ID MCAF1_MOUSE Reviewed; 1306 AA.
AC Q7TT18; Q3TJ86; Q3TZW1; Q3UVK5; Q3UYZ7; Q80ZK7; Q8C4A1; Q9JK31;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 157.
DE RecName: Full=Activating transcription factor 7-interacting protein 1;
DE AltName: Full=ATFa-associated modulator;
DE Short=mAM;
DE AltName: Full=MBD1-containing chromatin-associated factor 1;
GN Name=Atf7ip; Synonyms=Mcaf1;
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), FUNCTION, NUCLEAR LOCALIZATION
RP SIGNAL, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10777215; DOI=10.1038/sj.onc.1203492;
RA De Graeve F., Bahr A., Chatton B., Kedinger C.;
RT "A murine ATFa-associated factor with transcriptional repressing
RT activity.";
RL Oncogene 19:1807-1819(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Cerebellum, Forelimb, Spleen, and Urinary bladder;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Liver, and 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 [4]
RP FUNCTION, AND INTERACTION WITH SETDB1.
RX PubMed=14536086; DOI=10.1016/j.molcel.2003.08.007;
RA Wang H., An W., Cao R., Xia L., Erdjument-Bromage H., Chatton B.,
RA Tempst P., Roeder R.G., Zhang Y.;
RT "mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of
RT histone H3 to cause transcriptional repression.";
RL Mol. Cell 12:475-487(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-112; SER-514; SER-516;
RP SER-593 AND SER-700, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Recruiter that couples transcriptional factors to general
CC transcription apparatus and thereby modulates transcription regulation
CC and chromatin formation. Can both act as an activator or a repressor
CC depending on the context (PubMed:10777215). Required for HUSH-mediated
CC heterochromatin formation and gene silencing (By similarity). Mediates
CC MBD1-dependent transcriptional repression, probably by recruiting
CC complexes containing SETDB1. Stabilizes SETDB1, is required to
CC stimulate histone methyltransferase activity of SETDB1 and facilitates
CC the conversion of dimethylated to trimethylated H3 'Lys-9' (H3K9me3).
CC The complex formed with MBD1 and SETDB1 represses transcription and
CC couples DNA methylation and histone H3 'Lys-9' trimethylation (H3K9me3)
CC (PubMed:14536086). Facilitates telomerase TERT and TERC gene expression
CC by SP1 in cancer cells (By similarity). {ECO:0000250|UniProtKB:Q6VMQ6,
CC ECO:0000269|PubMed:10777215, ECO:0000269|PubMed:14536086}.
CC -!- SUBUNIT: Interacts with MBD1; the interaction is enhanced when MBD1 is
CC sumoylated (By similarity). Interacts with SETDB1; the interaction
CC protects SETDB1 from proteasomal degradation and is required to
CC stimulate histone methyltransferase activity and facilitate the
CC conversion of dimethylated to trimethylated H3 'Lys-9'
CC (PubMed:14536086). Interacts with SUMO ubiquitin-like proteins (SUMO1,
CC SUNO2 and SUMO3), with a preference for SUMO2 and SUMO3. Interacts with
CC SP1, ATF7 and ZHX1. Interacts with the general transcription machinery,
CC including ERCC2, ERCC3, GTF2E1, GTF2E2 and POLR2A (By similarity).
CC {ECO:0000250|UniProtKB:Q6VMQ6, ECO:0000269|PubMed:14536086}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10777215}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TT18-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TT18-2; Sequence=VSP_024040, VSP_024041;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at all stages studied.
CC {ECO:0000269|PubMed:10777215}.
CC -!- SIMILARITY: Belongs to the MCAF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE39609.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ132702; CAB77024.1; -; mRNA.
DR EMBL; BC022714; AAH22714.1; ALT_TERM; mRNA.
DR EMBL; AK082697; BAC38574.1; -; mRNA.
DR EMBL; AK134252; BAE22064.1; -; mRNA.
DR EMBL; AK137199; BAE23264.1; -; mRNA.
DR EMBL; AK157479; BAE34096.1; -; mRNA.
DR EMBL; AK167542; BAE39609.1; ALT_FRAME; mRNA.
DR EMBL; BC048827; AAH48827.1; ALT_TERM; mRNA.
DR EMBL; BC052460; AAH52460.1; -; mRNA.
DR EMBL; BC060246; AAH60246.1; -; mRNA.
DR CCDS; CCDS20651.1; -. [Q7TT18-1]
DR RefSeq; NP_062299.2; NM_019426.2. [Q7TT18-1]
DR RefSeq; XP_006506452.2; XM_006506389.3. [Q7TT18-1]
DR RefSeq; XP_017177170.1; XM_017321681.1. [Q7TT18-1]
DR AlphaFoldDB; Q7TT18; -.
