XIRP2_MOUSE
ID XIRP2_MOUSE Reviewed; 3784 AA.
AC Q4U4S6; A1ECA5; A2AVA2; Q5S4P6; Q5S4P7; Q5S4P8; Q8BS23;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Xin actin-binding repeat-containing protein 2;
DE AltName: Full=Beta-xin;
DE AltName: Full=Cardiomyopathy-associated protein 3;
DE AltName: Full=Myogenic MEF2-activated Xin-related protein;
DE AltName: Full=Myomaxin;
DE AltName: Full=mXinbeta;
GN Name=Xirp2; Synonyms=Cmya3, Xin2;
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 2), INDUCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH ACTN2.
RC TISSUE=Skeletal muscle;
RX PubMed=17046827; DOI=10.1074/jbc.m603244200;
RA Huang H.-T., Brand O.M., Mathew M., Ignatiou C., Ewen E.P., McCalmon S.A.,
RA Naya F.J.;
RT "Myomaxin is a novel transcriptional target of MEF2A that encodes a Xin-
RT related alpha-actinin-interacting protein.";
RL J. Biol. Chem. 281:39370-39379(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=A/J;
RA Tran P.V., Herron B.J., Scherz P.J., Qiu H., Turbe-Doan A., Parker K.,
RA Beier D.R.;
RT "Thm1 is a novel negative regulator of mouse Sonic hedgehog signaling.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Heart;
RA Xie L., Wang K.;
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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 [MRNA] OF 1-1427 (ISOFORM 1), TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=C57BL/6J;
RX PubMed=17766470; DOI=10.1152/ajpheart.00806.2007;
RA Gustafson-Wagner E.A., Sinn H.W., Chen Y.-L., Wang D.-Z., Reiter R.S.,
RA Lin J.L.-C., Yang B., Williamson R.A., Chen J., Lin C.-I., Lin J.J.-C.;
RT "Loss of mXinalpha, an intercalated disk protein, results in cardiac
RT hypertrophy and cardiomyopathy with conduction defects.";
RL Am. J. Physiol. 293:H2680-H2692(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-493.
RC STRAIN=C57BL/6J; TISSUE=Aorta;
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 [7]
RP INDUCTION.
RX PubMed=16500513; DOI=10.1016/j.amjhyper.2005.08.017;
RA Duka A., Schwartz F., Duka I., Johns C., Melista E., Gavras I., Gavras H.;
RT "A novel gene (Cmya3) induced in the heart by angiotensin II-dependent but
RT not salt-dependent hypertension in mice.";
RL Am. J. Hypertens. 19:275-281(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-815; SER-2139 AND
RP SER-2974, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Heart;
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: Protects actin filaments from depolymerization.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ACTN2. Interacts with F-actin (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q4U4S6; Q61762: Kcna5; NbExp=2; IntAct=EBI-10768169, EBI-26520959;
CC Q4U4S6; Q9JJV9: Scn5a; NbExp=2; IntAct=EBI-10768169, EBI-8313814;
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:17766470}.
CC Note=Colocalizes with actin stress fibers.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4U4S6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4U4S6-2; Sequence=VSP_030849, VSP_030850;
CC -!- TISSUE SPECIFICITY: Expression is restricted to heart and skeletal
CC muscle. Present in intercalated disks of the heart and in the Z-disk
CC region of skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:17046827, ECO:0000269|PubMed:17766470}.
CC -!- INDUCTION: By MEF2A in skeletal muscle. By angiotensin II in heart.
CC {ECO:0000269|PubMed:16500513, ECO:0000269|PubMed:17046827}.
CC -!- DOMAIN: Xin repeats bind F-actin.
CC -!- SIMILARITY: Belongs to the Xin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00721}.
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DR EMBL; EF122140; ABL63748.1; -; mRNA.
DR EMBL; DQ011666; AAY44537.1; -; mRNA.
DR EMBL; EF119716; ABO69252.1; -; mRNA.
DR EMBL; AL929411; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY775570; AAV52766.1; -; mRNA.
DR EMBL; AY775571; AAV52767.1; -; mRNA.
DR EMBL; AY775572; AAV52768.1; -; mRNA.
DR EMBL; AK040786; BAC30703.1; -; mRNA.
DR CCDS; CCDS16082.1; -. [Q4U4S6-1]
DR CCDS; CCDS38133.1; -. [Q4U4S6-2]
DR RefSeq; NP_001019789.1; NM_001024618.2. [Q4U4S6-1]
DR RefSeq; NP_001077388.1; NM_001083919.1. [Q4U4S6-2]
DR SMR; Q4U4S6; -.
DR BioGRID; 232312; 11.
DR IntAct; Q4U4S6; 4.
DR MINT; Q4U4S6; -.
DR STRING; 10090.ENSMUSP00000107966; -.
