ID F6R107_CIOIN Unreviewed; 705 AA.
AC F6R107; A0A1W2WM87;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Lysine-specific histone demethylase 1A {ECO:0000313|Ensembl:ENSCINP00000013511.3};
GN Name=LOC100187100 {ECO:0000313|Ensembl:ENSCINP00000013511.3};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000013511.3, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000013511.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR038051-1};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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DR EMBL; EAAA01003000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002131150.1; XM_002131114.3.
DR AlphaFoldDB; F6R107; -.
DR STRING; 7719.ENSCINP00000013511; -.
DR Ensembl; ENSCINT00000013511.3; ENSCINP00000013511.3; ENSCING00000006580.3.
DR GeneID; 100187100; -.
DR KEGG; cin:100187100; -.
DR GeneTree; ENSGT00940000157193; -.
DR HOGENOM; CLU_004498_5_1_1; -.
DR InParanoid; F6R107; -.
DR OMA; SSRGEMF; -.
DR OrthoDB; 5402444at2759; -.
DR TreeFam; TF312972; -.
DR Proteomes; UP000008144; Chromosome 9.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0140682; F:FAD-dependent H3K4me/H3K4me3 demethylase activity; IEA:UniProt.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:Ensembl.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007399; P:nervous system development; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:1903706; P:regulation of hemopoiesis; IEA:Ensembl.
DR GO; GO:1900052; P:regulation of retinoic acid biosynthetic process; IEA:Ensembl.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 1.10.287.80; ATP synthase, gamma subunit, helix hairpin domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR017366; Hist_Lys-spec_deMease.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF386; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1A; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF04433; SWIRM; 1.
DR PIRSF; PIRSF038051; Histone_Lys-demethylase; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR038051-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000008144}.
FT DOMAIN 10..111
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT BINDING 119..147
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT BINDING 148
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT BINDING 154
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT BINDING 170..171
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT BINDING 655
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
FT BINDING 664..665
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR038051-1"
SQ SEQUENCE 705 AA; 78421 MW; 6C2A100937C97E9D CRC64;
MEFTDNLGGL EGAAFQSRLP YNELSPEERD LFPDVASDVN GHLGFLNIRN RILQMWLDNP
KIELIYEVAV QRLTDLKEIT PENVALSLKI HKYLERHGFI NFGIFKRIHP IRKIKKAKVV
VIGAGMAGLA AARQLTSFGM EVITIEARDR VGGRVSTFRK GKFVADLGAM VVTGLGGNPI
TVISKQINME LHKIKQDCPL YETGGSRVPK EKDVLVEKEF NKLLEATAHL SHEMEIDKFK
DKQLSLGKAF ELVISLQEKS VKEQLLAHWH QIAKLHERHK DIVERMATLK QKALKSREVV
STIPTLNDME DKESEKAISN EFRRRCLMKD CREACKDFFK LNETRQNLES EIVAMEHNLP
SDVYLSSKDR QLLDWHLANL EFANAAPLDK LSLKHWNQDD AYEFSGSHLV VRNGYSILPT
AYADGLDIRL STTVRKMSYS DTGCSVVIQS TQTASPQTTI TCDAILCTLP LGVLNPPDPE
LDHGPAIEFD PPLPSWKIEA MKRMGFGNLN KVVLCFDRNF WESASANLFG HIGATTSSRG
ELFLFWAIYR APVLIALVAG KSANVMEHVG DGVVLSRAIA VLKGIFGPEN VPDPVNYTVT
RWGSDPWAKG SYSYVAVGSS GDDYDVMACP VDGAGASYEQ MMSSSGNPRL FFAGEHTMRN
YPATVHGALL SGFREAARIT DIFVGPITTN GNNQQGTVVT EITDH
//
