ID A0A2K5N5Q8_CERAT Unreviewed; 1234 AA.
AC A0A2K5N5Q8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=High density lipoprotein binding protein {ECO:0000313|Ensembl:ENSCATP00000032804.1};
GN Name=HDLBP {ECO:0000313|Ensembl:ENSCATP00000032804.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000032804.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000032804.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A2K5N5Q8; -.
DR Ensembl; ENSCATT00000057075.1; ENSCATP00000032804.1; ENSCATG00000039363.1.
DR GeneTree; ENSGT00900000141059; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000039363; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd22405; KH-I_Vigilin_rpt1; 1.
DR CDD; cd22413; KH-I_Vigilin_rpt10; 1.
DR CDD; cd22414; KH-I_Vigilin_rpt11; 1.
DR CDD; cd22415; KH-I_Vigilin_rpt12; 1.
DR CDD; cd22418; KH-I_Vigilin_rpt15; 1.
DR CDD; cd22406; KH-I_Vigilin_rpt2; 1.
DR CDD; cd22407; KH-I_Vigilin_rpt3; 1.
DR CDD; cd22408; KH-I_Vigilin_rpt4; 1.
DR CDD; cd22409; KH-I_Vigilin_rpt5; 1.
DR CDD; cd02394; KH-I_Vigilin_rpt6; 1.
DR CDD; cd22410; KH-I_Vigilin_rpt7; 1.
DR CDD; cd22411; KH-I_Vigilin_rpt8; 1.
DR CDD; cd22412; KH-I_Vigilin_rpt9; 1.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 13.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR PANTHER; PTHR10627; SCP160; 1.
DR PANTHER; PTHR10627:SF34; VIGILIN; 1.
DR Pfam; PF00013; KH_1; 13.
DR SMART; SM00322; KH; 13.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 12.
DR PROSITE; PS50084; KH_TYPE_1; 13.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117}.
FT DOMAIN 149..217
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 221..289
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 294..362
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 363..429
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 434..502
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 506..575
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 580..650
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 654..723
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 728..797
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 801..870
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 874..974
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 975..1088
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT DOMAIN 1092..1161
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT REGION 913..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 778..805
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 930..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1234 AA; 137680 MW; 12511560D3D777E1 CRC64;
MSSVAVLTQE SFAEHRSGLV PQQIKVATLN SEEESDPPTY KDAFPPLPEK AACLESAQEP
AGAWGNKIRP IKASVITQVF HVPLEERKYK DMNQFGEGEQ AKICLEIMQR TGAHLELSLA
KDQGLSIMVS GKLDAVMKAR KDIVARLQTQ ASATVAIPKE HHRFVIGKNG EKLQDLELKT
ATKIQIPRPD DPSNQIKITG TKEGIEKARH EVLLISAEQD KRAVERLEVE KAFHPFIAGP
YNRLVGEIMQ ETGTRINIPP PSVNRTEIVF TGEKEQLAQA VARIKKIYEE KKKKTTTIAV
EVKKSQHKYV IGPKGNSLQE ILERTGVSVE IPPSDSISET VILRGEPEKL GQALTEVYAK
ANSFTVSSVA APSWLHRFII GKKGQNLAKI TQQMPKVHIE FTEGEDKITL EGPTEDVNVA
QEQIEGMVKD LINRMDYVEI NIDHKFHRHL IGKSGANINR IKDQYKVSVR IPPDSEKSNL
IRIEGDPQGV QQAKRELLEL ASRMENERTK DLIIEQRFHR TIIGQKGERI REIRDKFPEV
IINFPDPAQK SDIVQLRGPK NEVEKCTKYM QKMVADLVEN SYSISVPIFK QFHKNIIGKG
GANIKKTRRD SCLLLIREES NTKIDLPTII ITGKRANCEA ARSRILSIQK DLANIAEVEV
SIPAKLHNSL IGTKGRLIRS IMEECGGVHI HFPVEGSGSD TVVIRGPSSD VEKAKKQLLH
LAEEKQTKSF TVDIRAKPEY HKFLIGKGGG KIRKVRDSTG ARVIFPAAED KDQDLITIIG
KEDAVREAQK ELEALIQNLD NVVEDSMLVD PKHHRHFVIR RGQVLREIAE EYGGVMVSFP
RSGTQSDKVT LKGAKDCVEA AKKRIQEIIE DLEAQVTLEC AIPQKFHRSV MGPKGSRIQQ
ITRDFSVQIK FPDREENPVH SAEPVVQENG DEAGEGREAK DSDPGSPRRC DIIIISGRKE
KCEAAKEALE ALVPVTIEVE VPFDLHRYVI GQKGSGIRKM MDEFEVDPFP GRPCHRSGLS
HPLLSASVRP QLLVDSHWLP SWRVGFPLTP GSQAPELQSD IIPQDQITIT GYEKNTEAAR
DAILRIVGEL EQMVSEDVPL DHRVHARIIG ARGKAIRKIM DEFKVDIRFP QSGAPDPNCV
TVTGLPENVE EAIDHILNLE EEYLADVVDS EVLQVYMKPP AHEEAKAPSR GFVVRDAPWT
ASSSEKAPDM SSSEEFPSFG AQVAPKTLPW GPKR
//
