CC50A_HUMAN
ID CC50A_HUMAN Reviewed; 361 AA.
AC Q9NV96; A8K9V8; E1P539; Q658Z3; Q96H09; Q9NSL9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Cell cycle control protein 50A {ECO:0000305};
DE AltName: Full=P4-ATPase flippase complex beta subunit TMEM30A;
DE AltName: Full=Transmembrane protein 30A;
GN Name=TMEM30A {ECO:0000312|HGNC:HGNC:16667}; Synonyms=C6orf67, CDC50A;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Trachea;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Amygdala, Lymph node, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [6]
RP IDENTIFICATION.
RX PubMed=15375526;
RA Katoh Y., Katoh M.;
RT "Identification and characterization of CDC50A, CDC50B and CDC50C genes in
RT silico.";
RL Oncol. Rep. 12:939-943(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-294.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-190.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [10]
RP FUNCTION.
RX PubMed=20510206; DOI=10.1016/j.bcp.2010.05.017;
RA Munoz-Martinez F., Torres C., Castanys S., Gamarro F.;
RT "CDC50A plays a key role in the uptake of the anticancer drug perifosine in
RT human carcinoma cells.";
RL Biochem. Pharmacol. 80:793-800(2010).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATP8A1; ATP8A2;
RP ATP8B1; ATP8B2 AND ATP8B4.
RX PubMed=20947505; DOI=10.1074/jbc.m110.139006;
RA van der Velden L.M., Wichers C.G., van Breevoort A.E., Coleman J.A.,
RA Molday R.S., Berger R., Klomp L.W., van de Graaf S.F.;
RT "Heteromeric interactions required for abundance and subcellular
RT localization of human CDC50 proteins and class 1 P4-ATPases.";
RL J. Biol. Chem. 285:40088-40096(2010).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATP8A1; ATP8B1; ATP8B2
RP AND ATP8B4.
RX PubMed=20961850; DOI=10.1074/jbc.m110.139543;
RA Bryde S., Hennrich H., Verhulst P.M., Devaux P.F., Lenoir G.,
RA Holthuis J.C.;
RT "CDC50 proteins are critical components of the human class-1 P4-ATPase
RT transport machinery.";
RL J. Biol. Chem. 285:40562-40572(2010).
RN [13]
RP INTERACTION WITH ATP8A2.
RX PubMed=21454556; DOI=10.1074/jbc.m111.229419;
RA Coleman J.A., Molday R.S.;
RT "Critical role of the beta-subunit CDC50A in the stable expression,
RT assembly, subcellular localization, and lipid transport activity of the P4-
RT ATPase ATP8A2.";
RL J. Biol. Chem. 286:17205-17216(2011).
RN [14]
RP INTERACTION WITH ATP11A; ATP11B AND ATP11C, AND SUBCELLULAR LOCATION.
RX PubMed=21914794; DOI=10.1074/jbc.m111.281006;
RA Takatsu H., Baba K., Shima T., Umino H., Kato U., Umeda M., Nakayama K.,
RA Shin H.W.;
RT "ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes
RT to the trans-Golgi network in a CDC50 protein-independent manner.";
RL J. Biol. Chem. 286:38159-38167(2011).
RN [15]
RP FUNCTION.
RX PubMed=21289302; DOI=10.4049/jimmunol.1002710;
RA Chen R., Brady E., McIntyre T.M.;
RT "Human TMEM30a promotes uptake of antitumor and bioactive choline
RT phospholipids into mammalian cells.";
RL J. Immunol. 186:3215-3225(2011).
RN [16]
RP FUNCTION, AND INTERACTION WITH ATP8B1; ATP10A; ATP10B; ATP10D AND ATP11A.
RX PubMed=25947375; DOI=10.1074/jbc.m115.655191;
RA Naito T., Takatsu H., Miyano R., Takada N., Nakayama K., Shin H.W.;
RT "Phospholipid Flippase ATP10A Translocates Phosphatidylcholine and Is
RT Involved in Plasma Membrane Dynamics.";
RL J. Biol. Chem. 290:15004-15017(2015).
