ID Q8C3L6_MOUSE PRELIMINARY; PRT; 513 AA. AC Q8C3L6; DT 01-MAR-2003 (TrEMBLrel. 23, Created) DT 01-MAR-2003 (TrEMBLrel. 23, Last sequence update) DT 01-MAR-2004 (TrEMBLrel. 26, Last annotation update) DE Mus musculus 0 day neonate kidney cDNA, RIKEN full-length enriched DE library, clone:D630039P21 product:H+-transporting ATP synthase DE (EC 3.6.1.34) 58K chain homolog. GN Name=Atp6v1b1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX MEDLINE=99279253; PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Meth. Enzymol. 303:19-44(1999). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX MEDLINE=21085660; PubMed=11217851; DOI=10.1038/35055500; RA RIKEN FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [3] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J; TISSUE=Kidney; RA The FANTOM Consortium, RA the RIKEN Genome Exploration Research Group Phase I & II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [4] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX MEDLINE=20499374; PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to RT prepare full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [5] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J; TISSUE=Kidney; RX MEDLINE=20530913; PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., RA Sumi N., Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., RA Yamamoto R., Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., RA Fujiwake S., Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., RA Yoneda Y., Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., RA Okazaki Y., Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system-384-format RT sequencing pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [6] RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J; TISSUE=Kidney; RA Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P., RA Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., RA Hayashida K., Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., RA Hori F., Imotani K., Ishii Y., Itoh M., Kagawa I., Kasukawa T., RA Katoh H., Kawai J., Kojima Y., Kondo S., Konno H., Kouda M., Koya S., RA Kurihara C., Matsuyama T., Miyazaki A., Murata M., Nakamura M., RA Nishi K., Nomura K., Numazaki R., Ohno M., Ohsato N., Okazaki Y., RA Saito R., Saitoh H., Sakai C., Sakai K., Sakazume N., Sano H., RA Sasaki D., Shibata K., Shinagawa A., Shiraki T., Sogabe Y., Tagami M., RA Tagawa A., Takahashi F., Takaku-Akahira S., Takeda Y., Tanaka T., RA Tomaru A., Toya T., Yasunishi A., Muramatsu M., Hayashizaki Y.; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Noncatalytic subunit of the peripheral V1 complex of CC vacuolar ATPase. V-ATPase is responsible for acidifying a variety CC of intracellular compartments in eukaryotic cells (By similarity). CC -!- SUBUNIT: V-ATPase is an heteromultimeric enzyme composed of a CC peripheral catalytic V1 complex (main components: subunits A, B, CC C, D, E, and F) attached to an integral membrane V0 proton pore CC complex (main component: the proteolipid protein) (By similarity). CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK085549; BAC39470.1; -; mRNA. DR MGI; MGI:103285; Atp6v1b1. DR GO; GO:0016324; C:apical plasma membrane; IDA. DR GO; GO:0016323; C:basolateral plasma membrane; IDA. DR GO; GO:0005624; C:membrane fraction; IDA. DR InterPro; IPR000194; ATPase_a/bcentre. DR InterPro; IPR000793; ATPase_a/b_C. DR InterPro; IPR004100; ATPase_a/b_N. DR InterPro; IPR005723; ATP_synthV_B. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF00306; ATP-synt_ab_C; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR TIGRFAMs; TIGR01040; V-ATPase_V1_B; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. KW ATP synthesis; Hydrogen ion transport; Hydrolase; Ion transport; KW Transport. SQ SEQUENCE 513 AA; 56832 MW; B2F0AFE362ECB518 CRC64; MATTVDSRSS GFTGNSCDPG TAQEHVQAVT RNYITHPRVT YRTVCSVNGP LVVLDQVKFA QYAEIVNFTL PDVTQRSGQV LEVAGTKAIV QVFEGTSGID SQKTTCEFTG DILRTPVSED MLGRIFNGSG KPIDKGPAVM AEEFLDINGQ PINPHDRIYP EEMIQTGISP IDVMNSIARG QKIPIFSAAG LPHNEIAAQI CRQAGLVKKS KAVLDYHEDN FAIVFAAMGV NMETARFFKS DFEQNGTMGN VCLFLNLAND PTIERIITPR LALTTAEFLA YQCEKHVLVI LTDMSSYAEA LREVSAAREE VPGRRGFPGY MYTDLATIYE RAGRVEGRGG SITQIPILTM PNDDITHPIP DLTGFITEGQ IYVDRQLHNR QVYPPINVLP SLSRLMKSAI GEGMTRKDHG DVSNQLYACY AIGKDVQAMK AVVGEEALTS EDLLYLEFLQ KFEKNFITQG PYENRTVFES LDLGWKLLRI FPKEMLKRIP QSMTDEFYSR QGAQQDPASD TAL //