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Q9NV96 (CC50A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cell cycle control protein 50A
Alternative name(s):
P4-ATPase flippase complex beta subunit TMEM30A
Transmembrane protein 30A
Gene names
Name:TMEM30A
Synonyms:C6orf67, CDC50A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accessory component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. The beta subunit may assist in binding of the phospholipid substrate. Required for the proper folding, assembly and ER to Golgi exit of the ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in regulation of neurite outgrowth, and, reconstituted to liposomes, predomiminantly transports phosphatidylserine (PS) and to a lesser extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase complex seems to play a role in regulation of cell migration probably involving flippase-mediated translocation of phosphatidylethanolamine (PE) at the plasma membrane. Required for the formation of the ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved in uptake of platelet-activating factor (PAF), synthetic drug alkylphospholipid edelfosine, and, probably in association with ATP8B1, of perifosine. Also mediate the export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from the ER to other membrane localizations. Ref.10 Ref.11 Ref.12 Ref.15

Subunit structure

Component of various P4-ATPase flippase complexes which consists of a catalytic alpha subunit and an accessory beta subunit. The ATP8A2:TMEM30A flippase complex has been purified, and ATP8B1:TMEM30A and ATP8B2:TMEM30A flippase complexes have been shown to form intermediate phosphoenzymes in vitro. Interacts with alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP11A, ATP11B and ATP11C. Ref.11 Ref.12 Ref.13 Ref.14

Subcellular location

Membrane; Multi-pass membrane protein By similarity. Cell membrane. Golgi apparatus. Cytoplasmic vesiclesecretory vesicle membrane By similarity. Apical cell membrane By similarity Ref.11 Ref.12 Ref.14.

Domain

The N-terminal domain seems to play a role in the reaction cycle of the catalytic subunit such as ATP8A2 By similarity.

Post-translational modification

N-glycosylated. Contains high mannose-type oligosaccharides By similarity.

Sequence similarities

Belongs to the CDC50/LEM3 family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NV96-1)

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: Q9NV96-2)

The sequence of this isoform differs from the canonical sequence as follows:
     79-114: Missing.
Isoform 3 (identifier: Q9NV96-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-119: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 361360Cell cycle control protein 50A
PRO_0000244469

Regions

Topological domain2 – 4948Cytoplasmic Potential
Transmembrane50 – 7021Helical; Potential
Topological domain71 – 325255Exoplasmic loop Potential
Transmembrane326 – 34621Helical; Potential
Topological domain347 – 36115Cytoplasmic Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.7
Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation1901N-linked (GlcNAc...) Ref.9
Glycosylation2941N-linked (GlcNAc...) Ref.8

Natural variations

Alternative sequence1 – 119119Missing in isoform 3.
VSP_019567
Alternative sequence79 – 11436Missing in isoform 2.
VSP_019568

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 64B3F28C3EB7801B

FASTA36140,684
        10         20         30         40         50         60 
MAMNYNAKDE VDGGPPCAPG GTAKTRRPDN TAFKQQRLPA WQPILTAGTV LPIFFIIGLI 

        70         80         90        100        110        120 
FIPIGIGIFV TSNNIREIEI DYTGTEPSSP CNKCLSPDVT PCFCTINFTL EKSFEGNVFM 

       130        140        150        160        170        180 
YYGLSNFYQN HRRYVKSRDD SQLNGDSSAL LNPSKECEPY RRNEDKPIAP CGAIANSMFN 

       190        200        210        220        230        240 
DTLELFLIGN DSYPIPIALK KKGIAWWTDK NVKFRNPPGG DNLEERFKGT TKPVNWLKPV 

       250        260        270        280        290        300 
YMLDSDPDNN GFINEDFIVW MRTAALPTFR KLYRLIERKS DLHPTLPAGR YSLNVTYNYP 

       310        320        330        340        350        360 
VHYFDGRKRM ILSTISWMGG KNPFLGIAYI AVGSISFLLG VVLLVINHKY RNSSNTADIT 


I 

« Hide

Isoform 2 [UniParc].

Checksum: 40D7000253A6787F
Show »

FASTA32536,713
Isoform 3 [UniParc].

Checksum: 262B426C680712B5
Show »

