Q7RTP6 (MICA3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein-methionine sulfoxide oxidase MICAL3
EC=1.14.13.-

Alternative name(s):
Molecule interacting with CasL protein 3
Short name=MICAL-3

Gene names

Name:	MICAL3
Synonyms:	KIAA0819, KIAA1364

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	2002 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 By similarity. Involved in exocytic vesicles tethering and fusion: the monooxygenase activity is required for this process. Ref.12
Catalytic activity	[protein]-methionine + NADPH + O2 = [protein]-methionine-sulfoxide + NADP+ + H2O.
Cofactor	FAD By similarity.
Subunit structure	Interacts with RAB1B. Interacts with ERC1 and RAB8A. Ref.7 Ref.12
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton Ref.7.
Tissue specificity	Ubiquitous. Ref.7
Sequence similarities	Belongs to the Mical family. Contains 1 CH (calponin-homology) domain. Contains 1 LIM zinc-binding domain.

Ontologies

Keywords
Biological process	Exocytosis
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 sequence or structural similarity. Source: UniProtKB exocytosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	FAD 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...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q7RTP6-1)

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: Q7RTP6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     934-948: SSSESEMEEEGEEEE → RSARRAAGRPPATRP
     949-2002: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q7RTP6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     746-746: R → RQLTQERGASQPSCCLPGQVRPAPTPRWK
     934-948: SSSESEMEEEGEEEE → RSARRAAGRPPATRP
     949-2002: Missing.

Isoform 4 (identifier: Q7RTP6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     934-966: SSSESEMEEEGEEEEEEPRLPPSDLGGVPWKEA → RDWVSPWLPRMVSNSWAQMIHPPQPPTVLGSQM
     967-2002: Missing.

Isoform 5 (identifier: Q7RTP6-5)

The sequence of this isoform differs from the canonical sequence as follows:
     747-747: Q → QQREKECSRT...PKALLDKKEL
     871-949: GVNGLEEPSI...MEEEGEEEEE → LTSLFGWVAR...GEFHWQAVAQ
     950-2002: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2002

2002

Protein-methionine sulfoxide oxidase MICAL3

PRO_0000075846

Regions

Domain

518 – 621

104

CH

Domain

762 – 824

63

LIM zinc-binding

Nucleotide binding

88 – 117

30

FAD Potential

Nucleotide binding

97 – 125

29

FAD By similarity

Region

2 – 494

493

Monooxygenase domain By similarity

Coiled coil

1821 – 1992

172

Potential

Compositional bias

688 – 691

4

Poly-Glu

Compositional bias

889 – 1138

250

Glu-rich

Compositional bias

1141 – 1505

365

Pro-rich

Sites

Binding site

97

1

FAD By similarity

Binding site

116

1

FAD By similarity

Binding site

118

1

FAD By similarity

Binding site

123

1

FAD By similarity

Binding site

125

1

FAD By similarity

Binding site

398

1

FAD By similarity

Amino acid modifications

Modified residue

649

1

Phosphoserine Ref.9 Ref.11

Modified residue

887

1

Phosphothreonine Ref.9

Modified residue

977

1

Phosphoserine By similarity

Modified residue

1192

1

Phosphoserine By similarity

Modified residue

1221

1

Phosphoserine By similarity

Modified residue

1310

1

Phosphoserine Ref.8 Ref.10

Modified residue

1337

1

Phosphoserine Ref.11

Modified residue

1341

1

Phosphothreonine Ref.11

Modified residue

1371

1

Phosphoserine Ref.9 Ref.13

Modified residue

1384

1

Phosphoserine Ref.9

Modified residue

1454

1

Phosphothreonine Ref.10

Natural variations

Alternative sequence

746

1

R → RQLTQERGASQPSCCLPGQV RPAPTPRWK in isoform 3.

VSP_039485

Alternative sequence

747

1

Q → QQREKECSRTCPKKVITLSP PPTPPPCRAHGGQQTYRDLD ADNRGKQSPHHERPEPEPPR RFFVDQWELSLSLRSSARPA SPSSDSLRQKYIKMYTGGVS SLAEQIANQLQRKEQPKALL DKKEL in isoform 5.

