ID CCNF_MOUSE Reviewed; 777 AA.
AC P51944; Q3TF73; Q60797; Q60799; Q8BSX9; Q8C4D9; Q8CI26;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 24-JAN-2024, entry version 167.
DE RecName: Full=Cyclin-F;
GN Name=Ccnf;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7767003; DOI=10.1007/bf00303265;
RA Obermayr F.O., Sutherland H.F., Kraus B., Frischauf A.-M.;
RT "Mouse cyclin F maps to a conserved linkage group on mouse chromosome 17.";
RL Mamm. Genome 6:149-150(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Croci L., Stayton C.L., Bossolasco M., Bianchi E., Corradi A.M., Pardi R.,
RA Consalez G.G.;
RT "Expression of cyclin F at early stages of mouse embryonic brain
RT development.";
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Kidney, Ovary, and Uterus;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [6]
RP INDUCTION.
RX PubMed=11572993; DOI=10.1073/pnas.201360898;
RA Wang X., Quail E., Hung N.J., Tan Y., Ye H., Costa R.H.;
RT "Increased levels of forkhead box M1B transcription factor in transgenic
RT mouse hepatocytes prevent age-related proliferation defects in regenerating
RT liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11468-11473(2001).
RN [7]
RP INDUCTION.
RX PubMed=12867420; DOI=10.1074/jbc.m305555200;
RA Kalinichenko V.V., Gusarova G.A., Tan Y., Wang I.C., Major M.L., Wang X.,
RA Yoder H.M., Costa R.H.;
RT "Ubiquitous expression of the forkhead box M1B transgene accelerates
RT proliferation of distinct pulmonary cell types following lung injury.";
RL J. Biol. Chem. 278:37888-37894(2003).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=14993286; DOI=10.1128/mcb.24.6.2487-2498.2004;
RA Tetzlaff M.T., Bai C., Finegold M., Wilson J., Harper J.W., Mahon K.A.,
RA Elledge S.J.;
RT "Cyclin F disruption compromises placental development and affects normal
RT cell cycle execution.";
RL Mol. Cell. Biol. 24:2487-2498(2004).
CC -!- FUNCTION: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins (By similarity). The SCF(CCNF) E3 ubiquitin-protein ligase
CC complex is an integral component of the ubiquitin proteasome system
CC (UPS) and links proteasome degradation to the cell cycle (By
CC similarity). Mediates the substrate recognition and the proteasomal
CC degradation of various target proteins involved in the regulation of
CC cell cycle progression and in the maintenance of genome stability (By
CC similarity). Mediates the ubiquitination and subsequent proteasomal
CC degradation of CP110 during G2 phase, thereby acting as an inhibitor of
CC centrosome reduplication (By similarity). In G2, mediates the
CC ubiquitination and proteasomal degradation of CDC6, thereby suppressing
CC DNA re-replication and preventing genome instability (By similarity).
CC Involved in the ubiquitination and degradation of the substrate adapter
CC CDH1 of the anaphase-promoting complex (APC/C), thereby acting as an
CC antagonist of APC/C in regulating G1 progression and S phase entry (By
CC similarity). May play a role in the G2 cell cycle checkpoint control
CC after DNA damage, possibly by promoting the ubiquitination of
CC MYBL2/BMYB (By similarity). {ECO:0000250|UniProtKB:P41002}.
CC -!- SUBUNIT: Component of the SCF(CCNF) complex consisting of CUL1, RBX1,
CC SKP1 and CCNF (By similarity). Interacts with SKP1 (By similarity).
CC Interacts with CUL1 (By similarity). Interacts with CCNB1; interaction
CC is required for nuclear localization of CCNB1 (By similarity).
CC Interacts with CCP110; this interaction leads to CCP110 ubiquitination
CC and degradation via the proteasome pathway (By similarity). Interacts
CC (via the Cyclin N-terminal domain) with MYBL2/BMYB (By similarity).
CC Interacts with FZR1/CDH1 (via N-terminus) (By similarity). Interacts
CC with RRM2 (via Cy motif and when phosphorylated at 'Thr-33'); the
CC interaction occurs exclusively in G2 and early M (By similarity).
CC Interacts with CDC6 (via Cy motif); the interaction takes place during
CC G2 and M phase (By similarity). {ECO:0000250|UniProtKB:P41002}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P41002}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41002}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome,
CC centriole {ECO:0000250|UniProtKB:P41002}. Note=Localization in the
CC centrosome is rare in S phase cells and increases in G2 cells,
CC Localizes on both the mother and daughter centrioles. Localization to
CC centrosomes is not dependent on CP110. Localizes to the nucleus in G2
CC phase. {ECO:0000250|UniProtKB:P41002}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Short;
CC IsoId=P51944-1; Sequence=Displayed;
CC Name=2; Synonyms=Long;
CC IsoId=P51944-2; Sequence=VSP_001257;
CC Name=3;
CC IsoId=P51944-3; Sequence=VSP_039778;
CC -!- INDUCTION: Expression is activated by the FOXM1 transcription factor.