FASTA24227,729

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Trachea.
[2]"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] (ISOFORMS 1 AND 3).
Tissue: Amygdala, Lymph node and Testis.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [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. expand/collapse author list , 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 status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[6]"Identification and characterization of CDC50A, CDC50B and CDC50C genes in silico."
Katoh Y., Katoh M.
Oncol. Rep. 12:939-943(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-294.
Tissue: Liver.
[9]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-190.
Tissue: Leukemic T-cell.
[10]"CDC50A plays a key role in the uptake of the anticancer drug perifosine in human carcinoma cells."
Munoz-Martinez F., Torres C., Castanys S., Gamarro F.
Biochem. Pharmacol. 80:793-800(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Heteromeric interactions required for abundance and subcellular localization of human CDC50 proteins and class 1 P4-ATPases."
van der Velden L.M., Wichers C.G., van Breevoort A.E., Coleman J.A., Molday R.S., Berger R., Klomp L.W., van de Graaf S.F.
J. Biol. Chem. 285:40088-40096(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATP8A1; ATP8A2; ATP8B1; ATP8B2 AND ATP8B4.
[12]"CDC50 proteins are critical components of the human class-1 P4-ATPase transport machinery."
Bryde S., Hennrich H., Verhulst P.M., Devaux P.F., Lenoir G., Holthuis J.C.
J. Biol. Chem. 285:40562-40572(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ATP8A1; ATP8B1; ATP8B2 AND ATP8B4.
[13]"Critical role of the beta-subunit CDC50A in the stable expression, assembly, subcellular localization, and lipid transport activity of the P4-ATPase ATP8A2."
Coleman J.A., Molday R.S.
J. Biol. Chem. 286:17205-17216(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATP8A2.
[14]"ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes to the trans-Golgi network in a CDC50 protein-independent manner."
Takatsu H., Baba K., Shima T., Umino H., Kato U., Umeda M., Nakayama K., Shin H.W.
J. Biol. Chem. 286:38159-38167(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATP11A; ATP11B AND ATP11C, SUBCELLULAR LOCATION.
[15]"Human TMEM30a promotes uptake of antitumor and bioactive choline phospholipids into mammalian cells."
Chen R., Brady E., McIntyre T.M.
J. Immunol. 186:3215-3225(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK001718 mRNA. Translation: BAA91859.1.
AK292823 mRNA. Translation: BAF85512.1.
AL832815 mRNA. Translation: CAH56262.1.
AL832490 mRNA. Translation: CAH56205.1.
AL162046 mRNA. Translation: CAB82389.1.
AL080250 Genomic DNA. Translation: CAI19900.1.
CH471051 Genomic DNA. Translation: EAW48743.1.
CH471051 Genomic DNA. Translation: EAW48744.1.
CH471051 Genomic DNA. Translation: EAW48745.1.
BC009006 mRNA. Translation: AAH09006.1.
CCDSCCDS47453.1. [Q9NV96-2]
CCDS4983.1. [Q9NV96-1]
PIRT47140.
RefSeqNP_001137430.1. NM_001143958.1. [Q9NV96-2]
NP_060717.1. NM_018247.3. [Q9NV96-1]
UniGeneHs.108530.

3D structure databases

ProteinModelPortalQ9NV96.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120872. 8 interactions.
IntActQ9NV96. 2 interactions.
MINTMINT-5006648.
STRING9606.ENSP00000359067.

Protein family/group databases

TCDB8.A.27.1.5. the cdc50 p-type atpase lipid flippase subunit (cdc50) family.

PTM databases

PhosphoSiteQ9NV96.

Polymorphism databases

DMDM74752991.

Proteomic databases

MaxQBQ9NV96.
PaxDbQ9NV96.
PeptideAtlasQ9NV96.
PRIDEQ9NV96.

Protocols and materials databases

DNASU55754.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000230461; ENSP00000230461; ENSG00000112697. [Q9NV96-1]
ENST00000370050; ENSP00000359067; ENSG00000112697. [Q9NV96-3]
ENST00000475111; ENSP00000431007; ENSG00000112697. [Q9NV96-2]
GeneID55754.
KEGGhsa:55754.
UCSCuc003phw.2. human. [Q9NV96-1]
uc003phx.2. human. [Q9NV96-2]

Organism-specific databases

CTD55754.
GeneCardsGC06M075962.
HGNCHGNC:16667. TMEM30A.
HPAHPA014561.
MIM611028. gene.
neXtProtNX_Q9NV96.
PharmGKBPA134936902.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5035.
HOGENOMHOG000209057.
HOVERGENHBG055537.
InParanoidQ9NV96.
OMADACKPED.
OrthoDBEOG7C5M8D.
PhylomeDBQ9NV96.
TreeFamTF300873.

Gene expression databases

ArrayExpressQ9NV96.
BgeeQ9NV96.
CleanExHS_TMEM30A.
GenevestigatorQ9NV96.

Family and domain databases

InterProIPR005045. DUF284_TM_euk.
[Graphical view]
PANTHERPTHR10926. PTHR10926. 1 hit.
PfamPF03381. CDC50. 1 hit.
[Graphical view]
PIRSFPIRSF015840. DUF284_TM_euk. 1 hit.
ProtoNetSearch...

Other

ChiTaRSTMEM30A. human.
GenomeRNAi55754.
NextBio60753.
PROQ9NV96.
SOURCESearch...

Entry information

Entry nameCC50A_HUMAN
AccessionPrimary (citable) accession number: Q9NV96
Secondary accession number(s): A8K9V8 expand/collapse secondary AC list , E1P539, Q658Z3, Q96H09, Q9NSL9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 94 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM