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CC50B_HUMAN
ID   CC50B_HUMAN             Reviewed;         351 AA.
AC   Q3MIR4; B3KR84; Q14D00;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Cell cycle control protein 50B;
DE   AltName: Full=P4-ATPase flippase complex beta subunit TMEM30B;
DE   AltName: Full=Transmembrane protein 30B;
GN   Name=TMEM30B; Synonyms=CDC50B;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart, and Lung;
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   [4]
RP   IDENTIFICATION.
RX   PubMed=15375526;
RA   Katoh Y., Katoh M.;
RT   "Identification and characterization of CDC50A, CDC50B and CDC50C genes in
RT   silico.";
RL   Oncol. Rep. 12:939-943(2004).
RN   [5]
RP   INTERACTION WITH ATP8B1 AND ATP8B2.
RX   PubMed=20947505; DOI=10.1074/jbc.m110.139006;
RA   van der Velden L.M., Wichers C.G., van Breevoort A.E., Coleman J.A.,
RA   Molday R.S., Berger R., Klomp L.W., van de Graaf S.F.;
RT   "Heteromeric interactions required for abundance and subcellular
RT   localization of human CDC50 proteins and class 1 P4-ATPases.";
RL   J. Biol. Chem. 285:40088-40096(2010).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATP8A1; ATP8B1; ATP8B2
RP   AND ATP8B4.
RX   PubMed=20961850; DOI=10.1074/jbc.m110.139543;
RA   Bryde S., Hennrich H., Verhulst P.M., Devaux P.F., Lenoir G.,
RA   Holthuis J.C.;
RT   "CDC50 proteins are critical components of the human class-1 P4-ATPase
RT   transport machinery.";
RL   J. Biol. Chem. 285:40562-40572(2010).
RN   [7]
RP   INTERACTION WITH ATP8B1.
RX   PubMed=21914794; DOI=10.1074/jbc.m111.281006;
RA   Takatsu H., Baba K., Shima T., Umino H., Kato U., Umeda M., Nakayama K.,
RA   Shin H.W.;
RT   "ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes
RT   to the trans-Golgi network in a CDC50 protein-independent manner.";
RL   J. Biol. Chem. 286:38159-38167(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       (Probable). Can mediate the export of alpha subunits ATP8A1, ATP8B1,
CC       ATP8B2 and ATP8B4 from the ER to the plasma membrane.
CC       {ECO:0000269|PubMed:20961850, 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.
CC       {ECO:0000269|PubMed:20947505, ECO:0000269|PubMed:20961850,
CC       ECO:0000269|PubMed:21914794, ECO:0000305}.
CC   -!- INTERACTION:
CC       Q3MIR4; O43520: ATP8B1; NbExp=5; IntAct=EBI-9527107, EBI-9524729;
CC       Q3MIR4; P98198: ATP8B2; NbExp=3; IntAct=EBI-9527107, EBI-9539266;
CC       Q3MIR4; O15529: GPR42; NbExp=3; IntAct=EBI-9527107, EBI-18076404;
CC       Q3MIR4; Q01453: PMP22; NbExp=3; IntAct=EBI-9527107, EBI-2845982;
CC       Q3MIR4; O00767: SCD; NbExp=3; IntAct=EBI-9527107, EBI-2684237;
CC       Q3MIR4; P11686: SFTPC; NbExp=3; IntAct=EBI-9527107, EBI-10197617;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20961850};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:20961850}.
CC   -!- SIMILARITY: Belongs to the CDC50/LEM3 family. {ECO:0000305}.
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DR   EMBL; AK091169; BAG52296.1; -; mRNA.
DR   EMBL; CH471061; EAW80799.1; -; Genomic_DNA.
DR   EMBL; BC101726; AAI01727.1; -; mRNA.
DR   EMBL; BC113559; AAI13560.1; -; mRNA.
DR   CCDS; CCDS32093.1; -.
DR   RefSeq; NP_001017970.1; NM_001017970.2.
DR   PDB; 7VGH; EM; 3.39 A; A=1-351.
DR   PDBsum; 7VGH; -.
DR   AlphaFoldDB; Q3MIR4; -.
DR   SMR; Q3MIR4; -.
DR   BioGRID; 127780; 275.
DR   ComplexPortal; CPX-6283; ATP8B1-CDC50B P4-ATPase complex.
DR   ComplexPortal; CPX-6286; ATP8A1-CDC50B P4-ATPase complex.