RN [17]
RP FUNCTION, AND INTERACTION WITH ATP11A.
RX PubMed=29799007; DOI=10.1038/s41467-018-04436-w;
RA Tsuchiya M., Hara Y., Okuda M., Itoh K., Nishioka R., Shiomi A., Nagao K.,
RA Mori M., Mori Y., Ikenouchi J., Suzuki R., Tanaka M., Ohwada T., Aoki J.,
RA Kanagawa M., Toda T., Nagata Y., Matsuda R., Takayama Y., Tominaga M.,
RA Umeda M.;
RT "Cell surface flip-flop of phosphatidylserine is critical for PIEZO1-
RT mediated myotube formation.";
RL Nat. Commun. 9:2049-2049(2018).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (3.90 ANGSTROMS) IN COMPLEX WITH ATP11C, FUNCTION,
RP AND MUTAGENESIS OF ARG-132; ARG-133 AND LYS-136.
RX PubMed=32493773; DOI=10.1074/jbc.ra120.014144;
RA Nakanishi H., Irie K., Segawa K., Hasegawa K., Fujiyoshi Y., Nagata S.,
RA Abe K.;
RT "Crystal structure of a human plasma membrane phospholipid flippase.";
RL J. Biol. Chem. 295:10180-10194(2020).
RN [19]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.83 ANGSTROMS)IN COMPLEX WITH ATP8A1,
RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-107; ASN-180 AND ASN-294, AND
RP INTERACTION WITH ATP8A1.
RX PubMed=31416931; DOI=10.1126/science.aay3353;
RA Hiraizumi M., Yamashita K., Nishizawa T., Nureki O.;
RT "Cryo-EM structures capture the transport cycle of the P4-ATPase
RT flippase.";
RL Science 365:1149-1155(2019).
CC -!- FUNCTION: Accessory component of a P4-ATPase flippase complex which
CC catalyzes the hydrolysis of ATP coupled to the transport of
CC aminophospholipids from the outer to the inner leaflet of various
CC membranes and ensures the maintenance of asymmetric distribution of
CC phospholipids. Phospholipid translocation seems also to be implicated
CC in vesicle formation and in uptake of lipid signaling molecules. The
CC beta subunit may assist in binding of the phospholipid substrate.
CC Required for the proper folding, assembly and ER to Golgi exit of the
CC ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in
CC regulation of neurite outgrowth, and, reconstituted to liposomes,
CC predomiminantly transports phosphatidylserine (PS) and to a lesser
CC extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase
CC complex seems to play a role in regulation of cell migration probably
CC involving flippase-mediated translocation of phosphatidylethanolamine
CC (PE) at the plasma membrane. Required for the formation of the ATP8A2,
CC ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved
CC in uptake of platelet-activating factor (PAF), synthetic drug
CC alkylphospholipid edelfosine, and, probably in association with ATP8B1,
CC of perifosine. Also mediates the export of alpha subunits ATP8A1,
CC ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and
CC ATP11C from the ER to other membrane localizations.
CC {ECO:0000269|PubMed:20510206, ECO:0000269|PubMed:20947505,
CC ECO:0000269|PubMed:20961850, ECO:0000269|PubMed:21289302,
CC ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:29799007,
CC ECO:0000269|PubMed:32493773}.
CC -!- SUBUNIT: Component of various P4-ATPase flippase complexes which
CC consists of a catalytic alpha subunit and an accessory beta subunit
CC (PubMed:31416931). Interacts with ATP8A1 to form a flippase complex;
CC this complex forms an intermediate phosphoenzyme (PubMed:31416931). The
CC ATP8A2:TMEM30A flippase complex has been purified, and ATP8B1:TMEM30A
CC and ATP8B2:TMEM30A flippase complexes have been shown to form
CC intermediate phosphoenzymes in vitro. Interacts with alpha subunits
CC ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B
CC and ATP11C. {ECO:0000269|PubMed:20947505, ECO:0000269|PubMed:20961850,
CC ECO:0000269|PubMed:21454556, ECO:0000269|PubMed:21914794,
CC ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:29799007,
CC ECO:0000269|PubMed:31416931, ECO:0000269|PubMed:32493773}.
CC -!- INTERACTION:
CC Q9NV96; O60312: ATP10A; NbExp=3; IntAct=EBI-2836942, EBI-26444318;
CC Q9NV96; P98196: ATP11A; NbExp=4; IntAct=EBI-2836942, EBI-21519640;
CC Q9NV96; Q9Y2G3: ATP11B; NbExp=2; IntAct=EBI-2836942, EBI-20857228;
CC Q9NV96; Q8NB49: ATP11C; NbExp=2; IntAct=EBI-2836942, EBI-11279131;
CC Q9NV96; Q9Y2Q0: ATP8A1; NbExp=5; IntAct=EBI-2836942, EBI-9539324;
CC Q9NV96; Q9Y2Q0-2: ATP8A1; NbExp=2; IntAct=EBI-2836942, EBI-21654619;
CC Q9NV96; O43520: ATP8B1; NbExp=9; IntAct=EBI-2836942, EBI-9524729;
CC Q9NV96; P98198: ATP8B2; NbExp=4; IntAct=EBI-2836942, EBI-9539266;
CC Q9NV96; Q8TF62: ATP8B4; NbExp=4; IntAct=EBI-2836942, EBI-9527207;
CC Q9NV96-1; O94823-1: ATP10B; NbExp=2; IntAct=EBI-26444832, EBI-26444823;
CC Q9NV96-2; P54253: ATXN1; NbExp=6; IntAct=EBI-12921610, EBI-930964;
CC Q9NV96-2; P42858: HTT; NbExp=3; IntAct=EBI-12921610, EBI-466029;
CC Q9NV96-2; P21145: MAL; NbExp=3; IntAct=EBI-12921610, EBI-3932027;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Cell membrane. Golgi apparatus. Cytoplasmic
CC vesicle, secretory vesicle membrane {ECO:0000250}. Apical cell membrane
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NV96-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NV96-2; Sequence=VSP_019568;
CC Name=3;
CC IsoId=Q9NV96-3; Sequence=VSP_019567;
CC -!- DOMAIN: The N-terminal domain seems to play a role in the reaction
CC cycle of the catalytic subunit such as ATP8A2. {ECO:0000250}.
CC -!- PTM: N-glycosylated. Contains high mannose-type oligosaccharides (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDC50/LEM3 family. {ECO:0000305}.
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DR EMBL; AK001718; BAA91859.1; -; mRNA.
DR EMBL; AK292823; BAF85512.1; -; mRNA.
DR EMBL; AL832815; CAH56262.1; -; mRNA.
DR EMBL; AL832490; CAH56205.1; -; mRNA.
DR EMBL; AL162046; CAB82389.1; -; mRNA.
DR EMBL; AL080250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48743.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48744.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48745.1; -; Genomic_DNA.
DR EMBL; BC009006; AAH09006.1; -; mRNA.
DR CCDS; CCDS47453.1; -. [Q9NV96-2]
DR CCDS; CCDS4983.1; -. [Q9NV96-1]
DR PIR; T47140; T47140.
DR RefSeq; NP_001137430.1; NM_001143958.1. [Q9NV96-2]
DR RefSeq; NP_060717.1; NM_018247.3. [Q9NV96-1]
DR PDB; 6K7G; EM; 3.30 A; C=1-361.
DR PDB; 6K7H; EM; 3.22 A; C=1-361.
DR PDB; 6K7I; EM; 3.22 A; C=1-361.
DR PDB; 6K7J; EM; 3.08 A; C=1-361.
DR PDB; 6K7K; EM; 3.04 A; C=1-361.
DR PDB; 6K7L; EM; 2.83 A; C=1-361.
DR PDB; 6K7M; EM; 2.95 A; C=1-361.
DR PDB; 6K7N; EM; 2.84 A; C=1-361.
DR PDB; 6LKN; X-ray; 3.90 A; C/F/J/N=1-361.
DR PDB; 7BSP; EM; 4.00 A; C=1-361.
DR PDB; 7BSQ; EM; 3.20 A; C=1-361.
