Q8TDZ2 (MICA1_HUMAN) 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

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1067 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 Probable. Acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. 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.12 Ref.14
Catalytic activity	[protein]-methionine + NADPH + O2 = [protein]-methionine-sulfoxide + NADP+ + H2O.
Cofactor	FAD. Ref.14
Subunit structure	Interacts with STK38 and STK38L By similarity. Associates with the SH3 domain of NEDD9. Interacts with VIM and PLXNA3. Interacts with RAB1B. Ref.1 Ref.8 Ref.9 Ref.10
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton Ref.1 Ref.9 Ref.10.
Tissue specificity	Expressed in the thymus, lung, spleen, kidney, testis and hematopoietic cells. Ref.1
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.
Biophysicochemical properties	Kinetic parameters: KM=4.7 µM for F-actin (at saturing NADPH concentration) Ref.14

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
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 direct assay Ref.14. Source: UniProtKB negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of protein phosphorylation Inferred from electronic annotation. Source: Compara signal transduction Non-traceable author statement Ref.1. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay Ref.1. Source: UniProtKB intermediate filament Non-traceable author statement Ref.1. Source: UniProtKB
Molecular_function	FAD binding Inferred from direct assay Ref.14. Source: UniProtKB actin binding Inferred from direct assay Ref.14. 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 direct assay Ref.14. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8TDZ2-1)

Also known as: MICAL-1a;

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: Q8TDZ2-2)

Also known as: MICAL-1b;

The sequence of this isoform differs from the canonical sequence as follows:
     312-397: Missing.

Isoform 3 (identifier: Q8TDZ2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-735: Missing.
     736-768: YEQHPGDGHFYCLQHLPQTDHKAEGSDRGPESP → MPRLTFAPKGWPHPPTSLHPGQVTDQTTWWLFQ

Note: No experimental confirmation available.

Isoform 4 (identifier: Q8TDZ2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MSCLSHSSLPSCCPPQEASM

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1067

1067

Protein-methionine sulfoxide oxidase MICAL1

PRO_0000075842

Regions

Domain

508 – 609

102

CH

Domain

695 – 757

63

LIM zinc-binding

Nucleotide binding

95 – 123

29

FAD By similarity

Region

1 – 489

489

Monooxygenase domain By similarity

Coiled coil

646 – 666

21

Potential

Coiled coil

919 – 962

44

Potential

Coiled coil

999 – 1027

29

Potential

Sites

Binding site

95

1

FAD By similarity

Binding site

114

1

FAD By similarity

Binding site

116

1

FAD By similarity

Binding site

121

1

FAD By similarity

Binding site

123

1

FAD By similarity

Binding site

393

1

FAD By similarity

Amino acid modifications

Modified residue

617

1

Phosphoserine Ref.13

Modified residue

872

1

Phosphoserine Ref.11 Ref.16

Modified residue

875

1

Phosphoserine Ref.13 Ref.16

Modified residue

876

1

Phosphoserine Ref.13 Ref.16

Natural variations

Alternative sequence

1 – 735

735

Missing in isoform 3.

VSP_009637

Alternative sequence

1

1

M → MSCLSHSSLPSCCPPQEASM in isoform 4.

VSP_042590

Alternative sequence

312 – 397

86

Missing in isoform 2.

VSP_009639

Alternative sequence

736 – 768

33

YEQHP…GPESP → MPRLTFAPKGWPHPPTSLHP GQVTDQTTWWLFQ in isoform 3.

VSP_009638

Natural variant

12

1

A → S.
Corresponds to variant rs4946977 [ dbSNP | Ensembl ].

VAR_067063

Natural variant

12

1

A → T.
Corresponds to variant rs4946977 [ dbSNP | Ensembl ].

VAR_050153

Natural variant

153

1

D → A.
Corresponds to variant rs34726911 [ dbSNP | Ensembl ].

VAR_050154

Natural variant

195

1

R → H.
Corresponds to variant rs34699467 [ dbSNP | Ensembl ].

VAR_067064

Natural variant

309

1

L → M in a breast cancer sample; somatic mutation. Ref.20

VAR_036191

Natural variant

453

1

R → C. Ref.6
Corresponds to variant rs17854785 [ dbSNP | Ensembl ].

VAR_067065

Natural variant

624

1

A → T. Ref.6
Corresponds to variant rs17850590 [ dbSNP | Ensembl ].

VAR_067066

Natural variant

758

1

A → E.
Corresponds to variant rs9320288 [ dbSNP | Ensembl ].