VSP_042600

Alternative sequence

871 – 949

79

GVNGL…EEEEE → LTSLFGWVARHSLGLCDKAK GMSQHLQSNISSFGQQVAQN PLDSFFMCQLLAFGVPFLYG LSEVLVQIRGEFHWQAVAQ in isoform 5.

VSP_042601

Alternative sequence

934 – 966

33

SSSES…PWKEA → RDWVSPWLPRMVSNSWAQMI HPPQPPTVLGSQM in isoform 4.

VSP_039486

Alternative sequence

934 – 948

15

SSSES…GEEEE → RSARRAAGRPPATRP in isoform 2 and isoform 3.

VSP_039487

Alternative sequence

949 – 2002

1054

Missing in isoform 2 and isoform 3.

VSP_039488

Alternative sequence

950 – 2002

1053

Missing in isoform 5.

VSP_042602

Alternative sequence

967 – 2002

1036

Missing in isoform 4.

VSP_039489

Natural variant

11

1

P → A.
Corresponds to variant rs11913706 [ dbSNP | Ensembl ].

VAR_059451

Natural variant

745

1

R → Q.
Corresponds to variant rs2289719 [ dbSNP | Ensembl ].

VAR_059452

Natural variant

750

1

M → L.
Corresponds to variant rs5992128 [ dbSNP | Ensembl ].

VAR_018263

Experimental info

Mutagenesis

93 – 98

6

GAGPCG → WAWPCW: Abolishes Monooxygenase activity and impairs ability to control docking and fusion of exocytic carriers. Ref.12

Sequence conflict

414

1

G → D in BX647382. Ref.2

Sequence conflict

1245

1

Q → R in BAA74842. Ref.5

Sequence conflict

1717

1

E → V in AAH06562. Ref.4

Isoform 4:

Sequence conflict

957

1

Q → R in BX647382. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2002

Helix Strand Turn

Details...

