ID   CC50A_PONAB             Reviewed;         361 AA.
AC   Q5R6C0;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Cell cycle control protein 50A {ECO:0000250|UniProtKB:Q9NV96};
DE   AltName: Full=P4-ATPase flippase complex beta subunit TMEM30A;
DE   AltName: Full=Transmembrane protein 30A;
GN   Name=TMEM30A {ECO:0000250|UniProtKB:Q9NV96}; Synonyms=CDC50A;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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). Can also mediate the
CC       export of alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A,
CC       ATP10B, ATP10D, ATP11A, ATP11B and ATP11C from the ER to other membrane
CC       localizations (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of various P4-ATPase flippase complexes which
CC       consists of a catalytic alpha subunit and an accessory beta subunit.
CC       Interacts with ATP8A1 to form a flippase complex; this complex forms an
CC       intermediate phosphoenzyme. Interacts with ATP8A2 to form a flippase
CC       complex (By similarity). ATP8B1:TMEM30A and ATP8B2:TMEM30A flippase
CC       complexes have been shown to form intermediate phosphoenzymes in vitro.
CC       Interacts with alpha subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A,
CC       ATP10B, ATP10D, ATP11A, ATP11B and ATP11C.
CC       {ECO:0000250|UniProtKB:Q9NV96}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9NV96}; Multi-
CC       pass membrane protein {ECO:0000250}. Golgi apparatus
CC       {ECO:0000250|UniProtKB:Q9NV96}. Cytoplasmic vesicle, secretory vesicle
CC       membrane {ECO:0000250|UniProtKB:Q9NV96}. Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q9NV96}. Photoreceptor inner segment
CC       {ECO:0000250|UniProtKB:Q17QL5}. Cell projection, cilium, photoreceptor
CC       outer segment {ECO:0000250|UniProtKB:Q17QL5}.
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; CR860571; CAH92696.1; -; mRNA.
DR   EMBL; CR860414; CAH92539.1; -; mRNA.
DR   AlphaFoldDB; Q5R6C0; -.
DR   SMR; Q5R6C0; -.
DR   STRING; 9601.ENSPPYP00000018784; -.
DR   eggNOG; KOG2952; Eukaryota.
DR   HOGENOM; CLU_025025_1_0_1; -.
DR   InParanoid; Q5R6C0; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:1990531; C:phospholipid-translocating ATPase complex; ISS:UniProtKB.
DR   GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR   GO; GO:0001750; C:photoreceptor outer segment; IEA:UniProtKB-SubCell.
DR   GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015914; P:phospholipid transport; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Acetylation; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW   Disulfide bond; Glycoprotein; Golgi apparatus; Lipid transport; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NV96"
FT   CHAIN           2..361
FT                   /note="Cell cycle control protein 50A"
FT                   /id="PRO_0000244471"
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..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..48
FT                   /note="Required for ATPase and aminophospholipid flippase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q17QL5"
FT   REGION          49..348
FT                   /note="Interaction with ATP8A2"
FT                   /evidence="ECO:0000250|UniProtKB:Q17QL5"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NV96"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        190
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        91..104
FT                   /evidence="ECO:0000250|UniProtKB:Q9NV96"
FT   DISULFID        94..102
FT                   /evidence="ECO:0000250|UniProtKB:Q9NV96"
FT   DISULFID        157..171
FT                   /evidence="ECO:0000250|UniProtKB:Q9NV96"
SQ   SEQUENCE   361 AA;  40635 MW;  BCC00C591BD19137 CRC64;
     MAMNYNAKDE VDGGPPCAPG GSAKTRRPDN TAFKQQRLPA WQPILTAGTV LPIFFIIGLI
     FIPIGIGIFV TSNNIREIEI DYTGTEPSSP CNKCLSPDVT PCICTINFTL EKSFEGNVFM
     YYGLSNFYQN HRRYVKSRDD SQLNGDSSAL LNPSKECEPY RRNEDKPIAP CGAIANSMFN
     DTLELFLIGN DSYPIPIALK KKGIAWWTDK NVKFRNPPGG DNLKERFKGT TKPVNWLKPV
     YMLDSDPDNN GFINEDFIVW MRTAALPTFR KLYRLIERKS DLHPTLPAGR YSLNVTYNYP
     VHYFDGRKRM ILSTISWMGG KNPFLGIAYI AVGSISFLLG VVLLVINHKY RNSSNTADIT
     I