CC50A_CHICK
ID CC50A_CHICK Reviewed; 372 AA.
AC Q5F362;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 72.
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;
GN ORFNames=RCJMB04_32j24;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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. Required for the formation of the
CC ATP8A2, ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes (By
CC 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 {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 -!- SIMILARITY: Belongs to the CDC50/LEM3 family. {ECO:0000305}.
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DR EMBL; AJ851788; CAH65422.1; -; mRNA.
DR RefSeq; NP_001012897.1; NM_001012879.1.
DR AlphaFoldDB; Q5F362; -.
DR SMR; Q5F362; -.
DR STRING; 9031.ENSGALP00000025582; -.
DR PaxDb; Q5F362; -.
DR GeneID; 421861; -.
DR KEGG; gga:421861; -.
DR CTD; 55754; -.
DR VEuPathDB; HostDB:geneid_421861; -.
DR eggNOG; KOG2952; Eukaryota.
DR InParanoid; Q5F362; -.
DR OrthoDB; 889671at2759; -.
DR PhylomeDB; Q5F362; -.
DR PRO; PR:Q5F362; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
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: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:0045332; P:phospholipid translocation; IBA:GO_Central.
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 Cell membrane; Cell projection; Cytoplasmic vesicle; Disulfide bond;
KW Glycoprotein; Golgi apparatus; Lipid transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..372
FT /note="Cell cycle control protein 50A"
FT /id="PRO_0000244473"
FT TOPO_DOM 1..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..336
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..372
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 192
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 305
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 100..116
FT /evidence="ECO:0000250|UniProtKB:Q9NV96"
FT DISULFID 103..114
FT /evidence="ECO:0000250|UniProtKB:Q9NV96"
FT DISULFID 169..183
FT /evidence="ECO:0000250|UniProtKB:Q9NV96"
SQ SEQUENCE 372 AA; 41448 MW; D94C3A23FE5B4EB5 CRC64;
MAVNYSAKEE ADGHPAGGGP GGGATAGGGG AVKTRKPDNT AFKQQRLPAW QPILTAGTVL
PAFFIIGLIF IPIGIGIFVT SNNIREYEID YTGVEPSSPC NKCLNVSWDS TPPCTCTINF
TLEHSFESNV FMYYGLSNFY QNHRRYVKSR DDSQLNGDNS SLLNPSKECE PYRTNEDKPI
APCGAIANSM FNDTLELYHI ENDTRTAITL IKKGIAWWTD KNVKFRNPKG DGNLTALFQG
TTKPVNWPKP VYMLDSEPDN NGFINEDFIV WMRTAALPTF RKLYRLIERK SNLQPTLQAG
KYSLNITYNY PVHSFDGRKR MILSTISWMG GKNPFLGIAY ITVGSICFFL GVVLLIIHHK
YGNRNTSADI PN
