LOCUS       NP_742031                437 aa            linear   ROD 26-APR-2024
DEFINITION  protein farnesyltransferase subunit beta [Rattus norvegicus].
ACCESSION   NP_742031
VERSION     NP_742031.1
DBSOURCE    REFSEQ: accession NM_172034.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 437)
  AUTHORS   Liu,Y., Qu,H.Q., Chang,X., Qu,J., Mentch,F.D., Nguyen,K., Tian,L.,
            Glessner,J., Sleiman,P.M.A. and Hakonarson,H.
  TITLE     Mutation burden analysis of six common mental disorders in African
            Americans by whole genome sequencing
  JOURNAL   Hum Mol Genet 31 (22), 3769-3776 (2022)
   PUBMED   35642741
REFERENCE   2  (residues 1 to 437)
  AUTHORS   Blanden,M.J., Suazo,K.F., Hildebrandt,E.R., Hardgrove,D.S.,
            Patel,M., Saunders,W.P., Distefano,M.D., Schmidt,W.K. and
            Hougland,J.L.
  TITLE     Efficient farnesylation of an extended C-terminal C(x)3X sequence
            motif expands the scope of the prenylated proteome
  JOURNAL   J Biol Chem 293 (8), 2770-2785 (2018)
   PUBMED   29282289
  REMARK    GeneRIF: Data suggest that substrate specificity of protein
            farnesyltransferase (subunits Fnta plus Fntb) is extensive; these
            results expand the scope of the potential prenylated proteome in
            this species. (Fnta = farnesyltransferase CAAX box alpha protein;
            Fntb = farnesyltransferase CAAX box beta protein)
REFERENCE   3  (residues 1 to 437)
  AUTHORS   Herlan,L., Schulz,A., Schulte,L., Schulz,H., Hubner,N. and
            Kreutz,R.
  TITLE     Novel candidate genes for impaired nephron development in a rat
            model with inherited nephron deficit and albuminuria
  JOURNAL   Clin Exp Pharmacol Physiol 42 (10), 1051-1058 (2015)
   PUBMED   26192016
REFERENCE   4  (residues 1 to 437)
  AUTHORS   Ibrahim,M.X., Sayin,V.I., Akula,M.K., Liu,M., Fong,L.G., Young,S.G.
            and Bergo,M.O.
  TITLE     Targeting isoprenylcysteine methylation ameliorates disease in a
            mouse model of progeria
  JOURNAL   Science 340 (6138), 1330-1333 (2013)
   PUBMED   23686339
REFERENCE   5  (residues 1 to 437)
  AUTHORS   Zhou,J., Vos,C.C., Gjyrezi,A., Yoshida,M., Khuri,F.R., Tamanoi,F.
            and Giannakakou,P.
  TITLE     The protein farnesyltransferase regulates HDAC6 activity in a
            microtubule-dependent manner
  JOURNAL   J Biol Chem 284 (15), 9648-9655 (2009)
   PUBMED   19228685
REFERENCE   6  (residues 1 to 437)
  AUTHORS   Long,S.B., Casey,P.J. and Beese,L.S.
  TITLE     Cocrystal structure of protein farnesyltransferase complexed with a
            farnesyl diphosphate substrate
  JOURNAL   Biochemistry 37 (27), 9612-9618 (1998)
   PUBMED   9657673
REFERENCE   7  (residues 1 to 437)
  AUTHORS   Finder,J.D., Litz,J.L., Blaskovich,M.A., McGuire,T.F., Qian,Y.,
            Hamilton,A.D., Davies,P. and Sebti,S.M.
  TITLE     Inhibition of protein geranylgeranylation causes a superinduction
            of nitric-oxide synthase-2 by interleukin-1beta in vascular smooth
            muscle cells
  JOURNAL   J Biol Chem 272 (21), 13484-13488 (1997)
   PUBMED   9153192
REFERENCE   8  (residues 1 to 437)
  AUTHORS   Park,H.W., Boduluri,S.R., Moomaw,J.F., Casey,P.J. and Beese,L.S.
  TITLE     Crystal structure of protein farnesyltransferase at 2.25 angstrom
            resolution
  JOURNAL   Science 275 (5307), 1800-1804 (1997)
   PUBMED   9065406
  REMARK    Erratum:[Science 1997 Apr 4;276(5309):21]
REFERENCE   9  (residues 1 to 437)
  AUTHORS   Zhang,F.L., Moomaw,J.F. and Casey,P.J.