VAR_017903

Natural variant

758

1

A → K Requires 2 nucleotide substitutions. Ref.1 Ref.3 Ref.6
Corresponds to variant rs35260632 [ dbSNP | Ensembl ].

VAR_067067

Natural variant

758

1

A → S.
Corresponds to variant rs59056467 [ dbSNP | Ensembl ].

VAR_067068

Natural variant

758

1

A → T.
Corresponds to variant rs59056467 [ dbSNP | Ensembl ].

VAR_061355

Experimental info

Sequence conflict

767

1

S → C in BAB15124. Ref.3

Sequence conflict

816

1

L → S in BAH12301. Ref.3

Sequence conflict

877

1

E → V in BAH12301. Ref.3

Sequence conflict

887

1

S → L in CAB59266. Ref.7

Sequence conflict

981

1

K → N in BAB13949. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

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.

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.

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.

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.

.

.

.

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.

.

.

.

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.

1067

Helix Strand Turn

Details...

Helix

511 – 524

14

Turn

533 – 538

6

Helix

541 – 550

10

Helix

552 – 554

3

Helix

560 – 562

3

Helix

565 – 578

14

Helix

588 – 593

6

Helix

597 – 610

14

Beta strand

698 – 700

3

Turn

706 – 708

3

Turn

719 – 721

3

Beta strand

725 – 727

3

Beta strand

735 – 737

3

Turn

740 – 742

3

Turn

748 – 750

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (MICAL-1a) [UniParc]. Last modified March 15, 2004. Version 2. Checksum: 78C1BBF3E3CCD56B	FASTA	1,067	117,875
	10 20 30 40 50 60 MASPTSTNPA HAHFESFLQA QLCQDVLSSF QELCGALGLE PGGGLPQYHK IKDQLNYWSA 70 80 90 100 110 120 KSLWTKLDKR AGQPVYQQGR ACTSTKCLVV GAGPCGLRVA VELALLGARV VLVEKRTKFS 130 140 150 160 170 180 RHNVLHLWPF TIHDLRALGA KKFYGRFCTG TLDHISIRQL QLLLLKVALL LGVEIHWGVT 190 200 210 220 230 240 FTGLQPPPRK GSGWRAQLQP NPPAQLANYE FDVLISAAGG KFVPEGFKVR EMRGKLAIGI 250 260 270 280 290 300 TANFVNGRTV EETQVPEISG VARIYNQSFF QSLLKATGID LENIVYYKDD THYFVMTAKK 310 320 330 340 350 360 QCLLRLGVLR QDWPDTNRLL GSANVVPEAL QRFTRAAADF ATHGKLGKLE FAQDAHGQPD 370 380 390 400 410 420 VSAFDFTSMM RAESSARVQE KHGARLLLGL VGDCLVEPFW PLGTGVARGF LAAFDAAWMV 430 440 450 460 470 480 KRWAEGAESL EVLAERESLY QLLSQTSPEN MHRNVAQYGL DPATRYPNLN LRAVTPNQVR 490 500 510 520 530 540 DLYDVLAKEP VQRNNDKTDT GMPATGSAGT QEELLRWCQE QTAGYPGVHV SDLSSSWADG 550 560 570 580 590 600 LALCALVYRL QPGLLEPSEL QGLGALEATA WALKVAENEL GITPVVSAQA VVAGSDPLGL 610 620 630 640 650 660 IAYLSHFHSA FKSMAHSPGP VSQASPGTSS AVLFLSKLQR TLQRSRAKEN AEDAGGKKLR 670 680 690 700 710 720 LEMEAETPST EVPPDPEPGV PLTPPSQHQE AGAGDLCALC GEHLYVLERL CVNGHFFHRS 730 740 750 760 770 780 CFRCHTCEAT LWPGGYEQHP GDGHFYCLQH LPQTDHKAEG SDRGPESPEL PTPSENSMPP 790 800 810 820 830 840 GLSTPTASQE GAGPVPDPSQ PTRRQIRLSS PERQRLSSLN LTPDPEMEPP PKPPRSCSAL 850 860 870 880 890 900 ARHALESSFV GWGLPVQSPQ ALVAMEKEEK ESPFSSEEEE EDVPLDSDVE QALQTFAKTS 910 920 930 940 950 960 GTMNNYPTWR RTLLRRAKEE EMKRFCKAQT IQRRLNEIEA ALRELEAEGV KLELALRRQS 970 980 990 1000 1010 1020 SSPEQQKKLW VGQLLQLVDK KNSLVAEEAE LMITVQELNL EEKQWQLDQE LRGYMNREEN 1030 1040 1050 1060 LKTAADRQAE DQVLRKLVDL VNQRDALIRF QEERRLSELA LGTGAQG
	Isoform 2 (MICAL-1b) [UniParc]. Checksum: 8EC7E9C12989C1E9	FASTA	981	108,552
