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Entry version 99 (12 Aug 2020)
Sequence version 1 (02 May 2006)
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Protein

3-hydroxy-3-methylglutaryl-coenzyme A reductase

Gene

HMGCR

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at transcript leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Transmembrane glycoprotein that is the rate-limiting enzyme in cholesterol biosynthesis as well as in the biosynthesis of nonsterol isoprenoids that are essential for normal cell function including ubiquinone and geranylgeranyl proteins.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Regulated by a negative feedback mechanism through sterols and non-sterol metabolites derived from mevalonate.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: (R)-mevalonate biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes (R)-mevalonate from acetyl-CoA.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. 3-hydroxy-3-methylglutaryl coenzyme A synthase, 3-hydroxy-3-methylglutaryl coenzyme A synthase (HMGCS2), 3-hydroxy-3-methylglutaryl coenzyme A synthase (HMGCS1), 3-hydroxy-3-methylglutaryl coenzyme A synthase (HMGCS2), 3-hydroxy-3-methylglutaryl coenzyme A synthase (LOC110260333), 3-hydroxy-3-methylglutaryl coenzyme A synthase, Hydroxymethylglutaryl-CoA synthase, mitochondrial (HMGCS2), 3-hydroxy-3-methylglutaryl coenzyme A synthase (LOC110260333), 3-hydroxy-3-methylglutaryl coenzyme A synthase, 3-hydroxy-3-methylglutaryl coenzyme A synthase (LOC110260333), 3-hydroxy-3-methylglutaryl coenzyme A synthase (LOC110260333), 3-hydroxy-3-methylglutaryl coenzyme A synthase (HMGCS1), 3-hydroxy-3-methylglutaryl coenzyme A synthase, 3-hydroxy-3-methylglutaryl coenzyme A synthase (HMGCS1)
  3. 3-hydroxy-3-methylglutaryl coenzyme A reductase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR), 3-hydroxy-3-methylglutaryl-coenzyme A reductase, Hydroxymethylglutaryl-CoA reductase (NADPH), 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR), 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR), 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR), 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR)
This subpathway is part of the pathway (R)-mevalonate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-mevalonate from acetyl-CoA, the pathway (R)-mevalonate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei558Charge relay systemBy similarity1
Active sitei688Charge relay systemBy similarity1
Active sitei764Charge relay systemBy similarity1
Active sitei863Proton donorPROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processCholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
LigandNADP

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.34, 6170

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00058;UER00103

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
3-hydroxy-3-methylglutaryl-coenzyme A reductase (EC:1.1.1.34)
Short name:
HMG-CoA reductase
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:HMGCR
Synonyms:HMGR
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSus scrofa (Pig)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9823 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaSuinaSuidaeSus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000008227 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei10 – 39HelicalSequence analysisAdd BLAST30
Transmembranei57 – 78HelicalSequence analysisAdd BLAST22
Transmembranei90 – 114HelicalSequence analysisAdd BLAST25
Transmembranei124 – 149HelicalSequence analysisAdd BLAST26
Transmembranei160 – 187HelicalSequence analysisAdd BLAST28
Transmembranei192 – 220HelicalSequence analysisAdd BLAST29
Transmembranei315 – 339HelicalSequence analysisAdd BLAST25

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3593154

DrugCentral

More...
DrugCentrali
Q1W675

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002580201 – 8853-hydroxy-3-methylglutaryl-coenzyme A reductaseAdd BLAST885

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki89Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki248Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi281N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi296N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi419N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi517N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi867N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei869Phosphoserine; by AMPKBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Undergoes sterol-mediated ubiquitination and ER-associated degradation (ERAD). Accumulation of sterols in the endoplasmic reticulum (ER) membrane, triggers binding of the reductase to the ER membrane protein INSIG1. This INSIG1 binding leads to the recruitment of the ubiquitin ligase, AMFR/gp78 or RNF145, initiating ubiquitination of the reductase. The ubiquitinated reductase is then extracted from the ER membrane and delivered to cytosolic 26S proteosomes by a mechanism probably mediated by the ATPase Valosin-containing protein VCP/p97. Lys-248 is the main site of ubiquitination. Ubiquitination is enhanced by the presence of a geranylgeranylated protein.By similarity
N-glycosylated. Deglycosylated by NGLY1 on release from the endoplasmic reticulum (ER) in a sterol-mediated manner.By similarity

