ID   CENPE_MOUSE             Reviewed;        2474 AA.
AC   Q6RT24; O35059; Q3KQQ6; Q3V044; Q6PD00; Q7TPX4; Q80YB4; Q8BWX6;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-NOV-2023, entry version 123.
DE   RecName: Full=Centromere-associated protein E {ECO:0000312|EMBL:AAR85498.1};
DE   AltName: Full=Centromere protein E;
DE            Short=CENP-E {ECO:0000250|UniProtKB:Q02224};
DE   AltName: Full=Kinesin superfamily protein 10 {ECO:0000303|PubMed:9275178};
DE            Short=KIF10 {ECO:0000303|PubMed:9275178};
DE   AltName: Full=Motor domain of KIF10 {ECO:0000312|EMBL:BAA22386.1};
DE   Flags: Precursor;
GN   Name=Cenpe {ECO:0000312|MGI:MGI:1098230};
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] {ECO:0000305, ECO:0000312|EMBL:AAR85498.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH BUB1B, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=12925705; DOI=10.1083/jcb.200303167;
RA   Weaver B.A., Bonday Z.Q., Putkey F.R., Kops G.J., Silk A.D.,
RA   Cleveland D.W.;
RT   "Centromere-associated protein-E is essential for the mammalian mitotic
RT   checkpoint to prevent aneuploidy due to single chromosome loss.";
RL   J. Cell Biol. 162:551-563(2003).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAH52843.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-546 AND 1652-2474.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH52843.1}, and Czech II
RC   {ECO:0000312|EMBL:AAI06097.1};
RC   TISSUE=Brain {ECO:0000312|EMBL:AAH59032.1}, Egg
RC   {ECO:0000312|EMBL:AAH52843.1}, Mammary tumor
RC   {ECO:0000312|EMBL:AAI06097.1}, and Olfactory epithelium
RC   {ECO:0000312|EMBL:AAH49989.1};
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   [3] {ECO:0000305, ECO:0000312|EMBL:BAE21661.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-520 AND 1705-2474.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE21661.1};
RC   TISSUE=Spinal cord {ECO:0000312|EMBL:BAC33868.1}, and Testis
RC   {ECO:0000312|EMBL:BAE21661.1};
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).
RN   [4] {ECO:0000305, ECO:0000312|EMBL:BAA22386.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 82-241, AND TISSUE SPECIFICITY.
RC   STRAIN=ICR {ECO:0000312|EMBL:BAA22386.1};
RC   TISSUE=Hippocampus {ECO:0000269|PubMed:9275178};
RX   PubMed=9275178; DOI=10.1073/pnas.94.18.9654;
RA   Nakagawa T., Tanaka Y., Matsuoka E., Kondo S., Okada Y., Noda Y., Kanai Y.,
RA   Hirokawa N.;
RT   "Identification and classification of 16 new kinesin superfamily (KIF)
RT   proteins in mouse genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:9654-9659(1997).
RN   [5] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=12361599; DOI=10.1016/s1534-5807(02)00255-1;
RA   Putkey F.R., Cramer T., Morphew M.K., Silk A.D., Johnson R.S.,
RA   McIntosh J.R., Cleveland D.W.;
RT   "Unstable kinetochore-microtubule capture and chromosomal instability
RT   following deletion of CENP-E.";
RL   Dev. Cell 3:351-365(2002).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Microtubule plus-end-directed kinetochore motor which plays
CC       an important role in chromosome congression, microtubule-kinetochore
CC       conjugation and spindle assembly checkpoint activation. Drives
CC       chromosome congression (alignment of chromosomes at the spindle equator
CC       resulting in the formation of the metaphase plate) by mediating the
CC       lateral sliding of polar chromosomes along spindle microtubules towards
CC       the spindle equator and by aiding the establishment and maintenance of
CC       connections between kinetochores and spindle microtubules. The
CC       transport of pole-proximal chromosomes towards the spindle equator is
CC       favored by microtubule tracks that are detyrosinated. Acts as a
CC       processive bi-directional tracker of dynamic microtubule tips; after
CC       chromosomes have congressed, continues to play an active role at
CC       kinetochores, enhancing their links with dynamic microtubule ends.