  TITLE     Properties and kinetic mechanism of recombinant mammalian protein
            geranylgeranyltransferase type I
  JOURNAL   J Biol Chem 269 (38), 23465-23470 (1994)
   PUBMED   8089111
REFERENCE   10 (residues 1 to 437)
  AUTHORS   Chen,W.J., Andres,D.A., Goldstein,J.L., Russell,D.W. and Brown,M.S.
  TITLE     cDNA cloning and expression of the peptide-binding beta subunit of
            rat p21ras farnesyltransferase, the counterpart of yeast DPR1/RAM1
  JOURNAL   Cell 66 (2), 327-334 (1991)
   PUBMED   1855253
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC087675.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC087675.1, M69056.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132262
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..437
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="6"
                     /map="6q24"
     Protein         1..437
                     /product="protein farnesyltransferase subunit beta"
                     /EC_number="2.5.1.58"
                     /note="FTase-beta; CAAX farnesyltransferase subunit beta;
                     ras proteins prenyltransferase subunit beta;
                     farnesyltransferase beta subunit; farnesyltransferase,
                     CAAX box, beta"
                     /calculated_mol_wt=48543
     Region          75..373
                     /region_name="FTase"
                     /note="Protein farnesyltransferase (FTase)_like proteins
                     containing the protein prenyltransferase (PTase) domain,
                     beta subunit (alpha 6 - alpha 6 barrel fold). FTases are a
                     subgroup of PTase family of lipid-modifying enzymes.
                     PTases catalyze the...; cd02893"
                     /db_xref="CDD:239223"
     Site            order(95,98..99,102,106,149,151..152,154..155,202,
                     205..206,248,250,254,297,299..300,303,352,361..362)
                     /site_type="active"
                     /note="active site cavity [active]"
                     /db_xref="CDD:239223"
     Site            order(98..99,102,151..152,202,297,352)
                     /site_type="active"
                     /note="peptide binding pocket [active]"
                     /db_xref="CDD:239223"
     Site            order(102,105,202,205,248,250,254,291,294,300,303,361)
                     /site_type="lipid-binding"
                     /note="lipid binding pocket [chemical binding]"
                     /db_xref="CDD:239223"
     Site            102
                     /site_type="other"
                     /note="Important for selectivity against geranylgeranyl
                     diphosphate. /evidence=ECO:0000250|UniProtKB:P49356;
                     propagated from UniProtKB/Swiss-Prot (Q02293.1)"
     Region          123..164
                     /region_name="PFTB 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02293.1)"
     Region          174..215
                     /region_name="PFTB 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02293.1)"
     Site            order(197,235,245..246,251,275,278,280..281,291..293)
                     /site_type="other"
                     /note="heterodimer interface [polypeptide binding]"
                     /db_xref="CDD:239223"
     Region          222..263
                     /region_name="PFTB 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02293.1)"
     Region          270..312
                     /region_name="PFTB 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02293.1)"
     Site            order(297,299,362)
                     /site_type="other"
                     /note="Zn2+ binding site [ion binding]"
                     /db_xref="CDD:239223"
     Region          332..374
                     /region_name="PFTB 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q02293.1)"
     Site            432
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2I1; propagated from
                     UniProtKB/Swiss-Prot (Q02293.1)"
     Site            436
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q8K2I1; propagated from
                     UniProtKB/Swiss-Prot (Q02293.1)"
     CDS             1..437
                     /gene="Fntb"
                     /coded_by="NM_172034.2:46..1359"
                     /db_xref="GeneID:64511"
                     /db_xref="RGD:620119"
ORIGIN      
        1 massssftyy cppssspvws eplyslrpeh arerlqddsv etvtsieqak veekiqevfs
       61 sykfnhlvpr lvlqrekhfh ylkrglrqlt dayecldasr pwlcywilhs lelldepipq
      121 ivatdvcqfl elcqspdggf gggpgqyphl aptyaavnal ciigteeayn vinrekllqy
      181 lyslkqpdgs flmhvggevd vrsaycaasv asltniitpd lfegtaewia rcqnweggig
      241 gvpgmeahgg ytfcglaalv ilkkerslnl ksllqwvtsr qmrfeggfqg rcnklvdgcy
      301 sfwqagllpl lhralhaqgd palsmshwmf hqqalqeyil mccqcpaggl ldkpgksrdf
      361 yhtcyclsgl siaqhfgsga mlhdvvmgvp envlqpthpv ynigpdkviq atthflqkpv
      421 pgfeecedav tsdpatd
//