Beta strand

519 – 521

3

Helix

523 – 531

9

Beta strand

535 – 537

3

Helix

545 – 548

4

Helix

551 – 560

10

Turn

562 – 564

3

Turn

567 – 569

3

Helix

575 – 589

15

Helix

598 – 603

6

Helix

609 – 623

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 13, 2010. Version 2. Checksum: F85C97FD4D647B80	FASTA	2,002	224,295
	10 20 30 40 50 60 MEERKHETMN PAHVLFDRFV QATTCKGTLK AFQELCDHLE LKPKDYRSFY HKLKSKLNYW 70 80 90 100 110 120 KAKALWAKLD KRGSHKDYKK GKACTNTKCL IIGAGPCGLR TAIDLSLLGA KVVVIEKRDA 130 140 150 160 170 180 FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGAIDHISIR QLQLILLKVA LILGIEIHVN 190 200 210 220 230 240 VEFQGLIQPP EDQENERIGW RALVHPKTHP VSEYEFEVII GGDGRRNTLE GFRRKEFRGK 250 260 270 280 290 300 LAIAITANFI NRNTTAEAKV EEISGVAFIF NQKFFQELRE ATGIDLENIV YYKDDTHYFV 310 320 330 340 350 360 MTAKKQSLLD KGVILHDYAD TELLLSRENV DQEALLSYAR EAADFSTQQQ LPSLDFAINH 370 380 390 400 410 420 YGQPDVAMFD FTCMYASENA ALVREQNGHQ LLVALVGDSL LEPFWPMGTG IARGFLAAMD 430 440 450 460 470 480 SAWMVRSWSL GTSPLEVLAE RESIYRLLPQ TTPENVSKNF SQYSIDPVTR YPNINVNFLR 490 500 510 520 530 540 PSQVRHLYDT GETKDIHLEM ESLVNSRTTP KLTRNESVAR SSKLLGWCQR QTDGYAGVNV 550 560 570 580 590 600 TDLTMSWKSG LALCAIIHRY RPDLIDFDSL DEQNVEKNNQ LAFDIAEKEL GISPIMTGKE 610 620 630 640 650 660 MASVGEPDKL SMVMYLTQFY EMFKDSLPSS DTLDLNAEEK AVLIASTRSP ISFLSKLGQT 670 680 690 700 710 720 ISRKRSPKDK KEKDLDGAGK RRKTSQSEEE EAPRGHRGER PTLVSTLTDR RMDVAVGNQN 730 740 750 760 770 780 KVKYMATQLL AKFEENAPAQ SIGIRRQGSM KKEFPQNLGG SDTCYFCQKR VYVMERLSAE 790 800 810 820 830 840 GKFFHRSCFK CEYCATTLRL SAYAYDIEDG KFYCKPHYCY RLSGYAQRKR PAVAPLSGKE 850 860 870 880 890 900 AKGPLQDGAT TDANGRANAV ASSTERTPGS GVNGLEEPSI AKRLRGTPER IELENYRLSL 910 920 930 940 950 960 RQAEALQEVP EETQAEHNLS SVLDTGAEED VASSSSESEM EEEGEEEEEE PRLPPSDLGG 970 980 990 1000 1010 1020 VPWKEAVRIH ALLKGKSEEE LEASKSFGPG NEEEEEEEEE YEEEEEEDYD EEEEESSEAG 1030 1040 1050 1060 1070 1080 NQRLQQVMHA ADPLEIQADV HWTHIREREE EERMAPASES SASGAPLDEN DLEEDVDSEP 1090 1100 1110 1120 1130 1140 AEIEGEAAED GDPGDTGAEL DDDQHWSDSP SDADRELRLP CPAEGEAELE LRVSEDEEKL 1150 1160 1170 1180 1190 1200 PASPKHQERG PSQATSPIRS PQESALLFIP VHSPSTEGPQ LPPVPAATQE KSPEERLFPE 1210 1220 1230 1240 1250 1260 PLLPKEKPKA DAPSDLKAVH SPIRSQPVTL PEARTPVSPG SPQPQPPVAA STPPPSPLPI 1270 1280 1290 1300 1310 1320 CSQPQPSTEA TVPSPTQSPI RFQPAPAKTS TPLAPLPVQS QSDTKDRLGS PLAVDEALRR 1330 1340 1350 1360 1370 1380 SDLVEEFWMK SAEIRRSLGL TPVDRSKGPE PSFPTPAFRP VSLKSYSVEK SPQDEGLHLL 1390 1400 1410 1420 1430 1440 KPLSIPKRLG LPKPEGEPLS LPTPRSPSDR ELRSAQEERR ELSSSSGLGL HGSSSNMKTL 1450 1460 1470 1480 1490 1500 GSQSFNTSDS AMLTPPSSPP PPPPPGEEPA TLRRKLREAE PNASVVPPPL PATWMRPPRE 1510 1520 1530 1540 1550 1560 PAQPPREEVR KSFVESVEEI PFADDVEDTY DDKTEDSSLQ EKFFTPPSCW PRPEKPRHPP 1570 1580 1590 1600 1610 1620 LAKENGRLPA LEGTLQPQKR GLPLVSAEAK ELAEERMRAR EKSVKSQALR DAMARQLSRM 1630 1640 1650 1660 1670 1680 