DR PDB; 7BSS; EM; 3.30 A; C=1-361.
DR PDB; 7BSU; EM; 3.20 A; C=1-361.
DR PDB; 7BSV; EM; 3.00 A; C=1-361.
DR PDB; 7BSW; EM; 3.90 A; C=1-361.
DR PDB; 7VGI; EM; 3.36 A; A=1-361.
DR PDB; 7VGJ; EM; 3.98 A; B=1-361.
DR PDB; 7VSG; EM; 3.90 A; B=1-361.
DR PDB; 7VSH; EM; 3.40 A; C=1-361.
DR PDBsum; 6K7G; -.
DR PDBsum; 6K7H; -.
DR PDBsum; 6K7I; -.
DR PDBsum; 6K7J; -.
DR PDBsum; 6K7K; -.
DR PDBsum; 6K7L; -.
DR PDBsum; 6K7M; -.
DR PDBsum; 6K7N; -.
DR PDBsum; 6LKN; -.
DR PDBsum; 7BSP; -.
DR PDBsum; 7BSQ; -.
DR PDBsum; 7BSS; -.
DR PDBsum; 7BSU; -.
DR PDBsum; 7BSV; -.
DR PDBsum; 7BSW; -.
DR PDBsum; 7VGI; -.
DR PDBsum; 7VGJ; -.
DR PDBsum; 7VSG; -.
DR PDBsum; 7VSH; -.
DR AlphaFoldDB; Q9NV96; -.
DR SMR; Q9NV96; -.
DR BioGRID; 120872; 159.
DR ComplexPortal; CPX-6282; ATP8B1-CDC50A P4-ATPase complex.
DR ComplexPortal; CPX-6285; ATP8A1-CDC50A P4-ATPase complex.
DR ComplexPortal; CPX-6301; ATP8A2-CDC50A P4-ATPase complex.
DR ComplexPortal; CPX-6302; ATP8B2-CDC50A P4-ATPase complex.
DR ComplexPortal; CPX-6304; ATP8B3-CDC50A P4-ATPase complex.
DR ComplexPortal; CPX-6305; ATP8B4-CDC50A P4-ATPase complex.
DR ComplexPortal; CPX-6307; ATP10A-CDC50A P4-ATPase complex.
DR ComplexPortal; CPX-6308; ATP10B-CDC50A P4-ATPase complex.
DR ComplexPortal; CPX-6309; ATP10D-CDC50A P4-ATPase complex.
DR ComplexPortal; CPX-6310; ATP11A-CDC50A P4-ATPase complex.
DR ComplexPortal; CPX-6311; ATP11B-CDC50A P4-ATPase complex.
DR ComplexPortal; CPX-6312; ATP11C-CDC50A P4-ATPase complex.
DR IntAct; Q9NV96; 61.
DR MINT; Q9NV96; -.
DR STRING; 9606.ENSP00000230461; -.
DR TCDB; 1.A.17.1.30; the calcium-dependent chloride channel (ca-clc) family.
DR TCDB; 8.A.27.1.5; the cdc50 p-type atpase lipid flippase subunit (cdc50) family.
DR GlyGen; Q9NV96; 4 sites.
DR iPTMnet; Q9NV96; -.
DR PhosphoSitePlus; Q9NV96; -.
DR BioMuta; TMEM30A; -.
DR DMDM; 74752991; -.
DR EPD; Q9NV96; -.
DR jPOST; Q9NV96; -.
DR MassIVE; Q9NV96; -.
DR MaxQB; Q9NV96; -.
DR PaxDb; Q9NV96; -.
DR PeptideAtlas; Q9NV96; -.
DR PRIDE; Q9NV96; -.
DR ProteomicsDB; 82763; -. [Q9NV96-1]
DR ProteomicsDB; 82764; -. [Q9NV96-2]
DR ProteomicsDB; 82765; -. [Q9NV96-3]
DR Antibodypedia; 31507; 62 antibodies from 24 providers.
DR DNASU; 55754; -.
