ID   VIGLN_HUMAN             Reviewed;        1268 AA.
AC   Q00341; B4DTQ2; E7EM71; Q53QU2; Q9UCY3;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2024, sequence version 3.
DT   27-MAR-2024, entry version 216.
DE   RecName: Full=Vigilin;
DE   AltName: Full=High density lipoprotein-binding protein;
DE            Short=HDL-binding protein;
GN   Name=HDLBP; Synonyms=HBP, VGL;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1318310; DOI=10.1016/s0021-9258(19)49815-3;
RA   McKnight G.L., Reasoner J., Gilbert T., Sundquist K.O., Hokland B.,
RA   McKernan P.A., Champagne J., Johnson C.J., Bailey M.C., Holly R.,
RA   O'Hara P.J., Oram J.F.;
RT   "Cloning and expression of a cellular high density lipoprotein-binding
RT   protein that is up-regulated by cholesterol loading of cells.";
RL   J. Biol. Chem. 267:12131-12141(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Muscle;
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   [5]
RP   PROTEIN SEQUENCE OF 2-16; 73-87; 147-159; 208-222; 232-283; 315-324;
RP   350-377; 483-494; 496-503; 535-557; 649-663; 902-908 AND 1120-1137,
RP   CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RC   TISSUE=Mammary carcinoma, and Osteosarcoma;
RA   Bienvenut W.V., Matallanas D., Cooper W.N., Kolch W., Glen H., Frame M.C.;
RL   Submitted (MAR-2008) to UniProtKB.
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=8605996; DOI=10.1016/0014-5793(96)00204-9;
RA   Kugler S., Grunweller A., Probst C., Klinger M., Mueller P.K., Kruse C.;
RT   "Vigilin contains a functional nuclear localisation sequence and is present
RT   in both the cytoplasm and the nucleus.";
RL   FEBS Lett. 382:330-334(1996).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-437, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-8; SER-11; SER-31 AND
RP   SER-317, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-1247 AND SER-1252,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [18]
RP   STRUCTURE BY NMR OF 142-222; 345-434; 645-727 AND 964-1200.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the 1st, 4th, 8th, 12th, 13th and 14th KH type-I
RT   domains from human vigilin.";
RL   Submitted (NOV-2005) to the PDB data bank.
RN   [19]
RP   VARIANTS [LARGE SCALE ANALYSIS] ASN-568 AND VAL-939.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [20]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: Appears to play a role in cell sterol metabolism. It may
CC       function to protect cells from over-accumulation of cholesterol.
CC   -!- INTERACTION:
CC       Q00341; P49711: CTCF; NbExp=4; IntAct=EBI-1049478, EBI-932887;
CC       Q00341; Q06609: RAD51; NbExp=2; IntAct=EBI-1049478, EBI-297202;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8605996}. Nucleus
CC       {ECO:0000269|PubMed:8605996}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q00341-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q00341-2; Sequence=VSP_044924, VSP_044925;
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DR   EMBL; M64098; AAA35962.1; -; mRNA.
DR   EMBL; AK300312; BAG62064.1; -; mRNA.
DR   EMBL; AC104841; AAY14717.1; -; Genomic_DNA.
DR   EMBL; BC001179; AAH01179.1; -; mRNA.
DR   CCDS; CCDS2547.1; -. [Q00341-1]
DR   CCDS; CCDS58760.1; -. [Q00341-2]
DR   PIR; A44125; A44125.
DR   RefSeq; NP_001230829.1; NM_001243900.2. [Q00341-2]
DR   RefSeq; NP_001307894.1; NM_001320965.1. [Q00341-1]
DR   RefSeq; NP_001307895.1; NM_001320966.1. [Q00341-1]
DR   RefSeq; NP_005327.1; NM_005336.5. [Q00341-1]
DR   RefSeq; NP_976221.1; NM_203346.4. [Q00341-1]
DR   RefSeq; XP_005247059.2; XM_005247002.3. [Q00341-1]
DR   RefSeq; XP_005247060.2; XM_005247003.4.
DR   RefSeq; XP_006712538.1; XM_006712475.3.
DR   RefSeq; XP_011509360.1; XM_011511058.2. [Q00341-1]
DR   RefSeq; XP_011509362.1; XM_011511060.2. [Q00341-1]
DR   RefSeq; XP_016859429.1; XM_017003940.1.
DR   PDB; 1VIG; NMR; -; A=432-502.
DR   PDB; 1VIH; NMR; -; A=432-502.
DR   PDB; 2CTE; NMR; -; A=142-222.
DR   PDB; 2CTF; NMR; -; A=346-434.