QQMELASGAP RPRKASSAPS QGKERRPDSP TRPTLRGSEE PTLKHEATSE EVLSPPSDSG 1690 1700 1710 1720 1730 1740 GPDGSFTSSE GSSGKSKKRS SLFSPRRNKK EKKSKGEGRP PEKPSSNLLE EAAAKPKSLW 1750 1760 1770 1780 1790 1800 KSVFSGYKKD KKKKADDKSC PSTPSSGATV DSGKHRVLPV VRAELQLRRQ LSFSEDSDLS 1810 1820 1830 1840 1850 1860 SDDVLEKSSQ KSRREPRTYT EEELNAKLTR RVQKAARRQA KQEELKRLHR AQIIQRQLQQ 1870 1880 1890 1900 1910 1920 VEERQRRLEE RGVAVEKALR GEAGMGKKDD PKLMQEWFKL VQEKNAMVRY ESELMIFARE 1930 1940 1950 1960 1970 1980 LELEDRQSRL QQELRERMAV EDHLKTEEEL SEEKQILNEM LEVVEQRDSL VALLEEQRLR 1990 2000 EREEDKDLEA AMLSKGFSLN WS
	Isoform 2 [UniParc]. Checksum: D50FC4EC6F46D30C	FASTA	948	106,837
	10 20 30 40 50 60 MEERKHETMN PAHVLFDRFV QATTCKGTLK AFQELCDHLE LKPKDYRSFY HKLKSKLNYW 70 80 90 100 110 120 KAKALWAKLD KRGSHKDYKK GKACTNTKCL IIGAGPCGLR TAIDLSLLGA KVVVIEKRDA 130 140 150 160 170 180 FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGAIDHISIR QLQLILLKVA LILGIEIHVN 190 200 210 220 230 240 VEFQGLIQPP EDQENERIGW RALVHPKTHP VSEYEFEVII GGDGRRNTLE GFRRKEFRGK 250 260 270 280 290 300 LAIAITANFI NRNTTAEAKV EEISGVAFIF NQKFFQELRE ATGIDLENIV YYKDDTHYFV 310 320 330 340 350 360 MTAKKQSLLD KGVILHDYAD TELLLSRENV DQEALLSYAR EAADFSTQQQ LPSLDFAINH 370 380 390 400 410 420 YGQPDVAMFD FTCMYASENA ALVREQNGHQ LLVALVGDSL LEPFWPMGTG IARGFLAAMD 430 440 450 460 470 480 SAWMVRSWSL GTSPLEVLAE RESIYRLLPQ TTPENVSKNF SQYSIDPVTR YPNINVNFLR 490 500 510 520 530 540 PSQVRHLYDT GETKDIHLEM ESLVNSRTTP KLTRNESVAR SSKLLGWCQR QTDGYAGVNV 550 560 570 580 590 600 TDLTMSWKSG LALCAIIHRY RPDLIDFDSL DEQNVEKNNQ LAFDIAEKEL GISPIMTGKE 610 620 630 640 650 660 MASVGEPDKL SMVMYLTQFY EMFKDSLPSS DTLDLNAEEK AVLIASTRSP ISFLSKLGQT 670 680 690 700 710 720 ISRKRSPKDK KEKDLDGAGK RRKTSQSEEE EAPRGHRGER PTLVSTLTDR RMDVAVGNQN 730 740 750 760 770 780 KVKYMATQLL AKFEENAPAQ SIGIRRQGSM KKEFPQNLGG SDTCYFCQKR VYVMERLSAE 790 800 810 820 830 840 GKFFHRSCFK CEYCATTLRL SAYAYDIEDG KFYCKPHYCY RLSGYAQRKR PAVAPLSGKE 850 860 870 880 890 900 AKGPLQDGAT TDANGRANAV ASSTERTPGS GVNGLEEPSI AKRLRGTPER IELENYRLSL 910 920 930 940 RQAEALQEVP EETQAEHNLS SVLDTGAEED VASRSARRAA GRPPATRP
	Isoform 3 [UniParc]. Checksum: D94482577189AD04	FASTA	976	109,911
	10 20 30 40 50 60 MEERKHETMN PAHVLFDRFV QATTCKGTLK AFQELCDHLE LKPKDYRSFY HKLKSKLNYW 70 80 90 100 110 120 KAKALWAKLD KRGSHKDYKK GKACTNTKCL IIGAGPCGLR TAIDLSLLGA KVVVIEKRDA 130 140 150 160 170 180 FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGAIDHISIR QLQLILLKVA LILGIEIHVN 190 200 210 220 230 240 VEFQGLIQPP EDQENERIGW RALVHPKTHP VSEYEFEVII GGDGRRNTLE GFRRKEFRGK 250 260 270 280 290 300 LAIAITANFI NRNTTAEAKV EEISGVAFIF NQKFFQELRE ATGIDLENIV YYKDDTHYFV 310 320 330 340 350 360 MTAKKQSLLD KGVILHDYAD TELLLSRENV DQEALLSYAR EAADFSTQQQ LPSLDFAINH 370 380 390 400 410 420 YGQPDVAMFD FTCMYASENA ALVREQNGHQ LLVALVGDSL LEPFWPMGTG IARGFLAAMD 430 440 450 460 470 480 SAWMVRSWSL GTSPLEVLAE RESIYRLLPQ TTPENVSKNF SQYSIDPVTR YPNINVNFLR 490 500 