ID A0A401RZQ7_CHIPU Unreviewed; 1266 AA.
AC A0A401RZQ7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=PHD finger protein 12 {ECO:0008006|Google:ProtNLM};
GN ORFNames=chiPu_0002033 {ECO:0000313|EMBL:GCC23635.1};
OS Chiloscyllium punctatum (Brownbanded bambooshark) (Hemiscyllium punctatum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Orectolobiformes; Hemiscylliidae;
OC Chiloscyllium.
OX NCBI_TaxID=137246 {ECO:0000313|EMBL:GCC23635.1, ECO:0000313|Proteomes:UP000287033};
RN [1] {ECO:0000313|EMBL:GCC23635.1, ECO:0000313|Proteomes:UP000287033}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC23635.1}.
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DR EMBL; BEZZ01000035; GCC23635.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401RZQ7; -.
DR STRING; 137246.A0A401RZQ7; -.
DR OMA; ADQDPNG; -.
DR Proteomes; UP000287033; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd22703; FHA_PHF12; 1.
DR CDD; cd15533; PHD1_PHF12; 1.
DR CDD; cd15534; PHD2_PHF12_Rco1; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 6.10.20.60; PHD finger protein 12; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR031966; PHF12_MRG-bd.
DR InterPro; IPR038098; PHF12_MRG-bd_sf.
DR InterPro; IPR002347; SDR_fam.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR43157:SF44; DEHYDROGENASE_REDUCTASE SDR FAMILY MEMBER 13; 1.
DR PANTHER; PTHR43157; PHOSPHATIDYLINOSITOL-GLYCAN BIOSYNTHESIS CLASS F PROTEIN-RELATED; 1.
DR Pfam; PF00106; adh_short; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF16737; PHF12_MRG_bd; 1.
DR PRINTS; PR00081; GDHRDH.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000287033};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT TRANSMEM 952..973
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..101
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 275..325
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 847..901
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT REGION 23..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1266 AA; 139063 MW; 6A9EB32ADD0A3E98 CRC64;
METKTIVYDL DTSGGLMEKI QALLAPPKSE ESDKKAKKLE KEPRRSGRAT NHDTCDSCKE
GGDLLCCDHC PAAFHLQCCN PPLSEEMLPP GDWMCHRCTV RRKKQEKKER FGQVNGVMDK
QTVKRTASPT VDMDFSDKTS SKALDSRVDS NCRSFAQAKS LERRVSRPGT PTSNASTDTP
TSEQNEVDDD MIDVDDENAA IEVDCSQLQI RNPFEILIAA AMERNPTQFQ LPNELTCTTA
LPGTSKRRRK EETTGKNVKK AQHELDHNGL VPLPVKVCFI CNRSCRVAPL VQCDYCPLLF
HMDCLDPPLT AMPTGRWMCP NHIEHVVLNQ KNMTLSNRCR IFDKFQDRIS QHAIKIDFLN
KIHRKHPPNR RHIKPVKRKN MKVPEAIKAQ YQYPPPLLPP AGIRDGELIC NETTSESQKH
LSNYEHFATE EEQQEWLRSV VALQCSIFKH LSAKQMPLFW DTEQTEKADI KPCVTAQCSA
DNSLNSAHQT AGKKQSPSPS PTTCNVTCTS GTNSQNSSGS SVSQQPGAAA AQEENAHSLY
SETSCKTLSS GTSNGPLSAE VKVNGPFPCT ISSEPSRQLA DTQRPKGPLT QVPSQISGQA
WLHSQLRPAT PPAASNLQNH FVGALVKSEN AGGPVSCLQR VPVSVTSVPA SLSTSCASSE
ITSSSQLKNT ASVQIAGRST TFMAKVVTTS SAIARAITPP RAAVDSVSTV LAPSRTLISP
AATGKVSPTV LSTGMSIGNK PVPLTAPSNS AIMFDLANSL QAAMEGSGEI ELSKLDEKLI
QVLAWQRIQQ LFPPKATSLP SVLSTSKVQT TTATTQTEVP GKEVQARAVF YPLTGKGQAV
SMCYRTLYIG TGADMDVCLI NYGHCNYVSG KHACIFYDEN TKHYELLNYS EHGTTVDNVL
YSCDFSEKTS PTPPSSIVAK VQSVIKYCKS RKEEVVQEET VMSSQGQGLH AMVSYIVAAA
ILVAIYVVTY YNFLKGIPCR SDTSLRGKTV IVTGANTGIG KETALDMARR GARVILACRN
KERAEAAVFD IRRKSGNNQV IFMQLDLASL KSVRAFAETF LKSEPQLHVL INNAGVGSGN
KTVDGYNTVL GVNHLGHFLL THLLLDRLKQ CAPSRIVTVT SMMYRFGKVD FSNLNPPGKG
SIQQMRNYSC SKLCNILFVR ELANNLEGTK VTCYSVHPGV VNTEVFRYMK FWQKMLFFPF
AALFFRTPTD GAQTSIYCAV QEGIEKFSGR YFTNCKVQEV LPHARDDAVA RKLWEVSERM
VGLRSY
//