DR   PDB; 2CTJ; NMR; -; A=645-726.
DR   PDB; 2CTK; NMR; -; A=964-1054.
DR   PDB; 2CTL; NMR; -; A=1044-1127.
DR   PDB; 2CTM; NMR; -; A=1119-1200.
DR   PDBsum; 1VIG; -.
DR   PDBsum; 1VIH; -.
DR   PDBsum; 2CTE; -.
DR   PDBsum; 2CTF; -.
DR   PDBsum; 2CTJ; -.
DR   PDBsum; 2CTK; -.
DR   PDBsum; 2CTL; -.
DR   PDBsum; 2CTM; -.
DR   AlphaFoldDB; Q00341; -.
DR   SMR; Q00341; -.
DR   BioGRID; 109319; 863.
DR   CORUM; Q00341; -.
DR   IntAct; Q00341; 77.
DR   MINT; Q00341; -.
DR   STRING; 9606.ENSP00000375836; -.
DR   ChEMBL; CHEMBL4295796; -.
DR   GlyGen; Q00341; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q00341; -.
DR   MetOSite; Q00341; -.
DR   PhosphoSitePlus; Q00341; -.
DR   SwissPalm; Q00341; -.
DR   BioMuta; HDLBP; -.
DR   DMDM; 218511884; -.
DR   EPD; Q00341; -.
DR   jPOST; Q00341; -.
DR   MassIVE; Q00341; -.
DR   MaxQB; Q00341; -.
DR   PaxDb; 9606-ENSP00000375836; -.
DR   PeptideAtlas; Q00341; -.
DR   ProteomicsDB; 16875; -.
DR   ProteomicsDB; 57845; -. [Q00341-1]
DR   Pumba; Q00341; -.
DR   Antibodypedia; 1371; 355 antibodies from 29 providers.
DR   DNASU; 3069; -.
DR   Ensembl; ENST00000310931.10; ENSP00000312042.4; ENSG00000115677.18. [Q00341-1]
DR   Ensembl; ENST00000391975.5; ENSP00000375836.1; ENSG00000115677.18. [Q00341-1]
DR   Ensembl; ENST00000391976.6; ENSP00000375837.2; ENSG00000115677.18. [Q00341-1]
DR   Ensembl; ENST00000427183.6; ENSP00000399139.2; ENSG00000115677.18. [Q00341-2]
DR   GeneID; 3069; -.
DR   KEGG; hsa:3069; -.
DR   MANE-Select; ENST00000310931.10; ENSP00000312042.4; NM_005336.6; NP_005327.1.
DR   UCSC; uc021vzg.1; human. [Q00341-1]
DR   AGR; HGNC:4857; -.
DR   CTD; 3069; -.
DR   DisGeNET; 3069; -.
DR   GeneCards; HDLBP; -.
DR   HGNC; HGNC:4857; HDLBP.
DR   HPA; ENSG00000115677; Low tissue specificity.
DR   MIM; 142695; gene.
DR   neXtProt; NX_Q00341; -.
DR   OpenTargets; ENSG00000115677; -.
DR   PharmGKB; PA29235; -.
DR   VEuPathDB; HostDB:ENSG00000115677; -.
DR   eggNOG; KOG2208; Eukaryota.
DR   GeneTree; ENSGT00900000141059; -.
DR   InParanoid; Q00341; -.
DR   OrthoDB; 5489311at2759; -.
DR   PhylomeDB; Q00341; -.
DR   TreeFam; TF323767; -.
DR   PathwayCommons; Q00341; -.
DR   Reactome; R-HSA-8964011; HDL clearance.
DR   SignaLink; Q00341; -.
DR   SIGNOR; Q00341; -.
DR   BioGRID-ORCS; 3069; 26 hits in 1165 CRISPR screens.
DR   ChiTaRS; HDLBP; human.
DR   EvolutionaryTrace; Q00341; -.
DR   GeneWiki; HDLBP; -.
DR   GenomeRNAi; 3069; -.
DR   Pharos; Q00341; Tbio.
DR   PRO; PR:Q00341; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q00341; Protein.
DR   Bgee; ENSG00000115677; Expressed in stromal cell of endometrium and 207 other cell types or tissues.
DR   ExpressionAtlas; Q00341; 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:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005844; C:polysome; IBA:GO_Central.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0008289; F:lipid binding; TAS:ProtInc.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0008203; P:cholesterol metabolic process; TAS:ProtInc.
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.