DR iPTMnet; Q4U4S6; -.
DR PhosphoSitePlus; Q4U4S6; -.
DR EPD; Q4U4S6; -.
DR jPOST; Q4U4S6; -.
DR MaxQB; Q4U4S6; -.
DR PaxDb; Q4U4S6; -.
DR PRIDE; Q4U4S6; -.
DR ProteomicsDB; 299706; -. [Q4U4S6-1]
DR ProteomicsDB; 299707; -. [Q4U4S6-2]
DR Antibodypedia; 33785; 55 antibodies from 15 providers.
DR Ensembl; ENSMUST00000028410; ENSMUSP00000028410; ENSMUSG00000027022. [Q4U4S6-1]
DR Ensembl; ENSMUST00000112347; ENSMUSP00000107966; ENSMUSG00000027022. [Q4U4S6-2]
DR GeneID; 241431; -.
DR KEGG; mmu:241431; -.
DR UCSC; uc008jxj.1; mouse. [Q4U4S6-2]
DR UCSC; uc008jxk.1; mouse. [Q4U4S6-1]
DR CTD; 129446; -.
DR MGI; MGI:2685198; Xirp2.
DR VEuPathDB; HostDB:ENSMUSG00000027022; -.
DR eggNOG; ENOG502SF50; Eukaryota.
DR GeneTree; ENSGT00530000063779; -.
DR HOGENOM; CLU_000319_0_0_1; -.
DR InParanoid; Q4U4S6; -.
DR OMA; HSQQSMK; -.
DR OrthoDB; 30028at2759; -.
DR PhylomeDB; Q4U4S6; -.
DR TreeFam; TF330745; -.
DR BioGRID-ORCS; 241431; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q4U4S6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q4U4S6; protein.
DR Bgee; ENSMUSG00000027022; Expressed in hindlimb stylopod muscle and 13 other tissues.
DR ExpressionAtlas; Q4U4S6; baseline and differential.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0030018; C:Z disc; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0051393; F:alpha-actinin binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IMP:MGI.
DR GO; GO:0045216; P:cell-cell junction organization; IMP:MGI.
DR GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR InterPro; IPR012510; Actin-binding_Xin_repeat.
DR InterPro; IPR030072; XIRP1/XIRP2.
DR InterPro; IPR030107; XIRP2.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR22591; PTHR22591; 1.
DR PANTHER; PTHR22591:SF1; PTHR22591:SF1; 1.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF08043; Xin; 21.
DR SMART; SM00132; LIM; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS51389; XIN; 28.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell junction; Coiled coil;
KW LIM domain; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Zinc.
FT CHAIN 1..3784
FT /note="Xin actin-binding repeat-containing protein 2"
FT /id="PRO_0000316988"
FT REPEAT 308..323
FT /note="Xin 1"
FT REPEAT 343..358
FT /note="Xin 2"
FT REPEAT 383..398
FT /note="Xin 3"
FT REPEAT 420..435
FT /note="Xin 4"
FT REPEAT 458..473
FT /note="Xin 5"
FT REPEAT 498..513
FT /note="Xin 6"
FT REPEAT 536..551
FT /note="Xin 7"
FT REPEAT 574..589
FT /note="Xin 8"
FT REPEAT 608..623
FT /note="Xin 9"
FT REPEAT 642..657
FT /note="Xin 10"
FT REPEAT 679..694
FT /note="Xin 11"
FT REPEAT 715..730
FT /note="Xin 12"
FT REPEAT 746..761
FT /note="Xin 13"
FT REPEAT 784..799
FT /note="Xin 14"
FT REPEAT 822..837
FT /note="Xin 15"
FT REPEAT 861..876
FT /note="Xin 16"
FT REPEAT 894..909
FT /note="Xin 17"
FT REPEAT 932..947
FT /note="Xin 18"
FT REPEAT 967..982
FT /note="Xin 19"
FT REPEAT 1006..1021
FT /note="Xin 20"
FT REPEAT 1042..1057
FT /note="Xin 21"
FT REPEAT 1079..1094
FT /note="Xin 22"
FT REPEAT 1117..1132
FT /note="Xin 23"
FT REPEAT 1154..1169
FT /note="Xin 24"
FT REPEAT 1188..1203
FT /note="Xin 25"
FT REPEAT 1219..1234
FT /note="Xin 26"
FT REPEAT 1256..1271
FT /note="Xin 27"
FT REPEAT 1291..1306
FT /note="Xin 28"
FT DOMAIN 3255..3315