Keywords - PTMi

Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q1W675

PRoteomics IDEntifications database

More...
PRIDEi
Q1W675

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q1W675

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

High expression found in liver, heart, kidney, bladder and subcutaneous fat. Lower levels in lung, uterus and large intestine. Lowest levels in cerebrum, spleen, spinal cord, stomach, ovary, longissimus muscle, and small intestine.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

Interacts with INSIG1 (via its SSD); the interaction, accelerated by sterols, leads to the recruitment of HMGCR to AMFR/gp78 for its ubiquitination by the sterol-mediated ERAD pathway.

Interacts with UBIAD1 (By similarity).

By similarity

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9823.ENSSSCP00000014973

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q1W675

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q1W675

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini61 – 218SSDPROSITE-ProRule annotationAdd BLAST158

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni340 – 448LinkerAdd BLAST109
Regioni450 – 885CatalyticAdd BLAST436

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi75 – 78INSIG-binding motifBy similarity4

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the HMG-CoA reductase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2480, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q1W675

KEGG Orthology (KO)

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KOi
K00021

Database of Orthologous Groups

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OrthoDBi
907394at2759

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00643, HMG-CoA_reductase_classI, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.3270.10, 1 hit
3.30.70.420, 1 hit
3.90.770.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002202, HMG_CoA_Rdtase
IPR023074, HMG_CoA_Rdtase_cat_sf
IPR023076, HMG_CoA_Rdtase_CS
IPR004554, HMG_CoA_Rdtase_eu_arc
IPR004816, HMG_CoA_Rdtase_metazoan
IPR023282, HMG_CoA_Rdtase_N
IPR009023, HMG_CoA_Rdtase_NAD(P)-bd_sf
IPR009029, HMG_CoA_Rdtase_sub-bd_dom_sf
IPR000731, SSD

The PANTHER Classification System

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PANTHERi
PTHR10572, PTHR10572, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00368, HMG-CoA_red, 1 hit
PF12349, Sterol-sensing, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00071, HMGCOARDTASE

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55035, SSF55035, 1 hit
SSF56542, SSF56542, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00920, 2A060605, 1 hit
TIGR00533, HMG_CoA_R_NADP, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00066, HMG_COA_REDUCTASE_1, 1 hit
PS00318, HMG_COA_REDUCTASE_2, 1 hit
PS01192, HMG_COA_REDUCTASE_3, 1 hit
PS50065, HMG_COA_REDUCTASE_4, 1 hit
PS50156, SSD, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q1W675-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLSRLFRMHG LFVASHPWEV IVGTVTLTIC MMSMNMFTGN DKICGWNYEC
60 70 80 90 100
PKFEEDVLSS DIIILTITRC IAILYIYFQF QNLRQLGSKY ILGIAGLFTI
110 120 130 140 150
FSSFVFSTVV IHFLDKELTG LNEALPFFLL LIDLSRASAL AKFALSSNSQ
160 170 180 190 200
DEVRENIARG MAILGPTFTL DALVECLVIG VGTMSGVRQL EIMCCFGCMS
210 220 230 240 250
VLATYFVFMT FFPACVSLVL ELSRESREGR PIWQLSHFAR VLEGEENKPN
260 270 280 290 300
PVTQRVKIIM SLGLVLVHAH SRWIADPSPQ NSTADNSKVS LGLDENVSKR
310 320 330 340 350
IEPSVSLWQF YLSKMISMDI EQVITLTLAL LLAVKYIFFE QAETESTLSL
360 370 380 390 400
KNPITSPVVT QKKVTDDCCR REPTLVRNDQ KFHTVEEEAR INRERKVEVI
410 420 430 440 450
KPLVAETDTS SRPTFVVGNS TLDSSLELEM QEPEIQIPSE PRPNEECLQI
460 470 480 490 500
LGNAEKGAKF LSDAEIIQLV NAKHIPAYKL ETLMETHERG VSIRRQLLSK
510 520 530 540 550
KLPEPSSLQY LPYRDYNYSL VMGACCENVI GYMPIPVGVA GPLCLDGKEF
560 570 580 590 600
QVPMATTEGC LVASTNRGCR AIGLGGGASS RILADGMTPV VRFPRACDSA
610 620 630 640 650
EVKAWLETPE GFAVIKEAFD STSRFARLQK LQMSVAGRNL YIRFQSRSGD
660 670 680 690 700
AMGMNMISKG TEKALSKLHE YFPEMQILAV SGNYCTDKKP AAVNWIEGRG
710 720 730 740 750
KSVVCEAVIP AKVVREVLKT TTEAMVEVNI NKNLVGSAMA GSIGGYNAHA
760 770 780 790 800
ANIVTAIYIA CGQDAAQNVG SSNCITLMEA SGPTNEDLYI SCTMPSIEIG
810 820 830 840 850
TVGGGTSLLP QQACLQMLGV QGACKDNPGE NARQLARIVC GTVMAGELSL
860 870 880
MAALAAGHLV RSHMIHNRSK INLQDLQGTC TKKAA
Length:885
Mass (Da):97,151
Last modified:May 2, 2006 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i046E93BF1155FAD2
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
DQ531631 Genomic DNA Translation: ABF83891.1
DQ432054 mRNA Translation: ABD96089.1

