ID VIGLN_RAT Reviewed; 1268 AA.
AC Q9Z1A6;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 24-JAN-2024, entry version 127.
DE RecName: Full=Vigilin;
DE AltName: Full=High density lipoprotein-binding protein;
DE Short=HDL-binding protein;
GN Name=Hdlbp; Synonyms=Hbp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Vinten J., Tranum-Jensen J., Voldstedlund M., Christiansen K., Carlsen J.,
RA Clausen H.;
RT "Rat homologue of HBP.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-35 AND SER-645, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Appears to play a role in cell sterol metabolism. It may
CC function to protect cells from over-accumulation of cholesterol (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
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DR EMBL; U90725; AAD09246.1; -; mRNA.
DR AlphaFoldDB; Q9Z1A6; -.
DR SMR; Q9Z1A6; -.
DR IntAct; Q9Z1A6; 1.
DR STRING; 10116.ENSRNOP00000074707; -.
DR iPTMnet; Q9Z1A6; -.
DR PhosphoSitePlus; Q9Z1A6; -.
DR jPOST; Q9Z1A6; -.
DR PaxDb; 10116-ENSRNOP00000048476; -.
DR UCSC; RGD:620962; rat.
DR AGR; RGD:620962; -.
DR RGD; 620962; Hdlbp.
DR eggNOG; KOG2208; Eukaryota.
DR InParanoid; Q9Z1A6; -.
DR PhylomeDB; Q9Z1A6; -.
DR Reactome; R-RNO-8964011; HDL clearance.
DR PRO; PR:Q9Z1A6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005844; C:polysome; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Acetylation; Cholesterol metabolism; Cytoplasm; HDL; Lipid metabolism;
KW Lipid transport; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Steroid metabolism; Sterol metabolism; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q00341"
FT CHAIN 2..1268
FT /note="Vigilin"
FT /id="PRO_0000050133"
FT DOMAIN 150..212
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 222..284
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 295..357
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 364..424
FT /note="KH 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 435..497
FT /note="KH 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 507..570
FT /note="KH 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 581..643
FT /note="KH 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 653..716
FT /note="KH 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 727..790
FT /note="KH 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 800..863
FT /note="KH 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 873..967
FT /note="KH 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 972..1034
FT /note="KH 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 1052..1117
FT /note="KH 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 1127..1190
FT /note="KH 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 910..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1214..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q00341"
FT MOD_RES 8
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00341"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00341"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 295
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 296
FT /note="Phosphothreonine"
FT /evidence="ECO:0000255"
FT MOD_RES 317
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00341"
FT MOD_RES 437
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q00341"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 991
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDJ3"
FT MOD_RES 1247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00341"
SQ SEQUENCE 1268 AA; 141584 MW; 7F1FE9C2ED3E560E CRC64;
MSSVAVLTQE SFAEHRSGLV PQQIIVATLN SEEESDPPTY KDAFPPLPEK AACLESAQEP
AGAWSNKIRP IKASVITQVF HVPLEERKYK DMNQFGEGEQ AKICLEIMQR TGAHLELSLA
KDQGLSIMVS GKLDAVMKAR KDIVARLQTQ ASATVPIPKE HHRFVIGKNG EKLQDLELKT
ATKIQIPRPD DPSNQIKITG TKEGIEKARH EVLLISAEQD KRAVKRLEVE KAFHPFIAGP
YNRLVGEIMQ ETGTRINIPP PSVNRTEIVF TGEKEQLAQA VARIKKIYEE KKKKTTTIAV
EVKKSQHKYV IGPKGNSLQE ILERTGVSVE IPPSDSISET VILRGEPEKL GQALTEVYAK
ANSFTVSSVS APSWLHRFII GKKGQNLAKI THQMPKVHIE FTEGEDKITL EGPTEDVNVA
QEQIEGMVKD LINRMDYVEI NIDHKFHRHL IGKSGANINR IKDQYKVSVR IPPDSEKSNL
IRIEGDPQGV QQAKRELLEL ASRMENERTK DLIIEQRFHR TIIGQKGERI REIRDKFPEV
IINFPDPAQK SEIVQLRGPK NEVEKCTKYM QKMVADLVEN SYSISVPIFK QFHKNIIGKG
GANIKKIREE SNTKIDLPAE NSNSETIVIT GKRANCEAAR SRILSIQKDL ANIAEVEVSI
PAKLHNSLIG TKGRLIRSIM EECGGVHIHF PVEGSGSDTV VIRGPSSDVE KAKKQLLHLA
EEKQTKSFTV DIRAKPEYHK FLIGKGGGKI RKVRDSTGAR IIFPAAEDKD QDLITIIGKE
DAVREAQKEL EALIQNLDNV VEDYMLVDPR HHRHFVIRRG QVLREIAEEY GGVMVSFPRS
GTQSDKVTLK GAKDCVEAAK KRIQEIIEDL EAQVTLECAI PQKFHRSVMG PKGSRIQQIT
RDYNVQIKFP DREENPVHSV EPSIQENGDE AGEGREAKET DPGSPRRCDI IVISGRKEKC
EAAKEALEAL VPVTIEVEVP FDLHRYIIGQ KGSGIRKMMD EFEVNIHVPA PELQSHTIAI
TGLAANLDRA KAGLLDRVKE LQAEQEDRAL RSFKLSVTVD PKYHPKIIGG KGAVITQIRL
EHDVNIQFPD KDDGNQPQDQ ITITGYEKNT EAARDAILKI VGELEQMVSE DVPLDHRVHA
RIIGARGKAI RKIMDEFKVD IRFPQSGAPD PNCVTVTGLP ENVEEAIDHI LNLEEEYLAD
VVDSEALQVY MKPPAHEESK APSKGFVVRD APWTSNSSEK APDMSSSEEI PTFGAQVAPK
TLPWGPKR
//
