ID A0A8I5ZQQ4_RAT Unreviewed; 471 AA. AC A0A8I5ZQQ4; DT 25-MAY-2022, integrated into UniProtKB/TrEMBL. DT 25-MAY-2022, sequence version 1. DT 02-OCT-2024, entry version 13. DE RecName: Full=Protein farnesyltransferase subunit beta {ECO:0000256|ARBA:ARBA00015798, ECO:0000256|RuleBase:RU365056}; DE Short=FTase-beta {ECO:0000256|RuleBase:RU365056}; DE EC=2.5.1.58 {ECO:0000256|ARBA:ARBA00012702, ECO:0000256|RuleBase:RU365056}; GN Name=Churc1 {ECO:0000313|Ensembl:ENSRNOP00000080450.1, GN ECO:0000313|RGD:1305116}; Synonyms=Fntb {ECO:0000313|RGD:620119}; 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 {ECO:0000313|Ensembl:ENSRNOP00000080450.1, ECO:0000313|Proteomes:UP000002494}; RN [1] {ECO:0000313|Ensembl:ENSRNOP00000080450.1, ECO:0000313|Proteomes:UP000002494} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000080450.1, RC ECO:0000313|Proteomes:UP000002494}; RX PubMed=15057822; DOI=10.1038/nature02426; RG Rat Genome Sequencing Project Consortium; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., RA Mockrin S., Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into mammalian RT evolution."; RL Nature 428:493-521(2004). RN [2] {ECO:0000313|Ensembl:ENSRNOP00000080450.1} RP IDENTIFICATION. RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000080450.1}; RG Ensembl; RL Submitted (JUN-2024) to UniProtKB. CC -!- FUNCTION: Essential subunit of the farnesyltransferase complex. CC Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate CC to a cysteine at the fourth position from the C-terminus of several CC proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. CC {ECO:0000256|RuleBase:RU365056}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = CC diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein]; CC Xref=Rhea:RHEA:13345, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11535, CC ChEBI:CHEBI:29950, ChEBI:CHEBI:33019, ChEBI:CHEBI:86019, CC ChEBI:CHEBI:175763; Evidence={ECO:0000256|RuleBase:RU365056}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|RuleBase:RU365056}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU365056}; CC -!- SUBUNIT: Heterodimer of FNTA and FNTB. {ECO:0000256|RuleBase:RU365056}. CC -!- SIMILARITY: Belongs to the protein prenyltransferase subunit beta CC family. {ECO:0000256|ARBA:ARBA00010497, ECO:0000256|RuleBase:RU365056}. 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 Ensembl; ENSRNOT00000120259.1; ENSRNOP00000080450.1; ENSRNOG00000007660.5. DR AGR; RGD:1305116; -. DR RGD; 1305116; Churc1. DR RGD; 620119; Fntb. DR GeneTree; ENSGT00950000183128; -. DR Proteomes; UP000002494; Chromosome 6. DR GO; GO:0005875; C:microtubule associated complex; IEA:Ensembl. DR GO; GO:0005965; C:protein farnesyltransferase complex; IEA:UniProtKB-UniRule. DR GO; GO:0004660; F:protein farnesyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IBA:GO_Central. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:InterPro. DR GO; GO:0097354; P:prenylation; IEA:UniProtKB-UniRule. DR CDD; cd02893; FTase; 1. DR Gene3D; 1.50.10.20; -; 1. DR InterPro; IPR026872; FTB. DR InterPro; IPR001330; PFTB_repeat. DR InterPro; IPR045089; PGGT1B-like. DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase. DR InterPro; IPR009508; Transcrpt_activator_Churchill. DR PANTHER; PTHR11774; GERANYLGERANYL TRANSFERASE TYPE BETA SUBUNIT; 1. DR PANTHER; PTHR11774:SF6; PROTEIN FARNESYLTRANSFERASE SUBUNIT BETA; 1. DR Pfam; PF06573; Churchill; 1. DR Pfam; PF00432; Prenyltrans; 5. DR SFLD; SFLDG01015; Prenyltransferase_Like_1; 1. DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1. PE 3: Inferred from homology; KW Metal-binding {ECO:0000256|RuleBase:RU365056}; KW Prenyltransferase {ECO:0000256|ARBA:ARBA00022602, KW ECO:0000256|RuleBase:RU365056}; KW Reference proteome {ECO:0000313|Proteomes:UP000002494}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365056}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365056}. SQ SEQUENCE 471 AA; 52692 MW; 5FE08D782C505AC7 CRC64; MCGDCVEKKY PNRGNTCLEN GSFLLNFAGC AVCSKRDFML ITNRSLKEED GEEIVTYDHL CKNCHHVIAR HEYTFSIMDE FQAKVEEKIQ EVFSSYKFNH LVPRLVLQRE KHFHYLKRGL RQLTDAYECL DASRPWLCYW ILHSLELLDE PIPQIVATDV CQFLELCQSP DGGFGGGPGQ YPHLAPTYAA VNALCIIGTE EAYNVINREK LLQYLYSLKQ PDGSFLMHVG GEVDVRSAYC AASVASLTNI ITPDLFEGTA EWIARCQNWE GGIGGVPGME AHGGYTFCGL AALVILKKER SLNLKSLLQW VTSRQMRFEG GFQGRCNKLV DGCYSFWQAG LLPLLHRALH AQGDPALSMS HWMFHQQALQ EYILMCCQCP AGGLLDKPGK SRDFYHTCYC LSGLSIAQHF GSGAMLHDVV MGVPENVLQP THPVYNIGPD KVIQATTHFL QKPVPGFEEC EDAVTSDPAT D //