETDQLL GKANVVPEAL QRFARAAADF ATHGKLGKLE FAQDARGRPD 370 380 390 400 410 420 VAAFDFTSMM RAESSARVQE KHGARLLLGL VGDCLVEPFW PLGTGVARGF LAAFDAAWMV 430 440 450 460 470 480 KRWAEGAGPL EVLAERESLY QLLSQTSPEN MHRNVAQYGL DPATRYPNLN LRAVTPNQVQ 490 500 510 520 530 540 DLYDMMDKEH AQRKSDEPDS RKTTTGSAGT EELLHWCQEQ TAGFPGVHVT DFSSSWADGL 550 560 570 580 590 600 ALCALVHHLQ PGLLEPSELQ GMGALEATTW ALRVAEHELG ITPVLSAQAV MAGSDPLGLI 610 620 630 640 650 660 AYLSHFHSAF KNTSHSSGLV SQPSGTPSAI LFLGKLQRSL QRTRAKVDEE TPSTEEPPVS 670 680 690 700 710 720 EPSMSPNTPE LSEHQEAGAE ELCELCGKHL YILERFCVDG HFFHRSCFCC HTCEATLWPG 730 740 750 760 770 780 GYGQHPGDGH FYCLQHLPQE DQKEADNNGS LESQELPTPG DSNMQPDPSS PPVTRVSPVP 790 800 810 820 830 840 SPSQPARRLI RLSSLERLRL SSLNIIPDSG AEPPPKPPRS CSDLARESLK SSFVGWGVPV 850 860 870 880 890 900 QAPQVPEAIE KGDDEEEEEE EEEEEEEPLP PLEPELEQTL LTLAKNPGAM TKYPTWRRTL 910 920 930 940 950 960 MRRAKEEEMK RFCKAQAIQR RLNEIEATMR ELEAEGTKLE LALRKESSSP EQQKKLWLDQ 970 980 990 1000 1010 1020 LLRLIQKKNS LVTEEAELMI TVQELDLEEK QRQLDHELRG YMNREETMKT EADLQSENQV 1030 1040 LRKLLEVVNQ RDALIQFQEE RRLREMPA
	Isoform 2 [UniParc]. Checksum: B2D2BF964B034CBC	FASTA	975	108,692
	10 20 30 40 50 60 MASPASTNPA HDHFETFVQA QLCQDVLSSF QGLCRALGVE SGGGLSQYHK IKAQLNYWSA 70 80 90 100 110 120 KSLWAKLDKR ASQPVYQQGQ ACTNTKLQLL LLKVALLLGV EIHWGVKFTG LQPPPRKGSG 130 140 150 160 170 180 WRAQLQPNPP AQLASYEFDV LISAAGGKFV PEGFTIREMR GKLAIGITAN FVNGRTVEET 190 200 210 220 230 240 QVPEISGVAR IYNQKFFQSL LKATGIDLEN IVYYKDETHY FVMTAKKQCL LRLGVLRQDL 250 260 270 280 290 300 SETDQLLGKA NVVPEALQRF ARAAADFATH GKLGKLEFAQ DARGRPDVAA FDFTSMMRAE 310 320 330 340 350 360 SSARVQEKHG ARLLLGLVGD CLVEPFWPLG TGVARGFLAA FDAAWMVKRW AEGAGPLEVL 370 380 390 400 410 420 AERESLYQLL SQTSPENMHR NVAQYGLDPA TRYPNLNLRA VTPNQVQDLY DMMDKEHAQR 430 440 450 460 470 480 KSDEPDSRKT TTGSAGTEEL LHWCQEQTAG FPGVHVTDFS SSWADGLALC ALVHHLQPGL 490 500 510 520 530 540 LEPSELQGMG ALEATTWALR VAEHELGITP VLSAQAVMAG SDPLGLIAYL SHFHSAFKNT 550 560 570 580 590 600 SHSSGLVSQP SGTPSAILFL GKLQRSLQRT RAKVDEETPS TEEPPVSEPS MSPNTPELSE 610 620 630 640 650 660 HQEAGAEELC ELCGKHLYIL ERFCVDGHFF HRSCFCCHTC EATLWPGGYG QHPGDGHFYC 670 680 690 700 710 720 LQHLPQEDQK EADNNGSLES QELPTPGDSN MQPDPSSPPV TRVSPVPSPS QPARRLIRLS 730 740 750 760 770 780 SLERLRLSSL NIIPDSGAEP PPKPPRSCSD LARESLKSSF VGWGVPVQAP QVPEAIEKGD 790 800 810 820 830 840 DEEEEEEEEE EEEEPLPPLE PELEQTLLTL AKNPGAMTKY PTWRRTLMRR AKEEEMKRFC 850 860 870 880 890 900 KAQAIQRRLN EIEATMRELE AEGTKLELAL RKESSSPEQQ KKLWLDQLLR LIQKKNSLVT 910 920 930 940 950 960 EEAELMITVQ ELDLEEKQRQ LDHELRGYMN REETMKTEAD LQSENQVLRK LLEVVNQRDA 970 LIQFQEERRL REMPA
	Isoform 3 [UniParc]. Checksum: AF50CC8B1FBBBAE2	FASTA	1,048	116,813
