ID A0A2Y9IQH8_ENHLU Unreviewed; 1111 AA.
AC A0A2Y9IQH8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Protein kinase C-binding protein 1 isoform X7 {ECO:0000313|RefSeq:XP_022350511.1};
GN Name=LOC111141930 {ECO:0000313|RefSeq:XP_022350511.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022350511.1};
RN [1] {ECO:0000313|RefSeq:XP_022350511.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022350511.1};
RG RefSeq;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_022350511.1; XM_022494803.1.
DR AlphaFoldDB; A0A2Y9IQH8; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd05508; Bromo_RACK7; 1.
DR CDD; cd15538; PHD_PRKCBP1; 1.
DR CDD; cd20160; PWWP_PRKCBP1; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 6.10.140.2220; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR044075; PRKCBP1_PHD.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR021931; ZMYND8.
DR InterPro; IPR037967; ZMYND8_Bromo_dom.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR002893; Znf_MYND.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46453; PROTEIN KINASE C-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR46453:SF3; PROTEIN KINASE C-BINDING PROTEIN 1; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF12064; DUF3544; 2.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00855; PWWP; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|PROSITE-ProRule:PRU00035};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000313|RefSeq:XP_022350511.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Transferase {ECO:0000313|RefSeq:XP_022350511.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00134}.
FT DOMAIN 83..128
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 160..230
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT DOMAIN 272..322
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 952..986
FT /note="MYND-type"
FT /evidence="ECO:0000259|PROSITE:PS50865"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 994..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 899..948
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..649
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1111 AA; 122394 MW; A50FAE38D5CAED34 CRC64;
MHPQSLAEEE IKTEQEVVEG MDISTRSKDP GSTERTAQKR KFPSPPHSSN GHSPQDTSTS
PIKKKKKPGL LNNNNKEQDG RNDFYCWVCH REGQVLCCEL CPRVYHAKCL RLTSEPEGDW
FCPECEKITV AECIETQSKA MTMLTIEQLS YLLKFAIQKM KQPGTDAFQK PVPLEQHPDY
AEYIFHPMDL CTLEKNAKKK MYGCTEAFLA DAKWILHNCI IYNGGNHKLT QIAKVVIKIC
EHEMNEIEVC PECYLAACQK RDNWFCEPCS NPHPLVWAKL KGFPFWPAKA LRDKDGQVDA
RFFGQHDRAW VPINNCYLMS KEIPFSVKKT KSIFNSAMQE MEVYVENIRR KFGVFNYSPF
RTPYTPNSQY QMLLDPSNPS AGAAKVDKQE KVKLNFDMTA SPKILMSKPM LSGGAGRRIS
LSDMPRSPMS TNSSVHTGSD VEQDAEKKAT SSHFSASEES MDFLDKSTDR SKAEMDLKEL
SESVQQQTAP VPLISPKRQI RSRFQLNLDK TIESCKAQLG INEISEDVYT AVEHSDSEDS
EKSDSSDSEY ISDDEQKSKN EPEDTEDKEG SRVDKEPSAV KKKPKLASPV ETKEELKSTS
PASEKADPGS VKEKASPPPE KDFSEKAKAS PHSTKDKLKG KDETDSPTVH LGLDSDSESE
LVIDLGEDHS GREGRKNKKE PKETSPKQDV VGKAPPSTTA GSQSPPETPL LTRSSSQTPT
AGVTVTTSTT STVTAPATTA TAAAAATAAA AAAAAATAAA AATTTGSPVK KQRPLLPKET
APAVQRVAWN SSTVQQKEIT QSPSTSTITL VTSTQSSPLV TSSGSTSTLA SSVSADLPIA
TASADVAADI AKYTSKMMDA IKGTMTEIYN DLSKNTTGST IAEIRRLRIE IEKLQWLHQQ
ELSEMKHNLE LTMAEMRQSL EQERDRLMAE VKKQLELEKQ QAVDETKKKQ WCANCKKEAI
FYCCWNTSYC DYPCQQAHWP EHMKSCTQSA TAPQQEADAE VNSETLNKPS QGSSSSTQAA
PTETASTSKE KEAPAEKSKD SGSTLDLSGS RETPSSILLG SNQGSDHSRS SKSSCWSSSD
EKRGPTRSEH NASSSSKSLL PKESRLDTFW D
//