	10 20 30 40 50 60 MASPTSTNPA HAHFESFLQA QLCQDVLSSF QELCGALGLE PGGGLPQYHK IKDQLNYWSA 70 80 90 100 110 120 KSLWTKLDKR AGQPVYQQGR ACTSTKCLVV GAGPCGLRVA VELALLGARV VLVEKRTKFS 130 140 150 160 170 180 RHNVLHLWPF TIHDLRALGA KKFYGRFCTG TLDHISIRQL QLLLLKVALL LGVEIHWGVT 190 200 210 220 230 240 FTGLQPPPRK GSGWRAQLQP NPPAQLANYE FDVLISAAGG KFVPEGFKVR EMRGKLAIGI 250 260 270 280 290 300 TANFVNGRTV EETQVPEISG VARIYNQSFF QSLLKATGID LENIVYYKDD THYFVMTAKK 310 320 330 340 350 360 QCLLRLGVLR QPFWPLGTGV ARGFLAAFDA AWMVKRWAEG AESLEVLAER ESLYQLLSQT 370 380 390 400 410 420 SPENMHRNVA QYGLDPATRY PNLNLRAVTP NQVRDLYDVL AKEPVQRNND KTDTGMPATG 430 440 450 460 470 480 SAGTQEELLR WCQEQTAGYP GVHVSDLSSS WADGLALCAL VYRLQPGLLE PSELQGLGAL 490 500 510 520 530 540 EATAWALKVA ENELGITPVV SAQAVVAGSD PLGLIAYLSH FHSAFKSMAH SPGPVSQASP 550 560 570 580 590 600 GTSSAVLFLS KLQRTLQRSR AKENAEDAGG KKLRLEMEAE TPSTEVPPDP EPGVPLTPPS 610 620 630 640 650 660 QHQEAGAGDL CALCGEHLYV LERLCVNGHF FHRSCFRCHT CEATLWPGGY EQHPGDGHFY 670 680 690 700 710 720 CLQHLPQTDH KAEGSDRGPE SPELPTPSEN SMPPGLSTPT ASQEGAGPVP DPSQPTRRQI 730 740 750 760 770 780 RLSSPERQRL SSLNLTPDPE MEPPPKPPRS CSALARHALE SSFVGWGLPV QSPQALVAME 790 800 810 820 830 840 KEEKESPFSS EEEEEDVPLD SDVEQALQTF AKTSGTMNNY PTWRRTLLRR AKEEEMKRFC 850 860 870 880 890 900 KAQTIQRRLN EIEAALRELE AEGVKLELAL RRQSSSPEQQ KKLWVGQLLQ LVDKKNSLVA 910 920 930 940 950 960 EEAELMITVQ ELNLEEKQWQ LDQELRGYMN REENLKTAAD RQAEDQVLRK LVDLVNQRDA 970 980 LIRFQEERRL SELALGTGAQ G
	Isoform 3 [UniParc]. Checksum: 7FF1E955AE2204DB	FASTA	332	37,715
	10 20 30 40 50 60 MPRLTFAPKG WPHPPTSLHP GQVTDQTTWW LFQELPTPSE NSMPPGLSTP TASQEGAGPV 70 80 90 100 110 120 PDPSQPTRRQ IRLSSPERQR LSSLNLTPDP EMEPPPKPPR SCSALARHAL ESSFVGWGLP 130 140 150 160 170 180 VQSPQALVAM EKEEKESPFS SEEEEEDVPL DSDVEQALQT FAKTSGTMNN YPTWRRTLLR 190 200 210 220 230 240 RAKEEEMKRF CKAQTIQRRL NEIEAALREL EAEGVKLELA LRRQSSSPEQ QKKLWVGQLL 250 260 270 280 290 300 QLVDKKNSLV AEEAELMITV QELNLEEKQW QLDQELRGYM NREENLKTAA DRQAEDQVLR 310 320 330 KLVDLVNQRD ALIRFQEERR LSELALGTGA QG
	Isoform 4 [UniParc]. Checksum: 947094500071E091	FASTA	1,086	119,821
	10 20 30 40 50 60 MSCLSHSSLP SCCPPQEASM ASPTSTNPAH AHFESFLQAQ LCQDVLSSFQ ELCGALGLEP 70 80 90 100 110 120 GGGLPQYHKI KDQLNYWSAK SLWTKLDKRA GQPVYQQGRA CTSTKCLVVG AGPCGLRVAV 130 140 150 160 170 180 ELALLGARVV LVEKRTKFSR HNVLHLWPFT IHDLRALGAK KFYGRFCTGT LDHISIRQLQ 190 200 210 220 230 240 LLLLKVALLL GVEIHWGVTF TGLQPPPRKG SGWRAQLQPN PPAQLANYEF DVLISAAGGK 250 260 270 280 290 300 FVPEGFKVRE MRGKLAIGIT ANFVNGRTVE ETQVPEISGV ARIYNQSFFQ SLLKATGIDL 310 320 330 340 350 360 ENIVYYKDDT HYFVMTAKKQ CLLRLGVLRQ DWPDTNRLLG SANVVPEALQ RFTRAAADFA 370 380 390 400 410 420 THGKLGKLEF AQDAHGQPDV SAFDFTSMMR AESSARVQEK HGARLLLGLV GDCLVEPFWP 430 440 450 460 470 480 LGTGVARGFL AAFDAAWMVK RWAEGAESLE VLAERESLYQ LLSQTSPENM HRNVAQYGLD 490 500 510 520 530 540 PATRYPNLNL RAVTPNQVRD LYDVLAKEPV QRNNDKTDTG MPATGSAGTQ EELLRWCQEQ 550 560 570 580 590 600 TAGYPGVHVS DLSSSWADGL ALCALVYRLQ PGLLEPSELQ GLGALEATAW ALKVAENELG 610 620 630 640 650 660 ITPVVSAQAV VAGSDPLGLI AYLSHFHSAF KSMAHSPGPV SQASPGTSSA VLFLSKLQRT 670 680 690 700 710 720 LQRSRAKENA EDAGGKKLRL EMEAETPSTE VPPDPEPGVP LTPPSQHQEA GAGDLCALCG 730 740 750 760 770 780 EHLYVLERLC VNGHFFHRSC FRCHTCEATL WPGGYEQHPG DGHFYCLQHL PQTDHKAEGS 790 800 810 820 830 840 DRGPESPELP TPSENSMPPG LSTPTASQEG AGPVPDPSQP TRRQIRLSSP ERQRLSSLNL 850 860 870 880 890 900 TPDPEMEPPP KPPRSCSALA RHALESSFVG WGLPVQSPQA LVAMEKEEKE SPFSSEEEEE 910 920 930 940 950 960 DVPLDSDVEQ ALQTFAKTSG TMNNYPTWRR TLLRRAKEEE MKRFCKAQTI QRRLNEIEAA 970 980 990 1000 1010 1020 LRELEAEGVK LELALRRQSS SPEQQKKLWV GQLLQLVDKK NSLVAEEAEL MITVQELNLE 1030 1040 1050 1060 1070 1080 EKQWQLDQEL RGYMNREENL KTAADRQAED QVLRKLVDLV NQRDALIRFQ EERRLSELAL GTGAQG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MICAL, a novel CasL interacting molecule, associates with vimentin." Suzuki T., Nakamoto T., Ogawa S., Seo S., Matsumura T., Tachibana K., Morimoto C., Hirai H. J. Biol. Chem. 277:14933-14941(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH NEDD9 AND VIM, VARIANT LYS-758.
