CC50A_BOVIN
ID CC50A_BOVIN Reviewed; 361 AA.
AC Q17QL5; F1MNX5;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
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};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, FUNCTION OF THE ATP8A2:TMEM30A FLIPPASE COMPLEX, IDENTIFICATION
RP IN ATP8A2:TMEM30A FLIPPASE COMPLEX, TOPOLOGY, SUBCELLULAR LOCATION, DOMAIN,
RP GLYCOSYLATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF THR-109; THR-182;
RP SER-192; THR-285 AND THR-296.
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).
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. {ECO:0000269|PubMed:21454556}.
CC -!- SUBUNIT: Component of various P4-ATPase flippase complexes which
CC consists of a catalytic alpha subunit and an accessory beta subunit
CC (PubMed:21454556). Interacts with ATP8A1 to form a flippase complex;
CC this complex forms an intermediate phosphoenzyme. Interacts with ATP8A2
CC to form a flippase complex (By similarity). ATP8B1:TMEM30A and
CC ATP8B2:TMEM30A flippase complexes have been shown to form intermediate
CC phosphoenzymes in vitro (PubMed:21454556). Interacts with alpha
CC subunits ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D,
CC ATP11A, ATP11B and ATP11C (By similarity).
CC {ECO:0000250|UniProtKB:Q9NV96, ECO:0000269|PubMed:21454556}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9NV96}; Multi-
CC pass membrane protein {ECO:0000250}. Golgi apparatus
CC {ECO:0000269|PubMed:21454556}. Cytoplasmic vesicle, secretory vesicle
CC membrane {ECO:0000250|UniProtKB:Q9NV96}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q9NV96}. Photoreceptor inner segment
CC {ECO:0000269|PubMed:21454556}. Cell projection, cilium, photoreceptor
CC outer segment {ECO:0000269|PubMed:21454556}.
CC -!- TISSUE SPECIFICITY: Expressed in photoreceptor cells; detected in
CC retina outer segment and other retinal layers (at protein level).
CC {ECO:0000269|PubMed:21454556}.
CC -!- DOMAIN: The N-terminal domain seems to play a role in the reaction
CC cycle of the catalytic subunit such as ATP8A2.
CC {ECO:0000269|PubMed:21454556}.
CC -!- PTM: N-glycosylated; contributes to ATP8A2:TMEM30A flippase complex
CC assembly but not to functional activity. {ECO:0000269|PubMed:21454556}.
CC -!- SIMILARITY: Belongs to the CDC50/LEM3 family. {ECO:0000305}.
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DR EMBL; DAAA02025272; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02025273; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DAAA02025274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC118287; AAI18288.1; -; mRNA.
DR RefSeq; NP_001068691.1; NM_001075223.1.
DR AlphaFoldDB; Q17QL5; -.
DR SMR; Q17QL5; -.
DR STRING; 9913.ENSBTAP00000006718; -.
DR PaxDb; Q17QL5; -.
DR PRIDE; Q17QL5; -.
DR Ensembl; ENSBTAT00000006718; ENSBTAP00000006718; ENSBTAG00000005100.
DR GeneID; 505797; -.
DR KEGG; bta:505797; -.
DR CTD; 55754; -.
DR VEuPathDB; HostDB:ENSBTAG00000005100; -.
DR VGNC; VGNC:36074; TMEM30A.
DR eggNOG; KOG2952; Eukaryota.
DR GeneTree; ENSGT00390000004660; -.
DR HOGENOM; CLU_025025_1_0_1; -.
DR InParanoid; Q17QL5; -.
DR OMA; TWNNDQP; -.
DR OrthoDB; 889671at2759; -.
DR TreeFam; TF300873; -.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000005100; Expressed in spermatid and 108 other tissues.
DR ExpressionAtlas; Q17QL5; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
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; IEA:Ensembl.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015247; F:aminophospholipid flippase activity; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0036010; P:protein localization to endosome; IEA:Ensembl.
DR GO; GO:0006855; P:xenobiotic transmembrane transport; IEA:Ensembl.
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 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_0000429840"
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:0000269|PubMed:21454556"
FT REGION 49..348
FT /note="Interaction with ATP8A2"
FT /evidence="ECO:0000269|PubMed:21454556"
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"
FT MUTAGEN 109
FT /note="T->A: Reduces ATP8A2 protein abundance. No effect on
FT interaction with ATP8A2, ATPase activity or flippase
FT activity."
FT /evidence="ECO:0000269|PubMed:21454556"
FT MUTAGEN 182
FT /note="T->A: Reduces ATP8A2 protein abundance. No effect on
FT interaction with ATP8A2 or ATPase activity."
FT /evidence="ECO:0000269|PubMed:21454556"
FT MUTAGEN 192
FT /note="S->A: Reduces ATP8A2 protein abundance. No effect on
FT interaction with ATP8A2 or ATPase activity."
FT /evidence="ECO:0000269|PubMed:21454556"
FT MUTAGEN 285
FT /note="T->A: No effect on ATP8A2 protein abundance,
FT interaction with ATP8A2 or ATPase activity."
FT /evidence="ECO:0000269|PubMed:21454556"
FT MUTAGEN 296
FT /note="T->A: Reduces ATP8A2 protein abundance. No effect on
FT interaction with ATP8A2 or ATPase activity."
FT /evidence="ECO:0000269|PubMed:21454556"
SQ SEQUENCE 361 AA; 40684 MW; BBE446F2595AFDE4 CRC64;
MAMNYNAKDE VDGGPPCPPG GTAKTRRPDN TAFKQQRLPA WQPILTAGTV LPTFFIIGLI
FIPIGIGIFV TSNNIREIEI DYTGTDPSSP CNKCLSPNVT PCVCTINFTL EQSFEGNVFM
YYGLSNFYQN HRRYVKSRDD GQLNGDPSAL LNPSKECEPY RRNEDKPIAP CGAIANSMFN
DTLELFQVGN ASDLTPIPLK KKGIAWWTDK NVKFRNPPGT DPLEERFKGT TKPVNWVKPV
YMLDSDEDNN GFINEDFIVW MRTAALPTFR KLYRLIERKN DLHPTLPAGR YYLNITYNYP
VHSFDGRKRM ILSTISWMGG KNPFLGIAYI TIGSISFLLG VVLLVINHKY RNSSNTADIT
I
