CC50A_RAT
ID CC50A_RAT Reviewed; 328 AA.
AC Q6AY41;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
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|RGD:1303315}; Synonyms=Cdc50a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
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 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). TP8B1: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; BC079203; AAH79203.1; -; mRNA.
DR RefSeq; NP_001004248.1; NM_001004248.1.
DR AlphaFoldDB; Q6AY41; -.
DR SMR; Q6AY41; -.
DR BioGRID; 256740; 1.
DR STRING; 10116.ENSRNOP00000015299; -.
DR GlyGen; Q6AY41; 2 sites.
DR iPTMnet; Q6AY41; -.
DR jPOST; Q6AY41; -.
DR PaxDb; Q6AY41; -.
DR PRIDE; Q6AY41; -.
DR Ensembl; ENSRNOT00000015299; ENSRNOP00000015299; ENSRNOG00000010895.
DR GeneID; 300857; -.
DR KEGG; rno:300857; -.
DR UCSC; RGD:1303315; rat.
DR CTD; 55754; -.
DR RGD; 1303315; Tmem30a.
DR eggNOG; KOG2952; Eukaryota.
DR GeneTree; ENSGT00390000004660; -.
DR HOGENOM; CLU_025025_1_0_1; -.
DR InParanoid; Q6AY41; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q6AY41; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000010895; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; Q6AY41; baseline and differential.
DR Genevisible; Q6AY41; RN.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015247; F:aminophospholipid flippase activity; ISO:RGD.
DR GO; GO:0015917; P:aminophospholipid transport; ISO:RGD.
DR GO; GO:0045332; P:phospholipid translocation; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:RGD.
DR GO; GO:0061092; P:positive regulation of phospholipid translocation; ISO:RGD.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; ISO:RGD.
DR GO; GO:0036010; P:protein localization to endosome; ISO:RGD.
DR GO; GO:0006855; P:xenobiotic transmembrane transport; ISO:RGD.
DR InterPro; IPR005045; CDC50/LEM3_fam.
DR InterPro; IPR030351; TMEM30A.
DR PANTHER; PTHR10926; PTHR10926; 2.
DR PANTHER; PTHR10926:SF17; PTHR10926:SF17; 2.
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..328
FT /note="Cell cycle control protein 50A"
FT /id="PRO_0000244472"
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..292
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..328
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..315
FT /note="Interaction with ATP8A2"
FT /evidence="ECO:0000250|UniProtKB:Q17QL5"
FT REGION 102..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9NV96"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 261
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT DISULFID 121..135
FT /evidence="ECO:0000250|UniProtKB:Q9NV96"
SQ SEQUENCE 328 AA; 37173 MW; EE3B6E0A33FB272F CRC64;
MAMNYSAKDE VDGGPTGPPG GAAKTRRPDN TAFKQQRLPA WQPILTAGTV LPTFFIIGLI
FIPIGIGIFV TSNNIREIEG NVFMYYGLSN FYQNHRRYVK SRDDSQLNGD PSALLNPSKE
CEPYRRNEDK PIAPCGAIAN SMFNDTLELF LVANESDPKP VPILLKKKGI AWWTDKNVKF
RNPPGKDSLQ EKFKDTTKPV NWHKPVYELD PDDESNNGFI NEDFIVWMRT AALPTFRKLY
RLIERTDDLH PTLPAGQYYL NITYNYPVHF FDGRKRMILS TISWMGGKNP FLGIAYITIG
SISFLLGVVL LVINHKYRNS SNTADITI
