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Database: UniProt
Entry: A0A0D9R0F2_CHLSB
LinkDB: A0A0D9R0F2_CHLSB
Original site: A0A0D9R0F2_CHLSB 
ID   A0A0D9R0F2_CHLSB        Unreviewed;      1286 AA.
AC   A0A0D9R0F2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=High density lipoprotein binding protein {ECO:0000313|Ensembl:ENSCSAP00000002091.1};
GN   Name=HDLBP {ECO:0000313|Ensembl:ENSCSAP00000002091.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000002091.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000002091.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000002091.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AQIB01000054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01000055; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AQIB01000056; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 60711.ENSCSAP00000002091; -.
DR   Ensembl; ENSCSAT00000003817.1; ENSCSAP00000002091.1; ENSCSAG00000005781.1.
DR   eggNOG; KOG2208; Eukaryota.
DR   GeneTree; ENSGT00900000141059; -.
DR   OMA; DHAGQQV; -.
DR   OrthoDB; 5489311at2759; -.
DR   Proteomes; UP000029965; Chromosome 10.
DR   Bgee; ENSCSAG00000005781; Expressed in fibroblast and 7 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; cd22416; KH-I_Vigilin_rpt13; 1.
DR   CDD; cd22417; KH-I_Vigilin_rpt14; 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; 14.
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; 14.
DR   SMART; SM00322; KH; 14.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 12.
DR   PROSITE; PS50084; KH_TYPE_1; 14.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117}.
FT   DOMAIN          167..235
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          239..307
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          312..380
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          381..447
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          452..520
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          524..593
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          598..666
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          670..739
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          744..813
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          817..886
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          890..990
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          991..1057
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          1069..1140
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   DOMAIN          1144..1213
FT                   /note="K Homology"
FT                   /evidence="ECO:0000259|SMART:SM00322"
FT   REGION          15..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          932..964
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1251..1286
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          794..821
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        20..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        946..964
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1256..1270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1286 AA;  143525 MW;  5F293D94CE75CB67 CRC64;
     MSSVAVLTQE SFAEHRSGLV PQQIKEREDS TERMHPPVVS ALSVATLNSE EESDPPTYKD
     AFPPLPEKAA CLESAQEPAG AWGNKIRPIK ASVITQVFHV PLEERKYKDM NQFGEGEQAK
     ICLEIMQRTG AHLELSLAKD QGLSIMVSGK LDAVMKARKD IVARLQTQAS ATVAIPKEHH
     RFVIGKNGEK LQDLELKTAT KIQIPRPDDP SNQIKITGTK EGIEKARHEV LLISAEQDKR
     AVERLEVEKA FHPFIAGPYN RLVGEIMQET GTRINIPPPS VNRTEIVFTG EKEQLAQAVA
     RIKKIYEEKK KKTTTIAVEV KKSQHKYVIG PKGNSLQEIL ERTGVSVEIP PSDSISETVI
     LRGEPEKLGQ ALTEVYAKAN SFTVSSVAAP SWLHRFIIGK KGQNLAKITQ QMPKVHIEFT
     EGEDKITLEG PTEDVNVAQE QIEGMVKDLI NRMDYVEINI DHKFHRHLIG KSGANINRIK
     DQYKVSVRIP PDSEKSNLIR IEGDPQGVQQ AKRELLELAS RMENERTKDL IIEQRFHRTI
     IGQKGERIRE IRDKFPEVII NFPDPAQKSD IVQLRGPKNE VEKCTKYMQK MVADLVENSY
     SISVPIFKQF HKNIIGKGGA NIKKIREESN TKIDLPAENS NSETIIITGK RANCEAARSR
     ILSIQKDLAN IAEVEVSIPA KLHNSLIGTK GRLIRSIMEE CGGVHIHFPV EGSGSDTVVI
     RGPSSDVEKA KKQLLHLAEE KQTKSFTVDI RAKPEYHKFL IGKGGGKIRK VRDSTGARVI
     FPAAEDKDQD LITIIGKEDA VREAQKELEA LIQNLDNVVE DSMLVDPKHH RHFVIRRGQV
     LREIAEEYGG VMVSFPRSGT QSDKVTLKGA KDCVEAAKKR IQEIIEDLEA QVTLECAIPQ
     KFHRSVMGPK GSRIQQITRD FNVQIKFPDR EENPVHSVEP VVQENGDEAG EGREAKDSDP
     GSPRRCDIII ISGRKEKCEA AKEALEALVP VTIEVEVPFD LHRYVIGQKG SGIRKMMDEF
     EVNIHVPAPE LQSDIIAITG LAANLDRAKA GLLERVKELQ AEQEDRALRS FKLSVTVDPK
     YHPKIIGRKG AVITQIRLEH DVNIQFPDKD DGNQPQDQIT ITGYEKNTEA ARDAILRIVG
     ELEQMVSEDV PLDHRVHARI IGARGKAIRK IMDEFKVDIR FPQSGAPDPN CVTVTGLPEN
     VEEAIDHILN LEEEYLADVV DSEVLQVYMK PPAHEEAKAP SRGFVVRDAP WTASSSEKAP
     DMSSSEEFPS FGAQVAPKTL PWGPKR
//
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