510 520 530 540 PSQVRHLYDT GETKDIHLEM ESLVNSRTTP KLTRNESVAR SSKLLGWCQR QTDGYAGVNV 550 560 570 580 590 600 TDLTMSWKSG LALCAIIHRY RPDLIDFDSL DEQNVEKNNQ LAFDIAEKEL GISPIMTGKE 610 620 630 640 650 660 MASVGEPDKL SMVMYLTQFY EMFKDSLPSS DTLDLNAEEK AVLIASTRSP ISFLSKLGQT 670 680 690 700 710 720 ISRKRSPKDK KEKDLDGAGK RRKTSQSEEE EAPRGHRGER PTLVSTLTDR RMDVAVGNQN 730 740 750 760 770 780 KVKYMATQLL AKFEENAPAQ SIGIRRQLTQ ERGASQPSCC LPGQVRPAPT PRWKQGSMKK 790 800 810 820 830 840 EFPQNLGGSD TCYFCQKRVY VMERLSAEGK FFHRSCFKCE YCATTLRLSA YAYDIEDGKF 850 860 870 880 890 900 YCKPHYCYRL SGYAQRKRPA VAPLSGKEAK GPLQDGATTD ANGRANAVAS STERTPGSGV 910 920 930 940 950 960 NGLEEPSIAK RLRGTPERIE LENYRLSLRQ AEALQEVPEE TQAEHNLSSV LDTGAEEDVA 970 SRSARRAAGR PPATRP
	Isoform 4 [UniParc]. Checksum: DC1B9C83CB4D3E35	FASTA	966	109,047
	10 20 30 40 50 60 MEERKHETMN PAHVLFDRFV QATTCKGTLK AFQELCDHLE LKPKDYRSFY HKLKSKLNYW 70 80 90 100 110 120 KAKALWAKLD KRGSHKDYKK GKACTNTKCL IIGAGPCGLR TAIDLSLLGA KVVVIEKRDA 130 140 150 160 170 180 FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGAIDHISIR QLQLILLKVA LILGIEIHVN 190 200 210 220 230 240 VEFQGLIQPP EDQENERIGW RALVHPKTHP VSEYEFEVII GGDGRRNTLE GFRRKEFRGK 250 260 270 280 290 300 LAIAITANFI NRNTTAEAKV EEISGVAFIF NQKFFQELRE ATGIDLENIV YYKDDTHYFV 310 320 330 340 350 360 MTAKKQSLLD KGVILHDYAD TELLLSRENV DQEALLSYAR EAADFSTQQQ LPSLDFAINH 370 380 390 400 410 420 YGQPDVAMFD FTCMYASENA ALVREQNGHQ LLVALVGDSL LEPFWPMGTG IARGFLAAMD 430 440 450 460 470 480 SAWMVRSWSL GTSPLEVLAE RESIYRLLPQ TTPENVSKNF SQYSIDPVTR YPNINVNFLR 490 500 510 520 530 540 PSQVRHLYDT GETKDIHLEM ESLVNSRTTP KLTRNESVAR SSKLLGWCQR QTDGYAGVNV 550 560 570 580 590 600 TDLTMSWKSG LALCAIIHRY RPDLIDFDSL DEQNVEKNNQ LAFDIAEKEL GISPIMTGKE 610 620 630 640 650 660 MASVGEPDKL SMVMYLTQFY EMFKDSLPSS DTLDLNAEEK AVLIASTRSP ISFLSKLGQT 670 680 690 700 710 720 ISRKRSPKDK KEKDLDGAGK RRKTSQSEEE EAPRGHRGER PTLVSTLTDR RMDVAVGNQN 730 740 750 760 770 780 KVKYMATQLL AKFEENAPAQ SIGIRRQGSM KKEFPQNLGG SDTCYFCQKR VYVMERLSAE 790 800 810 820 830 840 GKFFHRSCFK CEYCATTLRL SAYAYDIEDG KFYCKPHYCY RLSGYAQRKR PAVAPLSGKE 850 860 870 880 890 900 AKGPLQDGAT TDANGRANAV ASSTERTPGS GVNGLEEPSI AKRLRGTPER IELENYRLSL 910 920 930 940 950 960 RQAEALQEVP EETQAEHNLS SVLDTGAEED VASRDWVSPW LPRMVSNSWA QMIHPPQPPT VLGSQM
	Isoform 5 [UniParc]. Checksum: C550AC7BE7536179	FASTA	1,073	121,173
	10 20 30 40 50 60 MEERKHETMN PAHVLFDRFV QATTCKGTLK AFQELCDHLE LKPKDYRSFY HKLKSKLNYW 70 80 90 100 110 120 KAKALWAKLD KRGSHKDYKK GKACTNTKCL IIGAGPCGLR TAIDLSLLGA KVVVIEKRDA 130 140 150 160 170 180 FSRNNVLHLW PFTIHDLRGL GAKKFYGKFC AGAIDHISIR QLQLILLKVA LILGIEIHVN 190 200 210 220 230 240 VEFQGLIQPP EDQENERIGW RALVHPKTHP VSEYEFEVII GGDGRRNTLE GFRRKEFRGK 250 260 270 280 290 300 LAIAITANFI NRNTTAEAKV EEISGVAFIF NQKFFQELRE ATGIDLENIV YYKDDTHYFV 310 320 330 340 350 360 MTAKKQSLLD KGVILHDYAD TELLLSRENV DQEALLSYAR EAADFSTQQQ LPSLDFAINH 370 380 390 400 410 