Q9UJA2 (CRLS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cardiolipin synthase
Short name=CLS
EC=2.7.8.-

Alternative name(s):
Protein GCD10 homolog

Gene names

Name:	CRLS1
Synonyms:	C20orf155, CLS1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	301 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. Ref.1 Ref.6
Catalytic activity	2 Phosphatidylglycerol = diphosphatidylglycerol + glycerol.
Subcellular location	Mitochondrion inner membrane; Multi-pass membrane protein Ref.6.
Tissue specificity	Highly expressed in tissues such as heart, skeletal muscle and liver. Ref.6
Sequence similarities	Belongs to the CDP-alcohol phosphatidyltransferase class-I family.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cardiolipin biosynthetic process Traceable author statement. Source: Reactome phosphatidylglycerol acyl-chain remodeling Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Traceable author statement. Source: Reactome
Molecular_function	phosphotransferase activity, for other substituted phosphate groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UJA2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UJA2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-99: Missing.
     100-102: PSL → MPQ

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 301	301	Cardiolipin synthase		PRO_0000056816
Regions
	Transmembrane	109 – 129	21	Helical; Potential
	Transmembrane	133 – 153	21	Helical; Potential
	Transmembrane	190 – 212	23	Helical; Potential
	Transmembrane	250 – 270	21	Helical; Potential
	Transmembrane	272 – 292	21	Helical; Potential
Natural variations
	Alternative sequence	1 – 99	99	Missing in isoform 2.		VSP_041398
	Alternative sequence	100 – 102	3	PSL → MPQ in isoform 2.		VSP_041399

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 15CD406D29D3C405	FASTA	301	32,593
	10 20 30 40 50 60 MLALRVARGS WGALRGAAWA PGTRPSKRRA CWALLPPVPC CLGCLAERWR LRPAALGLRL 70 80 90 100 110 120 PGIGQRNHCS GAGKAAPRPA AGAGAAAEAP GGQWGPASTP SLYENPWTIP NMLSMTRIGL 130 140 150 160 170 180 APVLGYLIIE EDFNIALGVF ALAGLTDLLD GFIARNWANQ RSALGSALDP LADKILISIL 190 200 210 220 230 240 YVSLTYADLI PVPLTYMIIS RDVMLIAAVF YVRYRTLPTP RTLAKYFNPC YATARLKPTF 250 260 270 280 290 300 ISKVNTAVQL ILVAASLAAP VFNYADSIYL QILWCFTAFT TAASAYSYYH YGRKTVQVIK D
	Isoform 2 [UniParc]. Checksum: A7B6D9B4DEE662B4	FASTA	202	22,584
	10 20 30 40 50 60 MPQYENPWTI PNMLSMTRIG LAPVLGYLII EEDFNIALGV FALAGLTDLL DGFIARNWAN 70 80 90 100 110 120 QRSALGSALD PLADKILISI LYVSLTYADL IPVPLTYMII SRDVMLIAAV FYVRYRTLPT 130 140 150 160 170 180 PRTLAKYFNP CYATARLKPT FISKVNTAVQ LILVAASLAA PVFNYADSIY LQILWCFTAF 190 200 TTAASAYSYY HYGRKTVQVI KD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of human cardiolipin synthase." Houtkooper R.H., Akbari H., van Lenthe H., Kulik W., Wanders R.J.A., Frentzen M., Vaz F.M. FEBS Lett. 580:3059-3064(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[2]	Cheng Z., Gao G., Peng Y., Ren S., Chen Z., Han Z. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Liver cancer.
[3]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-301 (ISOFORM 1). Tissue: Melanoma.
[6]	"Cloning and characterization of a cDNA encoding human cardiolipin synthase (hCLS1)." Lu B., Xu F.Y., Jiang Y.J., Choy P.C., Hatch G.M., Grunfeld C., Feingold K.R. J. Lipid Res. 47:1140-1145(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ386730 mRNA. Translation: ABD46888.1. AF241784 mRNA. Translation: AAG44472.1. AL035461 Genomic DNA. Translation: CAB55278.1. CH471133 Genomic DNA. Translation: EAX10401.1. CH471133 Genomic DNA. Translation: EAX10402.1. AL832419 mRNA. Translation: CAH10649.1.
IPI	IPI00005167. IPI00895872.
RefSeq	NP_001120930.1. NM_001127458.1. NP_061968.1. NM_019095.4.
UniGene	Hs.224764.
3D structure databases
ProteinModelPortal	Q9UJA2.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000368140.
PTM databases
PhosphoSite	Q9UJA2.
Polymorphism databases
DMDM	37537857.
Proteomic databases
PaxDb	Q9UJA2.
PRIDE	Q9UJA2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000378863; ENSP00000368140; ENSG00000088766. ENST00000378868; ENSP00000368145; ENSG00000088766.
GeneID	54675.
KEGG	hsa:54675.
UCSC	uc002wmn.4. human. uc010gbr.3. human.
Organism-specific databases
CTD	54675.
GeneCards	GC20P005986.
HGNC	HGNC:16148. CRLS1.
MIM	608188. gene.
neXtProt	NX_Q9UJA2.
PharmGKB	PA25697.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0558.
HOGENOM	HOG000010898.
HOVERGEN	HBG051203.
InParanoid	Q9UJA2.
KO	K08744.
OMA	SRYFNPC.
OrthoDB	EOG4RV2S8.
PhylomeDB	Q9UJA2.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	Q9UJA2.
Bgee	Q9UJA2.
CleanEx	HS_CRLS1.
Genevestigator	Q9UJA2.
GermOnline	ENSG00000088766. Homo sapiens.
Family and domain databases
InterPro	IPR000462. CDP-OH_P_trans. [Graphical view]
Pfam	PF01066. CDP-OH_P_transf. 1 hit. [Graphical view]
PROSITE	PS00379. CDP_ALCOHOL_P_TRANSF. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CRLS1. human.
GenomeRNAi	54675.
NextBio	57228.
SOURCE	Search...

Entry information

Entry name

CRLS1_HUMAN

Accession

Primary (citable) accession number: Q9UJA2
Secondary accession number(s): D3DW09 , E9PAT4, Q27RP0, Q69YQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	May 1, 2000
Last modified:	April 3, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.