DR BioGRID; 207616; 14.
DR IntAct; Q7TT18; 3.
DR STRING; 10090.ENSMUSP00000032335; -.
DR GlyGen; Q7TT18; 16 sites, 1 O-linked glycan (16 sites).
DR iPTMnet; Q7TT18; -.
DR PhosphoSitePlus; Q7TT18; -.
DR EPD; Q7TT18; -.
DR jPOST; Q7TT18; -.
DR MaxQB; Q7TT18; -.
DR PaxDb; 10090-ENSMUSP00000032335; -.
DR PeptideAtlas; Q7TT18; -.
DR ProteomicsDB; 295837; -. [Q7TT18-1]
DR ProteomicsDB; 295838; -. [Q7TT18-2]
DR Pumba; Q7TT18; -.
DR Antibodypedia; 12020; 112 antibodies from 20 providers.
DR DNASU; 54343; -.
DR Ensembl; ENSMUST00000032335.13; ENSMUSP00000032335.7; ENSMUSG00000030213.13. [Q7TT18-1]
DR GeneID; 54343; -.
DR KEGG; mmu:54343; -.
DR UCSC; uc009elv.1; mouse. [Q7TT18-1]
DR UCSC; uc009elx.1; mouse. [Q7TT18-2]
DR AGR; MGI:1858965; -.
DR CTD; 55729; -.
DR MGI; MGI:1858965; Atf7ip.
DR VEuPathDB; HostDB:ENSMUSG00000030213; -.
DR eggNOG; ENOG502QSM2; Eukaryota.
DR GeneTree; ENSGT00530000063707; -.
DR HOGENOM; CLU_009529_0_0_1; -.
DR InParanoid; Q7TT18; -.
DR OMA; QETIHEP; -.
DR OrthoDB; 4053704at2759; -.
DR PhylomeDB; Q7TT18; -.
DR TreeFam; TF329427; -.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR BioGRID-ORCS; 54343; 16 hits in 86 CRISPR screens.
DR ChiTaRS; Atf7ip; mouse.
DR PRO; PR:Q7TT18; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q7TT18; Protein.
DR Bgee; ENSMUSG00000030213; Expressed in animal zygote and 263 other cell types or tissues.
DR ExpressionAtlas; Q7TT18; baseline and differential.
DR Genevisible; Q7TT18; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:0006306; P:DNA methylation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin formation; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0045898; P:regulation of RNA polymerase II transcription preinitiation complex assembly; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR026085; ATF7-int.
DR InterPro; IPR031870; ATF7IP_BD.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR PANTHER; PTHR23210; ACTIVATING TRANSCRIPTION FACTOR 7 INTERACTING PROTEIN; 1.
DR PANTHER; PTHR23210:SF22; ACTIVATING TRANSCRIPTION FACTOR 7-INTERACTING PROTEIN 1; 1.
DR Pfam; PF16788; ATF7IP_BD; 1.
DR Pfam; PF16794; fn3_4; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS50853; FN3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Coiled coil; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1306
FT /note="Activating transcription factor 7-interacting
FT protein 1"
FT /id="PRO_0000281781"
FT DOMAIN 1054..1143
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1196..1302
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..851
FT /note="Interaction with SETDB1"
FT /evidence="ECO:0000250"
FT REGION 689..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..1060
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1001..1011
FT /note="Interaction with SUMO"
FT /evidence="ECO:0000250"
FT REGION 1152..1196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1306
FT /note="Interaction with MBD1"
FT /evidence="ECO:0000250"
FT COILED 666..696
FT /evidence="ECO:0000255"
FT MOTIF 587..605
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:10777215"
FT COMPBIAS 104..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..466
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 920..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1017..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1053
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1186
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q6VMQ6"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 124