CC {ECO:0000269|PubMed:11572993, ECO:0000269|PubMed:12867420}.
CC -!- DOMAIN: The nuclear localization signals mediate the localization to
CC the nucleus and are required for CCNB1 localization to the nucleus.
CC {ECO:0000250|UniProtKB:P41002}.
CC -!- DOMAIN: The D box motifs 1-4 (amino acid sequence RxxL) are involved in
CC substrate binding, such as FZR1/CDH1, and may be ubiquitinated.
CC {ECO:0000250|UniProtKB:P41002}.
CC -!- PTM: Degraded when the spindle assembly checkpoint is activated during
CC the G2-M transition. Degradation is not dependent on the proteasome or
CC ubiquitin and depends on the C-terminal PEST sequence.
CC {ECO:0000250|UniProtKB:P41002}.
CC -!- PTM: Phosphorylated just before cells enter into mitosis.
CC {ECO:0000250|UniProtKB:P41002}.
CC -!- PTM: Ubiquitinated by the anaphase-promoting complex (APC/C); leading
CC to its degradation by the proteasome. {ECO:0000250|UniProtKB:P41002}.
CC -!- DISRUPTION PHENOTYPE: Death by 10.5 dpc, with many developmental
CC anomalies due in part to failures in yolk sac and chorioallantoic
CC placentation. Heterozygous mice are normal and fertile.
CC {ECO:0000269|PubMed:14993286}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin AB subfamily.
CC {ECO:0000305}.
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DR EMBL; Z47766; CAA87695.1; -; mRNA.
DR EMBL; U20612; AAA62317.1; -; mRNA.
DR EMBL; U20636; AAA63152.1; -; mRNA.
DR EMBL; AK030298; BAC26886.1; -; mRNA.
DR EMBL; AK082485; BAC38507.1; -; mRNA.
DR EMBL; AK159594; BAE35214.1; -; mRNA.
DR EMBL; AK169263; BAE41025.1; -; mRNA.
DR EMBL; AC117577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037662; AAH37662.1; -; mRNA.
DR CCDS; CCDS37484.1; -. [P51944-1]
DR PIR; I48317; I48317.
DR RefSeq; NP_031660.3; NM_007634.4. [P51944-1]
DR AlphaFoldDB; P51944; -.
DR SMR; P51944; -.
DR BioGRID; 198554; 5.
DR STRING; 10090.ENSMUSP00000111048; -.
DR iPTMnet; P51944; -.
DR PhosphoSitePlus; P51944; -.
DR EPD; P51944; -.
DR PaxDb; 10090-ENSMUSP00000111048; -.
DR ProteomicsDB; 280013; -. [P51944-1]
DR ProteomicsDB; 280014; -. [P51944-2]
DR ProteomicsDB; 280015; -. [P51944-3]
DR Antibodypedia; 10421; 255 antibodies from 33 providers.
DR DNASU; 12449; -.
DR Ensembl; ENSMUST00000115390.5; ENSMUSP00000111048.4; ENSMUSG00000072082.8. [P51944-1]
DR GeneID; 12449; -.
DR KEGG; mmu:12449; -.
DR UCSC; uc008ave.1; mouse. [P51944-1]
DR UCSC; uc008avg.1; mouse. [P51944-3]
DR AGR; MGI:102551; -.
DR CTD; 899; -.
DR MGI; MGI:102551; Ccnf.
DR VEuPathDB; HostDB:ENSMUSG00000072082; -.
DR eggNOG; KOG0654; Eukaryota.
DR GeneTree; ENSGT00810000125541; -.
DR HOGENOM; CLU_020348_0_0_1; -.
DR InParanoid; P51944; -.
DR OMA; HQAKKSC; -.
DR OrthoDB; 3020936at2759; -.
DR PhylomeDB; P51944; -.
DR TreeFam; TF101006; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 12449; 28 hits in 78 CRISPR screens.
DR ChiTaRS; Ccnf; mouse.
DR PRO; PR:P51944; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P51944; Protein.
DR Bgee; ENSMUSG00000072082; Expressed in ectoplacental cone and 157 other cell types or tissues.
DR ExpressionAtlas; P51944; baseline and differential.
DR Genevisible; P51944; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005814; C:centriole; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0010997; F:anaphase-promoting complex binding; ISO:MGI.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IBA:GO_Central.
DR GO; GO:0010826; P:negative regulation of centrosome duplication; IMP:MGI.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0000320; P:re-entry into mitotic cell cycle; IMP:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR CDD; cd20521; CYCLIN_CCNF_rpt1; 1.
DR CDD; cd22082; F-box_FBXO1; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 2.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR039361; Cyclin.
