ID A0A1S3KH32_LINUN Unreviewed; 1258 AA.
AC A0A1S3KH32;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Lysine-specific demethylase 6A isoform X2 {ECO:0000313|RefSeq:XP_013421536.1, ECO:0000313|RefSeq:XP_013421538.1};
GN Name=LOC106181631 {ECO:0000313|RefSeq:XP_013421536.1,
GN ECO:0000313|RefSeq:XP_013421538.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013421536.1};
RN [1] {ECO:0000313|RefSeq:XP_013421536.1, ECO:0000313|RefSeq:XP_013421538.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013421536.1,
RC ECO:0000313|RefSeq:XP_013421538.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the UTX family. {ECO:0000256|ARBA:ARBA00034483}.
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DR RefSeq; XP_013421536.1; XM_013566082.1.
DR RefSeq; XP_013421538.1; XM_013566084.1.
DR EnsemblMetazoa; XM_013566082.1; XP_013421536.1; LOC106181631.
DR EnsemblMetazoa; XM_013566084.1; XP_013421538.1; LOC106181631.
DR GeneID; 106181631; -.
DR OrthoDB; 20251at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032452; F:histone demethylase activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.1370; -; 1.
DR Gene3D; 2.10.110.20; -; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR046941; KDM6_GATAL_sf.
DR InterPro; IPR048562; KDM6A_B-like_C-hel.
DR InterPro; IPR048560; KDM6A_B-like_GATAL.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14017:SF1; LD02225P; 1.
DR PANTHER; PTHR14017; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF21322; KDM6_C-hel; 1.
DR Pfam; PF21326; KDM6_GATAL; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 67..100
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 952..1115
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 203..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 914..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..392
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..797
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1258 AA; 137737 MW; 0D0DCC98D9BE5DD2 CRC64;
MHHCIDQLGE KQAREVIAVQ CLQKSIEADP SSGQSWYFLG RCFSNVGKVH DAFVSYRQSI
DKSEANADTW CSIGVLYQQQ NQPMDALQAY ICAIQLDKSH VAAWTDLGVL YESVNQLKDA
LTCYINAAKN NKAYMNSNLQ NRIKFLQQQL SNIPMENLQP KNKPLPSIEE AWSLPIPAEL
TSRQGAMNTQ AKIAQQQRLG MHPQYMHSNT PSPHTPSSLS PGANTPHFNN NMNGVRGGPQ
QMGPHPSQQQ QQQRMSPGAA TPPQALGPHH PHGAVPQPMA GHMPQMQPGG MGVGHGPGQM
PPHMGPQGPL RHMGPSGMPS GGGGHMQSSS LAAMQQMSQN AAAAAALQQM ESQEQPGNAP
KRRKSQGKKK SSSQTPEPQG PPQGPPQGQV PPFYLSQPQM QQMNMLLMQQ SQGNLAPQHQ
QLLHQLQQQY YMQQQHQQQM MNAQGQQQHM NMPSPGHASP AHSPGHAGHM PGNMHNTPPP
PYPGNVPTRP MQAGHPGFPP NSQNFRPPLP GGGDFPGGPG HMPYAQHRNS LPHSSQPPSQ
QPRPNIPLPQ GHLTAAGPSN VQPPSSLPSS SQAGPGFPGG GSSQGGTFPH SSLTLGDLSD
SDLPKDLQNI DQELTALLSQ KDIATSLAED LLAQFAQSHD KEGAGGIMEG NHSQARTDSQ
IDADLSSLSA DLFKSVSGGA KMEPFSESSR TAQHVTDTNL EGDNNKISEE GDKKDTEGKD
SSVLSELRIN TGTTGRSPGP LLSPSSLSIN MSSSQLLAAC KGLGSNGLSN TSIMSERCPP
PAPPAPPYPP LPKDKLNPPT PSLYLESKRD AFSVELQQYC LSQPVAVIRG LAAALKLDLS
LFSTKSLVEA NPDHVMEVRS QRKQLPDENQ DIYGNNVWKC DSTRSHTSVA KYAQYQAASF
QESLKEEQDK AMGIFKGDSD SDSSSSGGGK GNKKKFKMLK FGTNVDLSDE KKWRPQLQEL
TKLPAFTRVV SASNALSHVG HTILGMNTVQ LYMKVPGSRT PGHQENNNFA SVNINIGPGD
CEWFGVPEEY WGVINNMCER QGINYLIGSW WPLLEDLYEE NIPVYRFIQK PGDLVWVNSG
TVHWVQAIGW CNNIAWNVGP LTVRQYQLAV ERYEWNKLQS VKSIVPIIHL SWNLARNVKI
SEPKLFEQIK YCLLRTLKQC QMTLEYIKTL GLEAKWHGRS KGEAAYYCNI CEIEVFNILF
VIEQEKKFHV HCLDCARKTS STLEGFIVLN QYTMDDLMEV YDNFQLHQQK SAITASSS
//