DR Ensembl; ENST00000230461.11; ENSP00000230461.6; ENSG00000112697.17. [Q9NV96-1]
DR Ensembl; ENST00000370050.9; ENSP00000359067.5; ENSG00000112697.17. [Q9NV96-3]
DR Ensembl; ENST00000475111.6; ENSP00000431007.1; ENSG00000112697.17. [Q9NV96-2]
DR Ensembl; ENST00000674151.1; ENSP00000500998.1; ENSG00000112697.17. [Q9NV96-3]
DR GeneID; 55754; -.
DR KEGG; hsa:55754; -.
DR MANE-Select; ENST00000230461.11; ENSP00000230461.6; NM_018247.4; NP_060717.1.
DR UCSC; uc003phw.3; human. [Q9NV96-1]
DR CTD; 55754; -.
DR DisGeNET; 55754; -.
DR GeneCards; TMEM30A; -.
DR HGNC; HGNC:16667; TMEM30A.
DR HPA; ENSG00000112697; Low tissue specificity.
DR MIM; 611028; gene.
DR neXtProt; NX_Q9NV96; -.
DR OpenTargets; ENSG00000112697; -.
DR PharmGKB; PA134936902; -.
DR VEuPathDB; HostDB:ENSG00000112697; -.
DR eggNOG; KOG2952; Eukaryota.
DR GeneTree; ENSGT00390000004660; -.
DR HOGENOM; CLU_025025_1_0_1; -.
DR InParanoid; Q9NV96; -.
DR OMA; TWNNDQP; -.
DR OrthoDB; 889671at2759; -.
DR PhylomeDB; Q9NV96; -.
DR TreeFam; TF300873; -.
DR PathwayCommons; Q9NV96; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q9NV96; -.
DR BioGRID-ORCS; 55754; 57 hits in 1082 CRISPR screens.
DR ChiTaRS; TMEM30A; human.
DR GenomeRNAi; 55754; -.
DR Pharos; Q9NV96; Tbio.
DR PRO; PR:Q9NV96; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NV96; protein.
DR Bgee; ENSG00000112697; Expressed in tendon of biceps brachii and 209 other tissues.
DR ExpressionAtlas; Q9NV96; baseline and differential.
DR Genevisible; Q9NV96; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0031901; C:early endosome membrane; IDA:ComplexPortal.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031902; C:late endosome membrane; IDA:ComplexPortal.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015247; F:aminophospholipid flippase activity; IDA:BHF-UCL.
DR GO; GO:0015917; P:aminophospholipid transport; IDA:BHF-UCL.
DR GO; GO:0045332; P:phospholipid translocation; IDA:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0061092; P:positive regulation of phospholipid translocation; IDA:UniProtKB.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0036010; P:protein localization to endosome; IMP:UniProtKB.
DR GO; GO:0006855; P:xenobiotic transmembrane transport; IDA:UniProtKB.
DR InterPro; IPR005045; CDC50/LEM3_fam.
DR InterPro; IPR030351; TMEM30A.
DR PANTHER; PTHR10926; PTHR10926; 1.
DR PANTHER; PTHR10926:SF17; PTHR10926:SF17; 1.
DR Pfam; PF03381; CDC50; 1.