CC       Suppresses chromosome congression in NDC80-depleted cells and
CC       contributes positively to congression only when microtubules are
CC       stabilized (By similarity). Plays an important role in the formation of
CC       stable attachments between kinetochores and spindle microtubules
CC       (PubMed:12925705). The stabilization of kinetochore-microtubule
CC       attachment also requires CENPE-dependent localization of other proteins
CC       to the kinetochore including BUB1B, MAD1 and MAD2. Plays a role in
CC       spindle assembly checkpoint activation (SAC) via its interaction with
CC       BUB1B resulting in the activation of its kinase activity, which is
CC       important for activating SAC (PubMed:12361599). Necessary for the
CC       mitotic checkpoint signal at individual kinetochores to prevent
CC       aneuploidy due to single chromosome loss (PubMed:12925705).
CC       {ECO:0000250|UniProtKB:Q02224, ECO:0000269|PubMed:12361599,
CC       ECO:0000269|PubMed:12925705}.
CC   -!- SUBUNIT: Monomer. Interacts with CENPF, SEPT7 KIF18A and PRC1 (By
CC       similarity). Interacts with BUB1B (PubMed:12925705). Interacts with
CC       SKAP; this interaction greatly favors SKAP binding to microtubules.
CC       Interacts with TRAPPC12 and CTCF (By similarity).
CC       {ECO:0000250|UniProtKB:Q02224, ECO:0000269|PubMed:12925705}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC       {ECO:0000269|PubMed:12361599, ECO:0000269|PubMed:12925705}. Chromosome,
CC       centromere, kinetochore {ECO:0000269|PubMed:12361599,
CC       ECO:0000269|PubMed:12925705}. Chromosome, centromere
CC       {ECO:0000250|UniProtKB:Q02224}. Note=Associates with kinetochores
CC       during congression (as early as prometaphase), relocates to the spindle
CC       midzone at anaphase, and is quantitatively discarded at the end of the
CC       cell division (PubMed:12361599, PubMed:12925705). Recruited to the
CC       kinetochore in a SEPT7, CENPQ and TRAPPC12-dependent manner. Recruited
CC       to the pericentromeric/centromeric regions of the chromosome in a CTCF-
CC       dependent manner (By similarity). {ECO:0000250|UniProtKB:Q02224,
CC       ECO:0000269|PubMed:12361599, ECO:0000269|PubMed:12925705}.
CC   -!- TISSUE SPECIFICITY: Expressed in hippocampus. Also detected in liver
CC       and fibroblasts (at protein level). {ECO:0000269|PubMed:12361599,
CC       ECO:0000269|PubMed:9275178}.
CC   -!- DOMAIN: The protein is composed of a N-terminal kinesin-motor domain
CC       involved in the chromosome movements, a long coil-coiled region
CC       involved in the homodimerization and an inhibitory C-tail involved in
CC       autoinhibition of the N-terminal catalytic part. {ECO:0000250}.
CC   -!- PTM: The C-terminal inhibitory domain is phosphorylated.
CC       Phosphorylation relieves autoinhibition of the kinetochore motor (By
CC       similarity). {ECO:0000250}.
CC   -!- PTM: Sumoylated with SUMO2 and SUMO3. The sumoylation mediates the
CC       association to the kinetochore. {ECO:0000250|UniProtKB:Q02224}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH52843.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=AAI06097.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC       Sequence=BAC33868.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY493378; AAR85498.1; -; mRNA.
DR   EMBL; BC049989; AAH49989.1; -; mRNA.
DR   EMBL; BC052843; AAH52843.1; ALT_SEQ; mRNA.
DR   EMBL; BC059032; AAH59032.1; -; mRNA.