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 173..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1864..1889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1963..1982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2018..2124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2152..2190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2203..2279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2293..2354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2461..2489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2551..2573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2640..2676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2801..2922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3478..3518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3536..3561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2285..2333
FT /evidence="ECO:0000255"
FT COILED 2683..2711
FT /evidence="ECO:0000255"
FT COILED 2739..2767
FT /evidence="ECO:0000255"
FT COILED 3043..3075
FT /evidence="ECO:0000255"
FT COMPBIAS 174..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1864..1882
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2031..2064
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2067..2084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2105..2119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2203..2224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2260..2276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2293..2308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2318..2352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2464..2489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2643..2671
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2809..2824
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2859..2889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3547..3561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX6"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX6"
FT MOD_RES 815
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX6"
FT MOD_RES 1576
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX6"
FT MOD_RES 2139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX6"
FT MOD_RES 2974
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71LX6"
FT VAR_SEQ 3253..3551
FT /note="DKEICIICQKTVYPMECLIADKQNFHKSCFRCHHCSSKLSLGNYASLHGRIY
FT CKPHFKQLFKSKGNYDEGFGHKQHKDRWNCKNQSSLVDFIPSGEPDAHENPTADTLLLG
FT DLTTHPDACNSKRQDNDLRKWGDRGKLKIVWPPCQEMPKKNSPPEEEFKVNKAKWPPEV
FT TIPVPSDFKRESLTEHVKTLESQGQEQDSVPDLQPCKHVCQKEDITGIKEIKGYEERKD
FT EKEAKDTLKDAEGLRSKRKSGMEFNDHNAHAQSDGKEKNALVNEADSADVLQVANTDDE
FT GGPENHRENFN -> ETVGPRQGNLHNLSKDSLSNGVPHSRQAEFS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:17046827, ECO:0000303|Ref.3"
FT /id="VSP_030849"
FT VAR_SEQ 3552..3784
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17046827, ECO:0000303|Ref.3"
FT /id="VSP_030850"
FT CONFLICT 44
FT /note="K -> E (in Ref. 5; AAV52766)"
FT /evidence="ECO:0000305"
FT CONFLICT 721
FT /note="T -> A (in Ref. 1; ABL63748)"
FT /evidence="ECO:0000305"
FT CONFLICT 837
FT /note="D -> G (in Ref. 1; ABL63748)"
FT /evidence="ECO:0000305"
FT CONFLICT 1633
FT /note="E -> G (in Ref. 1; ABL63748)"
FT /evidence="ECO:0000305"
FT CONFLICT 2114
FT /note="T -> A (in Ref. 1; ABL63748)"
FT /evidence="ECO:0000305"
FT CONFLICT 2179
FT /note="N -> S (in Ref. 1; ABL63748)"
FT /evidence="ECO:0000305"
FT CONFLICT 2408