DR PIRSF; PIRSF015840; DUF284_TM_euk; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Lipid transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..361
FT /note="Cell cycle control protein 50A"
FT /id="PRO_0000244469"
FT TOPO_DOM 2..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..325
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:31416931,
FT ECO:0007744|PDB:6K7G, ECO:0007744|PDB:6K7H,
FT ECO:0007744|PDB:6K7I, ECO:0007744|PDB:6K7J,
FT ECO:0007744|PDB:6K7K, ECO:0007744|PDB:6K7L,
FT ECO:0007744|PDB:6K7M"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:31416931,
FT ECO:0007744|PDB:6K7G, ECO:0007744|PDB:6K7H,
FT ECO:0007744|PDB:6K7I, ECO:0007744|PDB:6K7J,
FT ECO:0007744|PDB:6K7K, ECO:0007744|PDB:6K7L,
FT ECO:0007744|PDB:6K7M"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218,
FT ECO:0000269|PubMed:31416931, ECO:0007744|PDB:6K7G,
FT ECO:0007744|PDB:6K7H, ECO:0007744|PDB:6K7I,
FT ECO:0007744|PDB:6K7J, ECO:0007744|PDB:6K7K,
FT ECO:0007744|PDB:6K7L, ECO:0007744|PDB:6K7M"
FT DISULFID 91..104
FT /evidence="ECO:0000269|PubMed:31416931,
FT ECO:0007744|PDB:6K7G, ECO:0007744|PDB:6K7H,
FT ECO:0007744|PDB:6K7I, ECO:0007744|PDB:6K7J,
FT ECO:0007744|PDB:6K7K, ECO:0007744|PDB:6K7L,
FT ECO:0007744|PDB:6K7M, ECO:0007744|PDB:6K7N"
FT DISULFID 94..102
FT /evidence="ECO:0000269|PubMed:31416931,
FT ECO:0007744|PDB:6K7G, ECO:0007744|PDB:6K7H,
FT ECO:0007744|PDB:6K7I, ECO:0007744|PDB:6K7J,
FT ECO:0007744|PDB:6K7K, ECO:0007744|PDB:6K7L,
FT ECO:0007744|PDB:6K7M, ECO:0007744|PDB:6K7N"
FT DISULFID 157..171
FT /evidence="ECO:0000269|PubMed:31416931,
FT ECO:0007744|PDB:6K7G, ECO:0007744|PDB:6K7H,
FT ECO:0007744|PDB:6K7I, ECO:0007744|PDB:6K7J,
FT ECO:0007744|PDB:6K7K, ECO:0007744|PDB:6K7L,
FT ECO:0007744|PDB:6K7M"
FT VAR_SEQ 1..119
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_019567"
FT VAR_SEQ 79..114
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_019568"
FT MUTAGEN 132
FT /note="R->A: Decreases PS- and PE-dependent ATPase activity
FT of ATP11C:TMEM30A; when associated with A-133 and A-136."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 133
FT /note="R->A: Decreases PS- and PE-dependent ATPase activity
FT of ATP11C:TMEM30A; when associated with A-132 and A-136."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 136
FT /note="K->A: Decreases PS- and PE-dependent ATPase activity
FT of ATP11C:TMEM30A; when associated with A-132 and A-133."
FT /evidence="ECO:0000269|PubMed:32493773"
FT TURN 32..36
FT /evidence="ECO:0007829|PDB:6K7L"
FT HELIX 47..73
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:6K7L"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 103..112
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:6K7L"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:6K7L"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:6K7L"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:6K7L"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 182..188
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6K7M"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:6K7M"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:6K7L"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:6K7L"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:6K7L"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:6K7L"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:6K7L"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:6K7L"
FT HELIX 255..261
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 265..276
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 288..296
FT /evidence="ECO:0007829|PDB:6K7L"
FT TURN 302..305
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 307..314
FT /evidence="ECO:0007829|PDB:6K7L"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:6K7N"
FT HELIX 324..349
FT /evidence="ECO:0007829|PDB:6K7L"
SQ SEQUENCE 361 AA; 40684 MW; 64B3F28C3EB7801B CRC64;
MAMNYNAKDE VDGGPPCAPG GTAKTRRPDN TAFKQQRLPA WQPILTAGTV LPIFFIIGLI
FIPIGIGIFV TSNNIREIEI DYTGTEPSSP CNKCLSPDVT PCFCTINFTL EKSFEGNVFM
YYGLSNFYQN HRRYVKSRDD SQLNGDSSAL LNPSKECEPY RRNEDKPIAP CGAIANSMFN
DTLELFLIGN DSYPIPIALK KKGIAWWTDK NVKFRNPPGG DNLEERFKGT TKPVNWLKPV
YMLDSDPDNN GFINEDFIVW MRTAALPTFR KLYRLIERKS DLHPTLPAGR YSLNVTYNYP
VHYFDGRKRM ILSTISWMGG KNPFLGIAYI AVGSISFLLG VVLLVINHKY RNSSNTADIT
I