420 YGQPDVAMFD FTCMYASENA ALVREQNGHQ LLVALVGDSL LEPFWPMGTG IARGFLAAMD 430 440 450 460 470 480 SAWMVRSWSL GTSPLEVLAE RESIYRLLPQ TTPENVSKNF SQYSIDPVTR YPNINVNFLR 490 500 510 520 530 540 PSQVRHLYDT GETKDIHLEM ESLVNSRTTP KLTRNESVAR SSKLLGWCQR QTDGYAGVNV 550 560 570 580 590 600 TDLTMSWKSG LALCAIIHRY RPDLIDFDSL DEQNVEKNNQ LAFDIAEKEL GISPIMTGKE 610 620 630 640 650 660 MASVGEPDKL SMVMYLTQFY EMFKDSLPSS DTLDLNAEEK AVLIASTRSP ISFLSKLGQT 670 680 690 700 710 720 ISRKRSPKDK KEKDLDGAGK RRKTSQSEEE EAPRGHRGER PTLVSTLTDR RMDVAVGNQN 730 740 750 760 770 780 KVKYMATQLL AKFEENAPAQ SIGIRRQQRE KECSRTCPKK VITLSPPPTP PPCRAHGGQQ 790 800 810 820 830 840 TYRDLDADNR GKQSPHHERP EPEPPRRFFV DQWELSLSLR SSARPASPSS DSLRQKYIKM 850 860 870 880 890 900 YTGGVSSLAE QIANQLQRKE QPKALLDKKE LGSMKKEFPQ NLGGSDTCYF CQKRVYVMER 910 920 930 940 950 960 LSAEGKFFHR SCFKCEYCAT TLRLSAYAYD IEDGKFYCKP HYCYRLSGYA QRKRPAVAPL 970 980 990 1000 1010 1020 SGKEAKGPLQ DGATTDANGR ANAVASSTER TPGSLTSLFG WVARHSLGLC DKAKGMSQHL 1030 1040 1050 1060 1070 QSNISSFGQQ VAQNPLDSFF MCQLLAFGVP FLYGLSEVLV QIRGEFHWQA VAQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[2]	"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] (ISOFORM 4). Tissue: Testis.
[3]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1626-2002 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 682-966 (ISOFORM 4). Tissue: Lymph and Pancreas.
[5]	"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O. DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-2002 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1014-2002 (ISOFORM 1). Tissue: Brain.
[6]	"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: IDENTIFICATION (ISOFORM 3 AND PARTIAL ISOFORM 1).
[7]	"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, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[8]	"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-1310, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; THR-887; SER-1371 AND SER-1384, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-1310 AND THR-1454, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-649; SER-1337 AND THR-1341, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Rab6, Rab8, and MICAL3 cooperate in controlling docking and fusion of exocytotic carriers." Grigoriev I., Yu K.L., Martinez-Sanchez E., Serra-Marques A., Smal I., Meijering E., Demmers J., Peranen J., Pasterkamp R.J., van der Sluijs P., Hoogenraad C.C., Akhmanova A. Curr. Biol. 21:967-974(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ERC1 AND RAB8A, MUTAGENESIS OF 93-GLY--GLY-98.
[13]	"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-1371, MASS SPECTROMETRY.
[14]	"Solution structure of the CH domain from human MICAL-3 protein." RIKEN structural genomics initiative (RSGI) Submitted (JUN-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 515-630.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