DR   Genevisible; Q00341; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cholesterol metabolism;
KW   Cytoplasm; Direct protein sequencing; 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:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895"
FT   CHAIN           2..1268
FT                   /note="Vigilin"
FT                   /id="PRO_0000050131"
FT   DOMAIN          158..229
FT                   /note="KH 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          230..302
FT                   /note="KH 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          303..371
FT                   /note="KH 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          372..442
FT                   /note="KH 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          443..514
FT                   /note="KH 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          515..588
FT                   /note="KH 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          589..660
FT                   /note="KH 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          661..734
FT                   /note="KH 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          735..807
FT                   /note="KH 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          808..880
FT                   /note="KH 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          881..979
FT                   /note="KH 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          980..1059
FT                   /note="KH 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          1060..1134
FT                   /note="KH 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   DOMAIN          1135..1209
FT                   /note="KH 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT   REGION          914..944
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1233..1268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        928..944
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1238..1252
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895"
FT   MOD_RES         8
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         35
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1A6"
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:0007744|PubMed:23186163"
FT   MOD_RES         437
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:15592455"
FT   MOD_RES         645
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Z1A6"
FT   MOD_RES         991
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VDJ3"
FT   MOD_RES         1247
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         1252
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         1
FT                   /note="M -> MHLAERDRWLFVATVMMHFVSIKSGFPGLCVGVRSTM (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044924"
FT   VAR_SEQ         291..359
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044925"
FT   VARIANT         61
FT                   /note="A -> S (in dbSNP:rs11891776)"
FT                   /id="VAR_047976"
FT   VARIANT         229
FT                   /note="V -> I (in dbSNP:rs7572799)"
FT                   /id="VAR_055981"
FT   VARIANT         418
FT                   /note="N -> S (in dbSNP:rs7578199)"
FT                   /id="VAR_024511"
FT   VARIANT         568
FT                   /note="K -> N (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036052"
FT   VARIANT         939
FT                   /note="D -> V (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036053"
FT   VARIANT         1264
FT                   /note="W -> L (in dbSNP:rs12281)"
FT                   /id="VAR_029279"
FT   STRAND          151..156
FT                   /evidence="ECO:0007829|PDB:2CTE"
FT   TURN            159..161
FT                   /evidence="ECO:0007829|PDB:2CTE"
FT   HELIX           162..166
FT                   /evidence="ECO:0007829|PDB:2CTE"
FT   STRAND          168..170
FT                   /evidence="ECO:0007829|PDB:2CTE"
FT   HELIX           172..179
FT                   /evidence="ECO:0007829|PDB:2CTE"
FT   STRAND          195..200
FT                   /evidence="ECO:0007829|PDB:2CTE"
FT   HELIX           202..220
FT                   /evidence="ECO:0007829|PDB:2CTE"
FT   STRAND          365..370
FT                   /evidence="ECO:0007829|PDB:2CTF"
FT   HELIX           376..380
FT                   /evidence="ECO:0007829|PDB:2CTF"
FT   TURN            381..384
FT                   /evidence="ECO:0007829|PDB:2CTF"
FT   HELIX           386..393
FT                   /evidence="ECO:0007829|PDB:2CTF"