	10 20 30 40 50 60 MASPASTNPA HDHFETFVQA QLCQDVLSSF QGLCRALGVE SGGGLSQYHK IKAQLNYWSA 70 80 90 100 110 120 KSLWAKLDKR ASQPVYQQGQ ACTNTKCLVV GAGPCGLRAA VELALLGARV VLVEKRIKFS 130 140 150 160 170 180 RHNVLHLWPF TIHDLRALGA KKFYGRFCTG TLDHISIRQL QLLLLKVALL LGVEIHWGVK 190 200 210 220 230 240 FTGLQPPPRK GDGWRAQLQP NPPAQLASYE FDVLISAAGG KFVPEGFTIR EMRGKLAIGI 250 260 270 280 290 300 TANFVNGRTV EETQVPEISG VARIYNQKFF QSLLKATGID LENIVYYKDE THYFVMTAKK 310 320 330 340 350 360 QCLLRLGVLR QDLSETDQLL GKANVVPEAL QRFARAAADF ATHGKLGKLE FAQDARGRPD 370 380 390 400 410 420 VAAFDFTSMM RAESSARVQE KHGARLLLGL VGDCLVEPFW PLGTGVARGF LAAFDAAWMV 430 440 450 460 470 480 KRWAEGAGPL EVLAERESLY QLLSQTSPEN MHRNVAQYGL DPATRYPNLN LRAVTPNQVQ 490 500 510 520 530 540 DLYDMMDKEH AQRKSDEPDS RKTTTGSAGT EELLHWCQEQ TAGFPGVHVT DFSSSWADGL 550 560 570 580 590 600 ALCALVHHLQ PGLLEPSELQ GMGALEATTW ALRVAEHELG ITPVLSAQAV MAGSDPLGLI 610 620 630 640 650 660 AYLSHFHSAF KNTSHSSGLV SQPSGTPSAI LFLGKLQRSL QRTRAKVDEE TPSTEEPPVS 670 680 690 700 710 720 EPSMSPNTPE LSEHQEAGAE ELCELCGKHL YILERFCVDG HFFHRSCFCC HTCEATLWPG 730 740 750 760 770 780 GYGQHPGDGH FYCLQHLPQE DQKEADNNGS LESQELPTPG DSNMQPDPSS PPVTRVSPVP 790 800 810 820 830 840 SPSQPARRLI RLSSLERLRL SSLNIIPDSG AEPPPKPPRS CSDLARESLK SSFVGWGVPV 850 860 870 880 890 900 QAPQVPEAIE KGDDEEEEEE EEEEEEEPLP PLEPELEQTL LTLAKNPGAM TKYPTWRRTL 910 920 930 940 950 960 MRRAKEEEMK RFCKAQAIQR RLNEIEATMR ELEAEGTKLE LALRKESSSP EQQKKLWLDQ 970 980 990 1000 1010 1020 LLRLIQKKNS LVTEEAELMI TVQELDLEEK QRQLDHELRG YMNREETMKT EADLQSENQV 1030 1040 LRKLLEVVNQ RDALIQFQEE RRLREMPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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 1 AND 2). Strain: C57BL/6J and NOD.
[2]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Mammary tumor.
[4]	"MICAL-1 is a negative regulator of MST-NDR kinase signaling and apoptosis." Zhou Y., Adolfs Y., Pijnappel W.W., Fuller S.J., Van der Schors R.C., Li K.W., Sugden P.H., Smit A.B., Hergovich A., Pasterkamp R.J. Mol. Cell. Biol. 31:3603-3615(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH STK38 AND STK38L.
[5]	"High-resolution structure of the catalytic region of MICAL (molecule interacting with CasL), a multidomain flavoenzyme-signaling molecule." Siebold C., Berrow N., Walter T.S., Harlos K., Owens R.J., Stuart D.I., Terman J.R., Kolodkin A.L., Pasterkamp R.J., Jones E.Y. Proc. Natl. Acad. Sci. U.S.A. 102:16836-16841(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 1-489 IN COMPLEX WITH FAD.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK159369 mRNA. Translation: BAE35027.1.
AK170881 mRNA. Translation: BAE42090.1.
AK171234 mRNA. Translation: BAE42330.1.
AK171411 mRNA. Translation: BAE42437.1.
AK171429 mRNA. Translation: BAE42447.1.
AK171479 mRNA. Translation: BAE42481.1.
AC153360 Genomic DNA. No translation available.
BC021477 mRNA. Translation: AAH21477.1.
BC034682 mRNA. Translation: AAH34682.1.