CR456364 mRNA. Translation: CAG30250.1.
BX647382 mRNA. No translation available.
AC016026 Genomic DNA. No translation available.
AC016027 Genomic DNA. No translation available.
BC006562 mRNA. Translation: AAH06562.2.
BC085009 mRNA. Translation: AAH85009.1.
BC157876 mRNA. Translation: AAI57877.1.
BC171887 mRNA. Translation: AAI71887.1.
AB020626 mRNA. Translation: BAA74842.1.
AB037785 mRNA. Translation: BAA92602.1.
BK000464 mRNA. Translation: DAA01343.1.
BK000465 mRNA. Translation: DAA01344.1.

IPI

IPI00177937.
IPI00480203.
IPI00741791.
IPI00896430.
IPI00969176.

RefSeq

NP_001116203.1. NM_001122731.1.
NP_001129476.1. NM_001136004.1.
NP_056056.2. NM_015241.2.

UniGene

Hs.528024.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D88	NMR	-	A	518-625	[»]

ProteinModelPortal

Q7RTP6.

SMR

Q7RTP6. Positions 10-489, 515-630, 762-818.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q7RTP6. 3 interactions.

STRING

9606.ENSP00000414846.

PTM databases

PhosphoSite

Q7RTP6.

Polymorphism databases

DMDM

300669653.

Proteomic databases

PaxDb

Q7RTP6.

PeptideAtlas

O94909.

PRIDE

Q7RTP6.

Protocols and materials databases

DNASU

57553.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000207726; ENSP00000207726; ENSG00000243156.
ENST00000383094; ENSP00000372574; ENSG00000243156.
ENST00000400561; ENSP00000383406; ENSG00000243156.
ENST00000414725; ENSP00000391827; ENSG00000243156.
ENST00000429452; ENSP00000414846; ENSG00000243156.
ENST00000441493; ENSP00000416015; ENSG00000243156.
ENST00000444520; ENSP00000410315; ENSG00000243156.
ENST00000585038; ENSP00000462033; ENSG00000243156.

GeneID

57553.

KEGG

hsa:57553.

UCSC

uc002zng.4. human.
uc002znh.2. human.
uc002znj.1. human.
uc002znk.1. human.

Organism-specific databases

CTD

57553.

GeneCards

GC22M018270.
GC22M018271.

H-InvDB

HIX0213260.

HGNC

HGNC:24694. MICAL3.

HPA

HPA000639.
HPA003421.

MIM

608882. gene.

neXtProt

NX_Q7RTP6.

PharmGKB

PA142671454.

HUGE

Search...
Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5069.

HOGENOM

HOG000047263.

HOVERGEN

HBG081827.

InParanoid

O94909.

OMA

PQWKQGS.

Gene expression databases

ArrayExpress

Q7RTP6.

Bgee

Q7RTP6.

CleanEx

HS_MICAL3.

Genevestigator

Q7RTP6.

GermOnline

ENSG00000093100. 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.
IPR003042. Rng_hydrolase-like.
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]

PRINTS

PR00420. RNGMNOXGNASE.

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

MICAL3. human.

EvolutionaryTrace

Q7RTP6.

GenomeRNAi

57553.

NextBio

64022.

SOURCE

Search...

Entry information

Entry name

MICA3_HUMAN

Accession

Primary (citable) accession number: Q7RTP6
Secondary accession number(s): B2RXJ5 , E9PEF0, O94909, Q5U4P4, Q6ICK4, Q96DF2, Q9P2I3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	July 13, 2010
Last modified:	May 1, 2013
This is version 104 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.