DR InterPro; IPR013763; Cyclin-like_dom.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR004367; Cyclin_C-dom.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR048258; Cyclins_cyclin-box.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR10177:SF496; CYCLIN-F; 1.
DR PANTHER; PTHR10177; CYCLINS; 1.
DR Pfam; PF02984; Cyclin_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR Pfam; PF12937; F-box-like; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SMART; SM01332; Cyclin_C; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
DR SUPFAM; SSF81383; F-box domain; 1.
DR PROSITE; PS00292; CYCLINS; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell cycle; Cell division; Cyclin; Cytoplasm;
KW Cytoskeleton; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..777
FT /note="Cyclin-F"
FT /id="PRO_0000080464"
FT DOMAIN 29..76
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT DOMAIN 288..405
FT /note="Cyclin N-terminal"
FT /evidence="ECO:0000255"
FT REGION 544..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..761
FT /note="PEST"
FT REGION 651..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 20..28
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT MOTIF 310..313
FT /note="D box 1"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT MOTIF 343..346
FT /note="D box 2"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT MOTIF 349..352
FT /note="D box 3"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT MOTIF 568..574
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT MOTIF 762..765
FT /note="D box 4"
FT /evidence="ECO:0000250|UniProtKB:P41002"
FT COMPBIAS 544..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..732
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 5
FT /note="G -> GGECWRDGVGDRSYGTEAGGAWTRAPVTRECASHPPKHGV (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_001257"
FT VAR_SEQ 232..233
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039778"
FT CONFLICT 81
FT /note="L -> P (in Ref. 2; AAA62317/AAA63152)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="E -> Q (in Ref. 1; CAA87695)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="S -> T (in Ref. 1; CAA87695)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="L -> H (in Ref. 3; BAC26886)"
FT /evidence="ECO:0000305"
FT CONFLICT 263
FT /note="A -> T (in Ref. 2; AAA62317/AAA63152)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="S -> T (in Ref. 2; AAA62317/AAA63152)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="V -> G (in Ref. 1; CAA87695)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="T -> S (in Ref. 2; AAA62317/AAA63152)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="S -> A (in Ref. 1; CAA87695)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="H -> R (in Ref. 2; AAA62317/AAA63152)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="V -> I (in Ref. 1; CAA87695, 2; AAA62317/AAA63152
FT and 5; AAH37662)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="R -> Q (in Ref. 1; CAA87695)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="T -> A (in Ref. 1; CAA87695, 2; AAA62317/AAA63152
FT and 5; AAH37662)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="G -> E (in Ref. 2; AAA62317/AAA63152)"
FT /evidence="ECO:0000305"
FT CONFLICT 568..569
FT /note="RR -> E (in Ref. 1; CAA87695)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="S -> G (in Ref. 2; AAA62317/AAA63152)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="E -> R (in Ref. 2; AAA62317/AAA63152)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="Q -> K (in Ref. 3; BAE41025)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="M -> T (in Ref. 1; CAA87695, 2; AAA62317/AAA63152
FT and 5; AAH37662)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 777 AA; 86623 MW; 1FDA471590793DD6 CRC64;
MGSGGVIHCR CAKCFCYPTK RRIKRRPRNL TILSLPEDVL FHILKWLSVG DILAVRAVHS
HLKYLVDNHA SVWASASFQE LWPSPQNLKL FERAAEKGNF EAAVKLGIAY LYNEGLSVSD
EACAEVNGLK ASRFFSMAER LNTGSEPFIW LFIRPPWSVS GSCCKAVVHD SLRAECQLQR
SHKASILHCL GRVLNLFEDE EKRKQARSLL EESSRQGCLI SSYLLWESDR KVDMSDPGRC
LHSFRKLRDY AAKGCWEAQL ALAKACAGGS QLGLEGKACS ESVCQLFQAS QAVNKQQIFS
VQKGLSDTMR YILIDWLVEV ATMKDFTSLC LHLTVECVDR YLRRRLVPRY KLQLLGIACM
VICTRFISKE ILTIREAVWL TDNTYKYEDL VRVMGEIISA LEGKIRIPTV VDYKEVLLTL
VPVAPRTQHL CSFLCELTLL HTSLSIYAPA RLASAALLLA RLMHGQTQPW TTHLWDLTGF
SYSDLVPCVL SLHKKCFHDD APKDYRQVSL TAVKQRFEDK CYEEISREEV LSYADLCSTI
GVKQESPEPP SFPSSGEIHT FLSSPSGRRS KRKRENSLQE DRGSFVTTPT AELSNQEETL
LGSLLDWSLE CCSGYEGDQE SEGEKEGDVT APSRLLDVTV VYLNPEEHCC QESSDEEAWP
EDKIHPAPGT QAPPASAPRP LLCNRGDRAK DITTSGYSSV SSSSPISSLD GGMGGSPQST
SVLSVGSHSS TKPCHHQAKK SCLQCRPPNS PESGVHQQPV KRQNLSVHSD KDMHLAS
//
