ID   VIGLN_MOUSE             Reviewed;        1268 AA.
AC   Q8VDJ3;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Vigilin;
DE   AltName: Full=High density lipoprotein-binding protein;
DE            Short=HDL-binding protein;
GN   Name=Hdlbp;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=18630941; DOI=10.1021/pr800223m;
RA   Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT   "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT   chromatography adsorbent for phosphoproteome analysis.";
RL   J. Proteome Res. 7:3957-3967(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-1252, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-991, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
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; BC021765; AAH21765.1; -; mRNA.
DR   EMBL; BC023806; AAH23806.1; -; mRNA.
DR   EMBL; BC025648; AAH25648.1; -; mRNA.
DR   EMBL; BC027779; AAH27779.1; -; mRNA.
DR   EMBL; BC027788; AAH27788.1; -; mRNA.
DR   EMBL; BC035301; AAH35301.1; -; mRNA.
DR   CCDS; CCDS15189.1; -.
DR   RefSeq; NP_001288293.1; NM_001301364.1.
DR   RefSeq; NP_598569.1; NM_133808.5.
DR   RefSeq; XP_006529137.1; XM_006529074.2.
DR   RefSeq; XP_006529138.1; XM_006529075.2.
DR   RefSeq; XP_006529139.1; XM_006529076.2.
DR   RefSeq; XP_006529140.1; XM_006529077.3.
DR   AlphaFoldDB; Q8VDJ3; -.
DR   SMR; Q8VDJ3; -.
DR   BioGRID; 225750; 25.
DR   IntAct; Q8VDJ3; 4.
DR   MINT; Q8VDJ3; -.
DR   STRING; 10090.ENSMUSP00000127903; -.
DR   GlyGen; Q8VDJ3; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8VDJ3; -.
DR   MetOSite; Q8VDJ3; -.
DR   PhosphoSitePlus; Q8VDJ3; -.
DR   SwissPalm; Q8VDJ3; -.
DR   EPD; Q8VDJ3; -.
DR   jPOST; Q8VDJ3; -.
DR   MaxQB; Q8VDJ3; -.
DR   PaxDb; 10090-ENSMUSP00000127903; -.
DR   ProteomicsDB; 297574; -.
DR   Pumba; Q8VDJ3; -.
DR   Antibodypedia; 1371; 355 antibodies from 29 providers.
DR   DNASU; 110611; -.
DR   Ensembl; ENSMUST00000042498.14; ENSMUSP00000043047.8; ENSMUSG00000034088.16.
DR   Ensembl; ENSMUST00000170883.8; ENSMUSP00000127903.2; ENSMUSG00000034088.16.
DR   GeneID; 110611; -.
DR   KEGG; mmu:110611; -.
DR   UCSC; uc007cdx.2; mouse.
DR   AGR; MGI:99256; -.
DR   CTD; 3069; -.
DR   MGI; MGI:99256; Hdlbp.
DR   VEuPathDB; HostDB:ENSMUSG00000034088; -.
DR   eggNOG; KOG2208; Eukaryota.
DR   GeneTree; ENSGT00900000141059; -.
DR   HOGENOM; CLU_008532_0_0_1; -.
DR   InParanoid; Q8VDJ3; -.
DR   OMA; DHAGQQV; -.
DR   OrthoDB; 5489311at2759; -.
DR   PhylomeDB; Q8VDJ3; -.
DR   TreeFam; TF323767; -.
DR   Reactome; R-MMU-8964011; HDL clearance.
DR   BioGRID-ORCS; 110611; 6 hits in 81 CRISPR screens.
DR   ChiTaRS; Hdlbp; mouse.
DR   PRO; PR:Q8VDJ3; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q8VDJ3; Protein.
DR   Bgee; ENSMUSG00000034088; Expressed in embryonic post-anal tail and 265 other cell types or tissues.
DR   ExpressionAtlas; Q8VDJ3; baseline and differential.
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; 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; 14.
DR   SMART; SM00322; KH; 14.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 14.
DR   PROSITE; PS50084; KH_TYPE_1; 14.
DR   Genevisible; Q8VDJ3; MM.
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_0000050132"
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..947
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1213..1268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..947
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:17242355,
FT                   ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
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:0000250|UniProtKB:Q9Z1A6"
FT   MOD_RES         991
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         1247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q00341"
FT   MOD_RES         1252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
SQ   SEQUENCE   1268 AA;  141743 MW;  2502F3D4E9EE230C CRC64;
     MSSVAVLTQE SFAEHRSGLV PQQIKVATLN SEEENDPPTY KDAFPPLPEK AACLESAQEP
     AGAWSNKIRP IKASVITQVF HVPLEERKYK DMNQFGEGEQ AKICLEIMQR TGAHLELSLA
     KDQGLSIMVS GKLDAVMKAR KDIVARLQTQ ASATVPIPKE HHRFVIGKNG EKLQDLELKT
     ATKIQIPRPD DPSNQIKITG TKEGIEKARH EVLLISAEQD KRAVERLEVE KAFHPFIAGP
     YNRLVGEIMQ ETGTRINIPP PSVNRTEIVF TGEKEQLAQA VARIKKIYEE KKKKTTTIAV
     EVKKSQHKYV IGPKGNSLQE ILERTGVSVE IPPSDSISET VILRGEPEKL GQALTEVYAK
     ANSFTVSSVS APSWLHRFII GKKGQNLAKI TQQMPKVHIE FTEGEDKITL EGPTEDVNVA
     QEQIEGMVKD LINRMDYVEI NIDHKFHRHL IGKSGANINR IKDQYKVSVR IPPDSEKSNL
     IRIEGDPQGV QQAKRELLEL ASRMENERTK DLIIEQRFHR TIIGQKGERI REIRDKFPEV
     IINFPDPAQK SDIVQLRGPK NEVEKCTKYM QKMVADLVEN SYSISVPIFK QFHKNIIGKG
     GANIKKIREE SNTKIDLPAE NSNSETIIIT GKRANCEAAR SRILSIQKDL ANIAEVEVSI
     PAKLHNSLIG TKGRLIRSIM EECGGVHIHF PVEGSGSDTV VIRGPSSDVE KAKKQLLHLA
     EEKQTKSFTV DIRAKPEYHK FLIGKGGGKI RKVRDSTGAR IIFPAAEDKD QDLITIIGKE
     DAVREAQKEL EALIQNLENV VEDYMLVDPK HHRHFVIRRG QVLREIAEEY GGVMVSFPRS
     GTQSDKVTLK GAKDCVEAAK KRIQEIIEDL EAQVTVECAI PQKFHRSVMG PKGSRIQQIT
     RDYNVQIKFP DREENPVHSV EPSIQENGDE AGEGREAKET DPGSPRRCDI IIISGRKEKC
     EAAKEALEAL VPVTIEVEVP FDLHRYIIGQ KGSGIRKMMD EFEVNIHVPA PELQSDTIAI
     TGLAANLDRA KAGLLDRVKE LQAEQEDRAL RSFKLSVTVD PKYHPKIIGR KGAVITQIRL
     EHEVNIQFPD KDDGNQPQDQ ITITGYEKNT EAARDAILKI VGELEQMVSE DVPLDHRVHA
     RIIGARGKAI RKIMDEFKVD IRFPQSGAPD PNCVTVTGLP ENVEEAIDHI LNLEEEYLAD
     VVDSEALQVY MKPPAHEESR APSKGFVVRD APWTSNSSEK APDMSSSEEF PSFGAQVAPK
     TLPWGPKR
//