VIGLN_HUMAN
ID VIGLN_HUMAN Reviewed; 1268 AA.
AC Q00341; B4DTQ2; E7EM71; Q53QU2; Q9UCY3;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 207.
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), AND VARIANT ALA-61.
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), AND VARIANT ALA-61.
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), AND VARIANT ALA-61.
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 VARIANT [LARGE SCALE ANALYSIS] ALA-61, AND IDENTIFICATION BY MASS
RP 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.
DR RefSeq; NP_001307894.1; NM_001320965.1.
DR RefSeq; NP_001307895.1; NM_001320966.1.
DR RefSeq; NP_005327.1; NM_005336.5.
DR RefSeq; NP_976221.1; NM_203346.4.
DR RefSeq; XP_005247059.2; XM_005247002.3.
DR RefSeq; XP_005247060.2; XM_005247003.4.
DR RefSeq; XP_006712538.1; XM_006712475.3.
DR RefSeq; XP_011509360.1; XM_011511058.2.
DR RefSeq; XP_011509362.1; XM_011511060.2.
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; 229.
DR CORUM; Q00341; -.
DR IntAct; Q00341; 72.
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; Q00341; -.
DR PeptideAtlas; Q00341; -.
DR PRIDE; Q00341; -.
DR ProteomicsDB; 16875; -.
DR ProteomicsDB; 57845; -. [Q00341-1]
DR Antibodypedia; 1371; 329 antibodies from 29 providers.
DR DNASU; 3069; -.
DR Ensembl; ENST00000427183.6; ENSP00000399139.2; ENSG00000115677.18.
DR GeneID; 3069; -.
DR KEGG; hsa:3069; -.
DR UCSC; uc021vzg.1; human. [Q00341-1]
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 PharmGKB; PA29235; -.
DR VEuPathDB; HostDB:ENSG00000115677; -.
DR eggNOG; KOG2208; Eukaryota.
DR InParanoid; Q00341; -.
DR OrthoDB; 248989at2759; -.
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; 23 hits in 1089 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 205 other tissues.
DR ExpressionAtlas; Q00341; baseline and differential.
DR Genevisible; Q00341; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
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 Gene3D; 3.30.1370.10; -; 14.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR Pfam; PF00013; KH_1; 14.
DR SMART; SM00322; KH; 14.
DR SUPFAM; SSF54791; SSF54791; 12.
DR PROSITE; PS50084; KH_TYPE_1; 14.
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="S -> A (in dbSNP:rs11891776)"
FT /evidence="ECO:0000269|PubMed:1318310,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0007744|PubMed:21269460"
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; 141456 MW; 530C61A3CA9239CD CRC64;
MSSVAVLTQE SFAEHRSGLV PQQIKVATLN SEEESDPPTY KDAFPPLPEK AACLESAQEP
SGAWGNKIRP 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