FT   STRAND          395..401
FT                   /evidence="ECO:0007829|PDB:2CTF"
FT   STRAND          403..405
FT                   /evidence="ECO:0007829|PDB:2CTF"
FT   STRAND          407..412
FT                   /evidence="ECO:0007829|PDB:2CTF"
FT   HELIX           414..434
FT                   /evidence="ECO:0007829|PDB:2CTF"
FT   STRAND          436..442
FT                   /evidence="ECO:0007829|PDB:1VIG"
FT   HELIX           446..450
FT                   /evidence="ECO:0007829|PDB:1VIG"
FT   TURN            452..454
FT                   /evidence="ECO:0007829|PDB:1VIH"
FT   HELIX           457..464
FT                   /evidence="ECO:0007829|PDB:1VIG"
FT   STRAND          468..470
FT                   /evidence="ECO:0007829|PDB:1VIG"
FT   STRAND          476..487
FT                   /evidence="ECO:0007829|PDB:1VIG"
FT   HELIX           488..499
FT                   /evidence="ECO:0007829|PDB:1VIG"
FT   STRAND          656..659
FT                   /evidence="ECO:0007829|PDB:2CTJ"
FT   HELIX           662..669
FT                   /evidence="ECO:0007829|PDB:2CTJ"
FT   STRAND          671..673
FT                   /evidence="ECO:0007829|PDB:2CTJ"
FT   HELIX           674..683
FT                   /evidence="ECO:0007829|PDB:2CTJ"
FT   STRAND          687..689
FT                   /evidence="ECO:0007829|PDB:2CTJ"
FT   TURN            693..696
FT                   /evidence="ECO:0007829|PDB:2CTJ"
FT   STRAND          699..704
FT                   /evidence="ECO:0007829|PDB:2CTJ"
FT   HELIX           706..723
FT                   /evidence="ECO:0007829|PDB:2CTJ"
FT   STRAND          973..978
FT                   /evidence="ECO:0007829|PDB:2CTK"
FT   HELIX           981..988
FT                   /evidence="ECO:0007829|PDB:2CTK"
FT   STRAND          990..992
FT                   /evidence="ECO:0007829|PDB:2CTK"
FT   HELIX           993..1001
FT                   /evidence="ECO:0007829|PDB:2CTK"
FT   STRAND          1005..1007
FT                   /evidence="ECO:0007829|PDB:2CTK"
FT   TURN            1011..1013
FT                   /evidence="ECO:0007829|PDB:2CTK"
FT   STRAND          1017..1022
FT                   /evidence="ECO:0007829|PDB:2CTK"
FT   HELIX           1024..1050
FT                   /evidence="ECO:0007829|PDB:2CTK"
FT   STRAND          1054..1058
FT                   /evidence="ECO:0007829|PDB:2CTL"
FT   TURN            1061..1063
FT                   /evidence="ECO:0007829|PDB:2CTL"
FT   HELIX           1064..1067
FT                   /evidence="ECO:0007829|PDB:2CTL"
FT   STRAND          1070..1072
FT                   /evidence="ECO:0007829|PDB:2CTL"
FT   HELIX           1074..1082
FT                   /evidence="ECO:0007829|PDB:2CTL"
FT   STRAND          1085..1087
FT                   /evidence="ECO:0007829|PDB:2CTL"
FT   TURN            1091..1093
FT                   /evidence="ECO:0007829|PDB:2CTL"
FT   STRAND          1098..1105
FT                   /evidence="ECO:0007829|PDB:2CTL"
FT   HELIX           1107..1126
FT                   /evidence="ECO:0007829|PDB:2CTL"
FT   STRAND          1130..1133
FT                   /evidence="ECO:0007829|PDB:2CTM"
FT   TURN            1136..1138
FT                   /evidence="ECO:0007829|PDB:2CTM"
FT   HELIX           1139..1143
FT                   /evidence="ECO:0007829|PDB:2CTM"
FT   STRAND          1145..1147
FT                   /evidence="ECO:0007829|PDB:2CTM"
FT   HELIX           1149..1157
FT                   /evidence="ECO:0007829|PDB:2CTM"
FT   STRAND          1160..1162
FT                   /evidence="ECO:0007829|PDB:2CTM"
FT   STRAND          1173..1178
FT                   /evidence="ECO:0007829|PDB:2CTM"
FT   HELIX           1180..1198
FT                   /evidence="ECO:0007829|PDB:2CTM"
SQ   SEQUENCE   1268 AA;  141440 MW;  374ECB83D13A7431 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
     GANIKKIREE SNTKIDLPAE NSNSETIIIT GKRANCEAAR SRILSIQKDL ANIAEVEVSI
     PAKLHNSLIG TKGRLIRSIM EECGGVHIHF PVEGSGSDTV VIRGPSSDVE KAKKQLLHLA
     EEKQTKSFTV DIRAKPEYHK FLIGKGGGKI RKVRDSTGAR VIFPAAEDKD QDLITIIGKE
     DAVREAQKEL EALIQNLDNV VEDSMLVDPK HHRHFVIRRG QVLREIAEEY GGVMVSFPRS
     GTQSDKVTLK GAKDCVEAAK KRIQEIIEDL EAQVTLECAI PQKFHRSVMG PKGSRIQQIT
     RDFSVQIKFP DREENAVHST EPVVQENGDE AGEGREAKDC DPGSPRRCDI IIISGRKEKC
     EAAKEALEAL VPVTIEVEVP FDLHRYVIGQ KGSGIRKMMD EFEVNIHVPA PELQSDIIAI
     TGLAANLDRA KAGLLERVKE LQAEQEDRAL RSFKLSVTVD PKYHPKIIGR KGAVITQIRL
     EHDVNIQFPD KDDGNQPQDQ ITITGYEKNT EAARDAILRI VGELEQMVSE DVPLDHRVHA
     RIIGARGKAI RKIMDEFKVD IRFPQSGAPD PNCVTVTGLP ENVEEAIDHI LNLEEEYLAD
     VVDSEALQVY MKPPAHEEAK APSRGFVVRD APWTASSSEK APDMSSSEEF PSFGAQVAPK
     TLPWGPKR
//