CC50B_MOUSE
ID CC50B_MOUSE Reviewed; 353 AA.
AC Q8BHG3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Cell cycle control protein 50B;
DE AltName: Full=Transmembrane protein 30B;
GN Name=Tmem30b; Synonyms=Cdc50b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Cecum, Ovary, Skin, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(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 (Probable). Can mediate the export of alpha subunits ATP8A1, ATP8B1,
CC ATP8B2 and ATP8B4 from the ER to the plasma membrane (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- SUBUNIT: Component of a P4-ATPase flippase complex which consists of a
CC catalytic alpha subunit and an accessory beta subunit (Probable).
CC Interacts with alpha subunits ATP8A1, ATP8B1, ATP8B2 and ATP8B4 (By
CC similarity). {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein.
CC -!- SIMILARITY: Belongs to the CDC50/LEM3 family. {ECO:0000305}.
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DR EMBL; AK030302; BAC26887.1; -; mRNA.
DR EMBL; AK033580; BAC28372.1; -; mRNA.
DR EMBL; AK037246; BAC29774.1; -; mRNA.
DR EMBL; AK169014; BAE40811.1; -; mRNA.
DR CCDS; CCDS25975.1; -.
DR RefSeq; NP_848830.1; NM_178715.3.
DR AlphaFoldDB; Q8BHG3; -.
DR SMR; Q8BHG3; -.
DR STRING; 10090.ENSMUSP00000037476; -.
DR GlyGen; Q8BHG3; 2 sites.
DR PhosphoSitePlus; Q8BHG3; -.
DR jPOST; Q8BHG3; -.
DR MaxQB; Q8BHG3; -.
DR PaxDb; Q8BHG3; -.
DR PRIDE; Q8BHG3; -.
DR ProteomicsDB; 265702; -.
DR Antibodypedia; 24420; 122 antibodies from 23 providers.
DR DNASU; 238257; -.
DR Ensembl; ENSMUST00000042975; ENSMUSP00000037476; ENSMUSG00000034435.
DR GeneID; 238257; -.
DR KEGG; mmu:238257; -.
DR UCSC; uc007nwm.1; mouse.
DR CTD; 161291; -.
DR MGI; MGI:2442082; Tmem30b.
DR VEuPathDB; HostDB:ENSMUSG00000034435; -.
DR eggNOG; KOG2952; Eukaryota.
DR GeneTree; ENSGT00390000004660; -.
DR HOGENOM; CLU_025025_1_0_1; -.
DR InParanoid; Q8BHG3; -.
DR OMA; AWQPMLS; -.
DR OrthoDB; 889671at2759; -.
DR PhylomeDB; Q8BHG3; -.
DR TreeFam; TF300873; -.
DR BioGRID-ORCS; 238257; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q8BHG3; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BHG3; protein.
DR Bgee; ENSMUSG00000034435; Expressed in epithelium of stomach and 145 other tissues.
DR ExpressionAtlas; Q8BHG3; baseline and differential.
DR Genevisible; Q8BHG3; MM.
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; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015247; F:aminophospholipid flippase activity; ISO:MGI.
DR GO; GO:0015917; P:aminophospholipid transport; ISO:MGI.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; ISO:MGI.
DR InterPro; IPR005045; CDC50/LEM3_fam.
DR InterPro; IPR030352; TMEM30B.
DR PANTHER; PTHR10926; PTHR10926; 1.
DR PANTHER; PTHR10926:SF19; PTHR10926:SF19; 1.
DR Pfam; PF03381; CDC50; 1.
DR PIRSF; PIRSF015840; DUF284_TM_euk; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Lipid transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..353
FT /note="Cell cycle control protein 50B"
FT /id="PRO_0000244475"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..315
FT /note="Exoplasmic loop"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 353 AA; 39218 MW; 205C7B24AC338DE8 CRC64;
MTWSATARGA HQPDNTAFTQ QRLPAWQPLL SAGIALPLFF CAGLAFIGLG LGLFYSSNGI
KELEYDYTGN PGTGDCSVCA AKGQGRAPPP GCACSWSFTL PELFPGPVYL YYELSNFYQN
NRRYGVSRDD AQLSGLASAL RHPANECAPY QFRSDGLPIA PCGAIANSLF NDSFSLWHQR
QPSDPFVEVP LDRTAIAWWT DYHVKFRNPP LVNGSLALAF RGTAPPPNWH RPVYELSPDP
NNTGFINQDF VVWMRTAALP TFRKLYARIR QGNYSAGLPR GTYRVNITYN YPVRAFGGHK
LIILSNISWM GGKNPFLGIA YLVVGSLCIV MGFVMLVVYI RYQDQDDDDN DDE