[2]	"Characterization of long cDNA clones from human adult spleen." Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O. DNA Res. 7:357-366(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Spleen.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), VARIANTS LYS-758 AND LYS-758. Tissue: Colon mucosa, Embryo, Spleen and Thalamus.
[4]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORMS 1 AND 2), VARIANTS CYS-453; THR-624 AND LYS-758. Tissue: Blood, Lymph and Uterus.
[7]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 422-1067 (ISOFORMS 1/2). Tissue: Testis.
[8]	"MICALs, a family of conserved flavoprotein oxidoreductases, function in plexin-mediated axonal repulsion." Terman J.R., Mao T., Pasterkamp R.J., Yu H.-H., Kolodkin A.L. Cell 109:887-900(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PLXNA3.
[9]	"MICAL-1 isoforms, novel rab1 interacting proteins." Weide T., Teuber J., Bayer M., Barnekow A. Biochem. Biophys. Res. Commun. 306:79-86(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, INTERACTION WITH VIM.
[10]	"The MICAL proteins and rab1: a possible link to the cytoskeleton?" Fischer J., Weide T., Barnekow A. Biochem. Biophys. Res. Commun. 328:415-423(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAB1B, SUBCELLULAR LOCATION.
[11]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Release of MICAL autoinhibition by semaphorin-plexin signaling promotes interaction with collapsin response mediator protein." Schmidt E.F., Shim S.O., Strittmatter S.M. J. Neurosci. 28:2287-2297(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-617; SER-875 AND SER-876, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"Kinetic and spectroscopic characterization of the putative monooxygenase domain of human MICAL-1." Zucchini D., Caprini G., Pasterkamp R.J., Tedeschi G., Vanoni M.A. Arch. Biochem. Biophys. 515:1-13(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872; SER-875 AND SER-876, MASS SPECTROMETRY.
[17]	"Solution structure of the CH domain of human NEDD9-interacting protein with calponin homology and LIM domains." RIKEN structural genomics initiative (RSGI) Submitted (AUG-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 506-613.
[18]	"Solution structure of calponin homology domain of Human MICAL-1." Sun H., Dai H., Zhang J., Jin X., Xiong S., Xu J., Wu J., Shi Y. J. Biomol. NMR 36:295-300(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 506-614.
[19]	"Investigation of the four cooperative unfolding units existing in the MICAL-1 CH domain." Jin X., Zhang J., Dai H., Sun H., Wang D., Wu J., Shi Y. Biophys. Chem. 129:269-278(2007) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 506-614.
[20]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-309.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB048948 mRNA. Translation: BAB86289.1.
AK024500 mRNA. Translation: BAB15790.1.
AK021999 mRNA. Translation: BAB13949.1.
AK025392 mRNA. Translation: BAB15124.1.
AK296284 mRNA. Translation: BAH12301.1.
AL109947 Genomic DNA. Translation: CAI23343.1.
CH471051 Genomic DNA. Translation: EAW48344.1.
CH471051 Genomic DNA. Translation: EAW48345.1.
BC009972 mRNA. Translation: AAH09972.2.
BC042144 mRNA. Translation: AAH42144.1.
BC052983 mRNA. Translation: AAH52983.1.
AL122098 mRNA. Translation: CAB59266.1.