DR   ComplexPortal; CPX-6303; ATP8B2-CDC50B P4-ATPase complex.
DR   ComplexPortal; CPX-6306; ATP8B4-CDC50B P4-ATPase complex.
DR   IntAct; Q3MIR4; 88.
DR   STRING; 9606.ENSP00000450842; -.
DR   TCDB; 8.A.27.1.6; the cdc50 p-type atpase lipid flippase subunit (cdc50) family.
DR   GlyGen; Q3MIR4; 3 sites.
DR   iPTMnet; Q3MIR4; -.
DR   PhosphoSitePlus; Q3MIR4; -.
DR   BioMuta; TMEM30B; -.
DR   DMDM; 109819759; -.
DR   jPOST; Q3MIR4; -.
DR   MassIVE; Q3MIR4; -.
DR   MaxQB; Q3MIR4; -.
DR   PaxDb; Q3MIR4; -.
DR   PeptideAtlas; Q3MIR4; -.
DR   PRIDE; Q3MIR4; -.
DR   ProteomicsDB; 61791; -.
DR   Antibodypedia; 24420; 122 antibodies from 23 providers.
DR   DNASU; 161291; -.
DR   Ensembl; ENST00000555868.2; ENSP00000450842.1; ENSG00000182107.7.
DR   GeneID; 161291; -.
DR   KEGG; hsa:161291; -.
DR   MANE-Select; ENST00000555868.2; ENSP00000450842.1; NM_001017970.3; NP_001017970.1.
DR   UCSC; uc001xfl.4; human.
DR   CTD; 161291; -.
DR   DisGeNET; 161291; -.
DR   GeneCards; TMEM30B; -.
DR   HGNC; HGNC:27254; TMEM30B.
DR   HPA; ENSG00000182107; Low tissue specificity.
DR   MIM; 611029; gene.
DR   neXtProt; NX_Q3MIR4; -.
DR   OpenTargets; ENSG00000182107; -.
DR   PharmGKB; PA134993260; -.
DR   VEuPathDB; HostDB:ENSG00000182107; -.
DR   eggNOG; KOG2952; Eukaryota.
DR   GeneTree; ENSGT00390000004660; -.
DR   HOGENOM; CLU_025025_1_0_1; -.
DR   InParanoid; Q3MIR4; -.
DR   OMA; AWQPMLS; -.
DR   PhylomeDB; Q3MIR4; -.
DR   TreeFam; TF300873; -.
DR   PathwayCommons; Q3MIR4; -.
DR   SignaLink; Q3MIR4; -.
DR   BioGRID-ORCS; 161291; 16 hits in 1065 CRISPR screens.
DR   ChiTaRS; TMEM30B; human.
DR   GenomeRNAi; 161291; -.
DR   Pharos; Q3MIR4; Tbio.
DR   PRO; PR:Q3MIR4; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q3MIR4; protein.
DR   Bgee; ENSG00000182107; Expressed in mucosa of sigmoid colon and 155 other tissues.
DR   Genevisible; Q3MIR4; HS.
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; IPI:ComplexPortal.
DR   GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR   GO; GO:0015247; F:aminophospholipid flippase activity; IDA:BHF-UCL.
DR   GO; GO:0015917; P:aminophospholipid transport; IDA:BHF-UCL.
DR   GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR   GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Glycoprotein; Lipid transport; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..351
FT                   /note="Cell cycle control protein 50B"
FT                   /id="PRO_0000244474"
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..351
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
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   351 AA;  38941 MW;  B68C91A784E33A44 CRC64;
     MTWSATARGA HQPDNTAFTQ QRLPAWQPLL SASIALPLFF CAGLAFIGLG LGLYYSSNGI
     KELEYDYTGD PGTGNCSVCA AAGQGRALPP PCSCAWYFSL PELFQGPVYL YYELTNFYQN
     NRRYGVSRDD AQLSGLPSAL RHPVNECAPY QRSAAGLPIA PCGAIANSLF NDSFSLWHQR
     QPGGPYVEVP LDRSGIAWWT DYHVKFRNPP LVNGSLALAF QGTAPPPNWR RPVYELSPDP
     NNTGFINQDF VVWMRTAALP TFRKLYARIR QGNYSAGLPR GAYRVNITYN YPVRAFGGHK
     LLIFSSISWM GGKNPFLGIA YLVVGSLCIL TGFVMLVVYI RYQDQDDDDE E
 
 
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