NCBI Reference Sequences

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RefSeqi
NP_001116460.1, NM_001122988.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
100144446

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ssc:100144446

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ531631 Genomic DNA Translation: ABF83891.1
DQ432054 mRNA Translation: ABD96089.1
RefSeqiNP_001116460.1, NM_001122988.1

3D structure databases

SMRiQ1W675
ModBaseiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000014973

Chemistry databases

BindingDBiQ1W675
ChEMBLiCHEMBL3593154
DrugCentraliQ1W675

PTM databases

iPTMnetiQ1W675

Proteomic databases

PaxDbiQ1W675
PRIDEiQ1W675

Genome annotation databases

GeneIDi100144446
KEGGissc:100144446

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3156

Phylogenomic databases

eggNOGiKOG2480, Eukaryota
InParanoidiQ1W675
KOiK00021
OrthoDBi907394at2759

Enzyme and pathway databases

UniPathwayiUPA00058;UER00103
BRENDAi1.1.1.34, 6170

Family and domain databases

CDDicd00643, HMG-CoA_reductase_classI, 1 hit
Gene3Di1.10.3270.10, 1 hit
3.30.70.420, 1 hit
3.90.770.10, 1 hit
InterProiView protein in InterPro
IPR002202, HMG_CoA_Rdtase
IPR023074, HMG_CoA_Rdtase_cat_sf
IPR023076, HMG_CoA_Rdtase_CS
IPR004554, HMG_CoA_Rdtase_eu_arc
IPR004816, HMG_CoA_Rdtase_metazoan
IPR023282, HMG_CoA_Rdtase_N
IPR009023, HMG_CoA_Rdtase_NAD(P)-bd_sf
IPR009029, HMG_CoA_Rdtase_sub-bd_dom_sf
IPR000731, SSD
PANTHERiPTHR10572, PTHR10572, 1 hit
PfamiView protein in Pfam
PF00368, HMG-CoA_red, 1 hit
PF12349, Sterol-sensing, 1 hit
PRINTSiPR00071, HMGCOARDTASE
SUPFAMiSSF55035, SSF55035, 1 hit
SSF56542, SSF56542, 1 hit
TIGRFAMsiTIGR00920, 2A060605, 1 hit
TIGR00533, HMG_CoA_R_NADP, 1 hit
PROSITEiView protein in PROSITE
PS00066, HMG_COA_REDUCTASE_1, 1 hit
PS00318, HMG_COA_REDUCTASE_2, 1 hit
PS01192, HMG_COA_REDUCTASE_3, 1 hit
PS50065, HMG_COA_REDUCTASE_4, 1 hit
PS50156, SSD, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiHMDH_PIG
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q1W675
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: May 2, 2006
Last modified: August 12, 2020
This is version 99 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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