IPI

IPI00386301.
IPI00647681.
IPI01014373.

PIR

T34532.

RefSeq

NP_001152763.1. NM_001159291.1.
NP_073602.3. NM_022765.3.

UniGene

Hs.33476.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WYL	NMR	-	A	510-612	[»]
2CO8	NMR	-	A	687-755	[»]
2DK9	NMR	-	A	506-614	[»]

ProteinModelPortal

Q8TDZ2.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1343875.

STRING

9606.ENSP00000351664.

PTM databases

PhosphoSite

Q8TDZ2.

Polymorphism databases

DMDM

45593495.

Proteomic databases

PaxDb

Q8TDZ2.

PRIDE

Q8TDZ2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000358577; ENSP00000351385; ENSG00000135596.
ENST00000358807; ENSP00000351664; ENSG00000135596.
ENST00000368952; ENSP00000357948; ENSG00000135596.

GeneID

64780.

KEGG

hsa:64780.

UCSC

uc003ptj.3. human.
uc010kdr.3. human.

Organism-specific databases

CTD

64780.

GeneCards

GC06M109766.

HGNC

HGNC:20619. MICAL1.

HPA

HPA030178.

MIM

607129. gene.

neXtProt

NX_Q8TDZ2.

PharmGKB

PA134900249.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5069.

HOGENOM

HOG000047263.

HOVERGEN

HBG052474.

InParanoid

Q8TDZ2.

OMA

QEKHGAR.

OrthoDB

EOG4GF3DN.

PhylomeDB

Q8TDZ2.

Gene expression databases

ArrayExpress

Q8TDZ2.

Bgee

Q8TDZ2.

CleanEx

HS_MICAL1.

Genevestigator

Q8TDZ2.

GermOnline

ENSG00000135596. Homo sapiens.

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. human.

EvolutionaryTrace

Q8TDZ2.

GenomeRNAi

64780.

NextBio

66810.

SOURCE

Search...

Entry information

Entry name

MICA1_HUMAN

Accession

Primary (citable) accession number: Q8TDZ2
Secondary accession number(s): B7Z3R5 , E1P5F0, Q7Z633, Q8IVS9, Q96G47, Q9H6X6, Q9H7I0, Q9HAA1, Q9UFF7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 8, 2002
Last sequence update:	March 15, 2004
Last modified:	May 1, 2013
This is version 119 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.