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6VMQ6"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VMQ6"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VMQ6"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VMQ6"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VMQ6"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6VMQ6"
FT CROSSLNK 592
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6VMQ6"
FT CROSSLNK 944
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6VMQ6"
FT CROSSLNK 974
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6VMQ6"
FT VAR_SEQ 1..959
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024040"
FT VAR_SEQ 960..989
FT /note="SSATPRIVTENQTNKTVDSSINKKAADSTS -> MRPFSPLPLLLPHISLVA
FT SAPLQNQTSFIF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_024041"
FT CONFLICT 121
FT /note="S -> Y (in Ref. 2; BAE22064)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="G -> A (in Ref. 1; CAB77024 and 3; AAH22714/
FT AAH48827)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="S -> G (in Ref. 1; CAB77024 and 3; AAH22714/
FT AAH48827)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="D -> E (in Ref. 3; AAH22714/AAH48827)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="S -> L (in Ref. 1; CAB77024 and 3; AAH22714/
FT AAH48827)"
FT /evidence="ECO:0000305"
FT CONFLICT 545
FT /note="S -> P (in Ref. 2; BAE39609)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="A -> V (in Ref. 3; AAH22714/AAH48827)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="S -> T (in Ref. 1; CAB77024 and 3; AAH22714/
FT AAH48827)"
FT /evidence="ECO:0000305"
FT CONFLICT 564..565
FT /note="DG -> GS (in Ref. 1; CAB77024)"
FT /evidence="ECO:0000305"
FT CONFLICT 600..602
FT /note="ESK -> QST (in Ref. 1; CAB77024)"
FT /evidence="ECO:0000305"
FT CONFLICT 622
FT /note="K -> G (in Ref. 1; CAB77024)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="K -> E (in Ref. 1; CAB77024)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="Q -> R (in Ref. 1; CAB77024)"
FT /evidence="ECO:0000305"
FT CONFLICT 964
FT /note="P -> T (in Ref. 2; BAE39609)"
FT /evidence="ECO:0000305"
FT CONFLICT 968
FT /note="T -> A (in Ref. 1; CAB77024)"
FT /evidence="ECO:0000305"
FT CONFLICT 1201
FT /note="H -> Q (in Ref. 2; BAE39609)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1306 AA; 138593 MW; D09FE3ACC93FA207 CRC64;
MDSVEEPQKK VFKARKTMRA SDRQQLDAVH RVKGELLRAD GKLLNGSHEN GDLDPTSPLE
NTDCIQDREE VNGIDGICFQ SEESTTEWKE TPCMPNVAVK NKQEDLNSEA LSPSITCDLS
SRVTTEPGSG SPASDNPGCG TPVSDNPASD NPASDNPASD NPDSGDLAAG ELATTVQATG
DSACEEPPSS DPSSSDPTSS EPSSSEPTCS EPISGDPVSE EAASHDLVSG DSTCSEPVSG
EPVSHEAASS EPATSEPASD EPVARVVAAC ELAPGESALD DCAPSGDSQS DEPPSSEDSL
PRSVCSGLAS GELTPGELSV EPATDTVKPS SSAVCEAGPD PDKTEPSSNN SDDCPGKSED
DEHLDQIQSK DSCDEGNKVN SNVVEKEEPL ETHSAIICSD LPPENTTKIA EDPIAEPALE
EEAISSSMEV DQSEKDEHKS PAEPVAAVSE DPAEEDKEDT VVDNTDSMET DEIIPILEKL
APTEDELSCF SKASLLPVET SQDLEDKMEG SFGSPSKQES SENLPKEAFL VLSDEEDLSC
GKDESEAVAQ SKMSTPEGEK SEKDGKAEEE ERVPAEEQPP VRNEFSRRKR SKSEDMDSVE
SKRRRYMDEE YEAEFQVKIT AKGDINQKLQ KVIQWLLQEK LCALQCAVFD KTLAELKTRV
EKIECNKRHK AVLTELQAKI ARLTKRFGAA KDDLKKRQES PPNPPISPGK PANDTNSNNN
MTYRNAGTVR QLLESKRNVS EGPPPSFQTP VNTVSSASHA TSTAVVSSQP KLQTSATSGS
LPAAPLLPAP STATVVATTQ VPSGTPQPTI SLQPLPVILH VPVAVTSQPQ LLQSHPGTLV
TNQPSGNVEF ISVQSQPTVS GLTKNPVSLP PLPNPTKPNI PSVPSPSSIQ RNSSTTAAPL
GTTLAVQAVP TAHSIVQATR TSLPTVGPSG LYSSSSSRGP IQMKIPISTF SPPSSAEQNS
SATPRIVTEN QTNKTVDSSI NKKAADSTSQ SGKASSSDSS GVIDLTMDDE ESGTTQDPKK
ISPPSSSTVS TSQPMSRPLQ PILPAPPLQP SGVPTSGPSQ ATIHVLPTAP TTVNVTHRPV
TQVTTRLPVP RAPANHQVVY TTLPAPTTQA PLRGTVMQAP AVRQVNPQNS VTVRVPQTTT
YVVNNGLTLG SAGPQLTVHH RPPQVHNEPP RPLHPAPLPE APQPQRLPPE AASTSLPQKP
HLKLARVQSQ NGIVLSWSVL EVDRSCATVD SYHLYAYHEE PSATVPSQWK KIGEVKALPL
PMACTLTQFV SGSKYYFAVR AKDIYGRFGP FCDPQSTDVI SSSQNS
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