DR   EMBL; BC106096; AAI06097.1; ALT_SEQ; mRNA.
DR   EMBL; AK049676; BAC33868.1; ALT_FRAME; mRNA.
DR   EMBL; AK133445; BAE21661.1; -; mRNA.
DR   EMBL; AB001426; BAA22386.1; -; mRNA.
DR   RefSeq; NP_776123.3; NM_173762.4.
DR   AlphaFoldDB; Q6RT24; -.
DR   SMR; Q6RT24; -.
DR   BioGRID; 230907; 124.
DR   IntAct; Q6RT24; 4.
DR   STRING; 10090.ENSMUSP00000057938; -.
DR   GlyGen; Q6RT24; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6RT24; -.
DR   PhosphoSitePlus; Q6RT24; -.
DR   EPD; Q6RT24; -.
DR   jPOST; Q6RT24; -.
DR   MaxQB; Q6RT24; -.
DR   PaxDb; 10090-ENSMUSP00000057938; -.
DR   ProteomicsDB; 281536; -.
DR   Pumba; Q6RT24; -.
DR   DNASU; 229841; -.
DR   GeneID; 229841; -.
DR   KEGG; mmu:229841; -.
DR   AGR; MGI:1098230; -.
DR   CTD; 1062; -.
DR   MGI; MGI:1098230; Cenpe.
DR   eggNOG; KOG0242; Eukaryota.
DR   InParanoid; Q6RT24; -.
DR   OrthoDB; 1118452at2759; -.
DR   PhylomeDB; Q6RT24; -.
DR   Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR   Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR   Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-MMU-68877; Mitotic Prometaphase.
DR   Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR   Reactome; R-MMU-983189; Kinesins.
DR   BioGRID-ORCS; 229841; 20 hits in 80 CRISPR screens.
DR   ChiTaRS; Cenpe; mouse.
DR   PRO; PR:Q6RT24; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q6RT24; Protein.
DR   GO; GO:0005694; C:chromosome; ISO:MGI.
DR   GO; GO:0000775; C:chromosome, centromeric region; ISO:MGI.
DR   GO; GO:0000779; C:condensed chromosome, centromeric region; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR   GO; GO:0005828; C:kinetochore microtubule; ISO:MGI.
DR   GO; GO:0005874; C:microtubule; ISO:MGI.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR   GO; GO:0030496; C:midbody; ISO:MGI.
DR   GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR   GO; GO:1990023; C:mitotic spindle midzone; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0000940; C:outer kinetochore; IDA:MGI.
DR   GO; GO:0051233; C:spindle midzone; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043515; F:kinetochore binding; IDA:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR   GO; GO:0003777; F:microtubule motor activity; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR   GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; ISO:MGI.
DR   GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
DR   GO; GO:0051382; P:kinetochore assembly; ISO:MGI.
DR   GO; GO:0099607; P:lateral attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR   GO; GO:0051310; P:metaphase chromosome alignment; ISS:UniProtKB.
DR   GO; GO:0099606; P:microtubule plus-end directed mitotic chromosome migration; ISO:MGI.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0000278; P:mitotic cell cycle; ISO:MGI.
DR   GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; ISO:MGI.
DR   GO; GO:0007080; P:mitotic metaphase chromosome alignment; ISS:UniProtKB.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:UniProtKB.
DR   GO; GO:0007052; P:mitotic spindle organization; ISO:MGI.
DR   GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
DR   GO; GO:0051984; P:positive regulation of chromosome segregation; IMP:UniProtKB.
DR   GO; GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:UniProtKB.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0050793; P:regulation of developmental process; IMP:UniProtKB.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; ISO:MGI.
DR   GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:UniProtKB.
DR   GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
DR   GO; GO:0007057; P:spindle assembly involved in female meiosis I; IMP:MGI.
DR   CDD; cd01374; KISc_CENP_E; 1.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR   InterPro; IPR027640; Kinesin-like_fam.
DR   InterPro; IPR019821; Kinesin_motor_CS.
DR   InterPro; IPR001752; Kinesin_motor_dom.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR   PANTHER; PTHR47968:SF36; CENTROMERE-ASSOCIATED PROTEIN E; 1.
DR   Pfam; PF00225; Kinesin; 1.
DR   PRINTS; PR00380; KINESINHEAVY.
DR   SMART; SM00129; KISc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR   PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Centromere; Chromosome;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Developmental protein; Kinetochore;
KW   Lipoprotein; Methylation; Mitosis; Motor protein; Nucleotide-binding;
KW   Phosphoprotein; Prenylation; Reference proteome; Ubl conjugation.
FT   CHAIN           1..2471
FT                   /note="Centromere-associated protein E"
FT                   /id="PRO_0000365106"
FT   PROPEP          2472..2474
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000396743"
FT   DOMAIN          6..329
FT                   /note="Kinesin motor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   REGION          1962..2252
FT                   /note="Kinetochore binding domain"
FT                   /evidence="ECO:0000250|UniProtKB:Q02224"
FT   REGION          2196..2217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2286..2471
FT                   /note="Globular autoinhibitory domain"
FT                   /evidence="ECO:0000250"
FT   REGION          2371..2441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          334..2366
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        2393..2411
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         86..93
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT   MOD_RES         614
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02224"
FT   MOD_RES         2414
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02224"
FT   MOD_RES         2426
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02224"
FT   MOD_RES         2471
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           2471
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:Q02224"
FT   CONFLICT        231..241
FT                   /note="LNLVDLAGSER -> IKLIDTVDLEG (in Ref. 4; BAA22386)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1760
FT                   /note="T -> A (in Ref. 3; BAC33868)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   2474 AA;  286525 MW;  BAF52DD6068A2903 CRC64;
     MAEEASVAVC VRVRPLNSRE EELGEATHIY WKTDKNAIYQ SDGGKSFQFD RVFDSNETTK
     NVYEEIAVPI ISSAIQGYNG TIFAYGQTAS GKTHTMMGSE DCLGVIPRAI HDIFQRIKKF
     PEREFLLRVS YMEIYNETIT DLLCNAQKMK PLIIREDTNR TVYVSDLTEE VVYTAEMALK
     WLATGEKNRH YGITKMNQRS SRSHTIFRMI LESREKAEPS NCDGSVKVSH LNLVDLAGSE