IPI

IPI00116371.

RefSeq

NP_001157905.1. NM_001164433.1.
NP_612188.1. NM_138315.2.

UniGene

Mm.290431.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BRA	X-ray	2.00	A/B	1-484	[»]
2BRY	X-ray	1.45	A/B	1-489	[»]
2C4C	X-ray	2.90	A/B	1-489	[»]

ProteinModelPortal

Q8VDP3.

SMR

Q8VDP3. Positions 7-489, 506-612, 673-741.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8VDP3. 4 interactions.

STRING

10090.ENSMUSP00000019967.

PTM databases

PhosphoSite

Q8VDP3.

Proteomic databases

PaxDb

Q8VDP3.

PRIDE

Q8VDP3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000019967; ENSMUSP00000019967; ENSMUSG00000019823.
ENSMUST00000099934; ENSMUSP00000097519; ENSMUSG00000019823.
ENSMUST00000119962; ENSMUSP00000113783; ENSMUSG00000019823.

GeneID

171580.

KEGG

mmu:171580.

Organism-specific databases

CTD

64780.

MGI

MGI:2385847. Mical1.

Phylogenomic databases

eggNOG

COG5069.

GeneTree

ENSGT00640000091174.

HOGENOM

HOG000047263.

HOVERGEN

HBG052474.

OMA

QEKHGAR.

Gene expression databases

ArrayExpress

Q8VDP3.

Bgee

Q8VDP3.

Genevestigator

Q8VDP3.

GermOnline

ENSMUSG00000019823. Mus musculus.

Family and domain databases

Gene3D

1.10.418.10. 1 hit.
2.10.110.10. 1 hit.

InterPro

IPR001715. CH-domain.
IPR022735. DUF3585.
IPR002938. mOase_FAD-bd.
IPR001781. Znf_LIM.
[Graphical view]

Pfam

PF00307. CH. 1 hit.
PF12130. DUF3585. 1 hit.
PF01494. FAD_binding_3. 1 hit.
PF00412. LIM. 1 hit.
[Graphical view]

SMART

SM00033. CH. 1 hit.
SM00132. LIM. 1 hit.
[Graphical view]

SUPFAM

SSF47576. Calponin-homology. 1 hit.

PROSITE

PS50021. CH. 1 hit.
PS00478. LIM_DOMAIN_1. 1 hit.
PS50023. LIM_DOMAIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MICAL1. mouse.

EvolutionaryTrace

Q8VDP3.

NextBio

371076.

SOURCE

Search...

Entry information

Entry name

MICA1_MOUSE

Accession

Primary (citable) accession number: Q8VDP3
Secondary accession number(s): D3Z4C6 , E9PXR1, Q3TB77, Q3TBH9, Q3TX89

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	March 1, 2002
Last modified:	May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program