     RAAQTGAEGV RLKEGCFINR NLFILGQVIK KLSDGQVGGF INYRDSKLTR ILQNSLGGNA
     KTRIICTITP ASLDETLTTL QFASTAKYMK NTPYVNEVSN DEALLKRYRR EIADLRKQLE
     EVNTKTRAQE MEKDQLAQLL DEKDLLQKVQ DEKINNLKRM LVTSSSIALQ QELEIKRKRR
     VTWCYGKMKD SNYEKEFKVP TSITTRKRKT SVTSLRENSL MKFGESAASS EFEMLNNTLE
     SLAEVEWSSA TTLLSEENVE SELNSLNAQY NDLVLDYEQL RRENEDLKLK LKEKNELEEF
     ELLEQKEERD QEMQLMHEVS NLKNLIKHAE EYNQDLENDL SSKVKLLKEK EEQIKNLQEY
     IDAQKSEKMK IDLSYTSDAT EDLKQAMRTL SDLDTVALDA KKESAFLRSE NLELKEKINE
     LSDSRKQMES DIQMYQRQLE AKKKMQTDLD KELQLAFQEI SKLSALVDGK GLLSNLELEK
     RITDLQKELN KEAEEKQTLQ EEVNLLSELK SLPSEVETLR RELYEKSEEL HIITTEREKL
     FSEMAHKDSR IQGLLEEIGN TRDDLATSQL SRRGSDGEWQ ALESLHAELE HRHAGVLEER
     ERLKQEIGAL SKEAESLAFS LDSVKAELSH KTQELEQKTV EGQERLNKME ALREELESRD
     SSLQSVEKEK VLLTEKLQQA LKEVKALTQE KKNLKQLQES LQTERDQLRS DIQDTVNMNI
     DTQEQLLNAL ESLKQHQETI NMLKMKAAEE LSDNLHVKDR GGARDEAQQK MDGIDEQNES
     AHTLLGGGKD NEVTEEQRKI DSLMQENSGL QQTLESVRAE KEQLKMDLKE NIEMSIENQE
     ELRILRDELK RQQEVAAQEK DHATEKTQEL SRTQERLAKT EEKLEEKNQK LQETQQQLLS
     TQEAMSKLQA KVIDMESLQN EFRNQGLALE RVETEKLELA QRLHESYEEV KSITKERNDL
     KELQESFEIE KKQLKEYARE IEAEGLQAKE ELNIAHANLK EYQEIITELR GSISENEAQG
     ASTQDTAKSA PELQGEVPEL LEQELLPVVK EARHSAEKVN GLEPVGAHSR TVHSMTMEGI
     EIGNLRLTKK LEESQMEISC LTREREDLRR TQETLQVECT QLKEDARRTL ANHLETEEEL
     NLARCCLKEQ ENKIDTLITS LSQRETELSS VRGQLALTTA ELERKVQELC EKQEELTRKE
     TSEAQGKMSE LEQLRELLLA QASALQNAES DRLRLNTQLE ESQEEMKTLR EEREELRRMQ
     EALHVESEQQ KESMKEISSK LQELQNKEYE CLAMKTINET QGSRCEMDHL NQQLEAQKST
     LEKVEMENVN LTQRLHETLE EMRSVAKERD ELWSMEERLT VERDQLKKSL EETVTKGMEK
     EEELRVAHVH LEEHQETINK LRKMVSDYTD EISHTQGDLK HTNAVVEAQN QDLREKEHQL
     SQVKADLRET VDQMEQLKKK LEAQSSTLES REIEKLELTQ QLNENLKKIT LVTKENDSLK
     IMDEALREER DQLRKSLQQT EARDLENQEK LRIAHMNLKE HQETIDRLME TMSEKTEEIS
     NMKMELENVN MKLQEKVQEL KTSERQRVKL KADASEAKKE LKEQGLTLSK IEMENLNLAQ
     KIHENLEEMK SVRKERDDLK KLEEILRMER DQLKDNLREA MLKAHQNHEE TMKCGKGLLC
     AGEYCTGRLR EKCFRIEKLL KRYSEMANDY ECLNKVSLDL ERETKTQKEL SVTVRTKLSL
     PHTQTKEMEK LLTANQRCSL EFHRALKRLK YVLSSIARIK EEQHESINKR EMAFIQEVEK
     QNELQIQIQS LSQTYRIPAR DLQIKLSQEM DLHIEEMLKD FSENDFLTIK TEVQQVLNNR
     KEITEFLGKW LNTLFDTENL KSTIQKENKS IGLVNNFYHS RITAMINEST EFEERSATRS
     KDLDQYLKSL KETTEQLSEV YQTLTASQSV VHLHPTVQPS TRDSERPQAA SGAEQLTSKN
     KIALGAVPYK EEIEDLKMQL VKSDLEKKAT AKEFDKKILS LKATVEHQEE MIRLLRENLR
     GHQQAQDTSM ISEQDSQLLS KPLTCGGGSG IVQSTKALIL KSEYKRMGSE ISKLKQQNEQ
     LRKQNNQLLS DNSQLSNEVK TWEERTLKRD SYRETTCENS PKSPKVTRTD SKRRQNTTSQ
     CRAQNLQDPV PKDSPKSWFF DNRSKSLPAP HPIRYFDNSS LGLCPEPDDV ENVEPKTDLC
     QASLEKDVSQ CKTQ
//