FT /note="S -> P (in Ref. 1; ABL63748)"
FT /evidence="ECO:0000305"
FT CONFLICT 2457
FT /note="T -> A (in Ref. 1; ABL63748)"
FT /evidence="ECO:0000305"
FT CONFLICT 2784
FT /note="D -> G (in Ref. 1; ABL63748)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3784 AA; 428259 MW; C95FD2E0AD5CEBBC CRC64;
MARYQAAVSR GDTRSFSANV MEESDVCTVP GGLAKMKRQF EKDKMTSTCN AFSEYQYRHE
SRAEQEAIHS SQEIIRRNEQ EVSKGHGTDV FKAEMMSHLE KHTEETKQAS QFHQYVQETV
IDSPEEEELP KVSTKILKEQ FEKSAQENFL RSDKETSPPA KCMKIENDIE ETLKPSSAVG
TSSSYTSTRQ RKETSTSSYS NHSLTSTTLA QDNGTPSGKM EEFPPPPPDV CQTPMDVTAF
SQSPEFPSPP RRLPMPKDLY SKQRNLYELN RLYRHIHPEL RKNLEKDYIS EVSEIVSSQI
NSGNALSADV QKARYVFENT NDSSQKDLNS ERENLEWDEI LKGEVQSIRW IFENQPLDSI
NHGSTDEGYT SKGIADQELI AGSDVKYTTW MFETQPIDAL GIPSAGTEGN TEKIPELARG
DVYTARWMFE TRPLDSMNKM HECQEETAST LTKDITGGDV KTVRYMFETQ QLDQLGQLHS
VDELNLLQLR SELKEIKGNV KRSIKCFETQ PLYVIRDGSG QMLEIKTVQR EDIEKGDVRT
ARWMFETQPL DTINKDITEI KVVRGISMEE NVKGGVSRAK WLFETQPLEK IKEESGEAVL
KTEAVIGTDV SKKCWMFETQ PLDILKDSPD TDSVSPEERI GGDVKTTKHL FETLPIEALK
DSPDIGKLQK ITASEEEKGD VKHQKWVFET QRLEDIREDK KEYTRTVRLE AVDRGHVKNY
THIFESNNLI KVDASHQIEV EGVTRGTVEL NKSLFETTPL YAIQDHLGKY HQVKTVQQEE
IVRGDVRSCR WLFETRPIDQ FDESLHKFQI IRGISAQEIQ AGNVKSARWL FETQPLDSIK
YFSNVEETDS KTEQSTDIVK GDVKTCKWLF ETQPMESLYE KASLMTNSED IHKGDVRTCM
WLFETQPLDA IKDDSEATVK LQTVKQEEIQ GGDVQTACFL FETENLDNIQ GDEGKENKPL
EMDIQSGDVS GMKFKFENQS LDSINCSSEN VLSKIKTLKA EDIQKGNVLK CRWLFENQPI
DMIKESQECD GLVKTVTDVQ GGDVRKGCFI FETFSLDEIK DESDGISMRE TNLGEIIKGD
VKSYKMLFET QPLYAIQDHE GFYHEVTTVK KEETIHGDVR GTRWLFETKP LDSIHESEDV
YVIKSVTQED IQKGDVSSVR YRFETQPLDM ISDKSHNIVP TVDYIQGGNV QMNKQLFESE
GGNKKNYVRT VSVNEIQKGN VKTSTWLFET HRIDELGEES RYENIKTVTQ EDVQKGDVKQ
AVWLFENQTL DSINELDEND TKMTKEEIPP SDVKTTTWLF ETTPIHEFNK TRVEKEEIIG
KSIKETLEDL YSQRVVEAPG IIIEADEVGD VRMAKYKLMN QTTPEIQKEE VIRADLGNIM
MNLLSQRDCT KKEIFVSEEE KGNVNFTKTQ LLNRSMEFHA EKEEIVRGDV KQAIQKLFSE
ERRAKKGILI QEDEKGDINM TIYCLLHENA GDKTEREDIL GGDVRRTIHN LLSSASNGKI
SERTKIDASE RGNVQFFTTC IETGALDYLK QLQTGSNEST LTASKQEGEE EIIGGDVEGT
KFLLKKRQSS FERTVSETDI IPGDVRHTVK VFMTEPQSSS YKTVKDEIIK GDLKSTLNSL
NQAMNQKTVA KAEEIVKDDR LAILKSLKES GDRQKEPKQS GGMSRDIGQA IECLERATNT
RTEILKKELI LDDLKTSLRS LKEEQCGFKE VDKQGIVKDV LPGMLGFSER PKIGIHPAAV
QRDKKSLLQP VPGPFEPAIK QQAGPGTLDE TTQKPCLRSL IEERTEANLP KAPKGTVKIV
IDREQNNDAL EKSLRKMSNS EHRAMKNVLD MSDRMGIWTE SKEYLCSDDH MSKHLSATMS
IKESLKSKES ENMREAKDDV ISSTQSVDKT FRKQQTQTCE LGNDQKSRFQ DSYGKNQKNI
QNIEITRDFQ KQALLSQEKQ YSNKEMKKNE ASLQPLPVGK EVHSVPGVTV SGKNHKRIQA
TDKRQKTDVC LESQDFLMKT NTSKELKMAM ERSFNPINLH PECGIKENED SLPPPSPPPL
PPSNASSEIE FPLPPPPPLM LLPGKNESPP SSPTEKTRTE FESLSTLPLP PPPVDEKAEQ
ECLSTTLPPP PPPTPCQPGH LLPSSVLGHH REAFLQQFSQ KEALGVHLPH SQAKILTGKS
PPPTLPKPKL PKRIKDKMNQ YSSSGELERS LSDVEIKATL SKDQKRSMVT MSSEHRETKQ
DVFGKGLVGR KQLPVDSANS LSQTVPEIPA PKEKQTAPLV KSHSFPSGSE QQSPKPYMRK
FKTPLMIAEE KYRQQREELE KQRQESSSHN VIKTETQHQS LSEKEEEIEL QKATEAISTP
RKESDFPRAR PNLDSESRAV IAGECSESQL ATASTLTVAT ERLQHVLAAS EDELTLRQEG
IQNSSDASQS KLACETSQSH KECKAQQTFE QHVKRLPFPQ TKPSSPSFKV KTIKLSTLDH
TGTETDLSSK HHTKQSEVDI QTSTEQTDKE IKKTQASIQC DDKPSVPEKY FQLPKTEKRV
TIQMPKEYAE KSHKSKLQTV PKKQGIFGEF DRGNVLGREG KNQDSSVSCS KEDRLIDERK
QEHLQNQRVP RSVQQKVINE RLDSQMQNFQ QTEIQTSRST IECEEFSQSY NATQEKTCLK
DKGKQQGQVT SNTEESKQEL RQNQSAFSSV KDSQHDDGKC TINILEFLRK REELQQILSR
VKQFEAESSK SGLKTFQILL NIVPVWLISE EKREYGVRVA MENNFEKVKE EITHIKTQAE
EMLLQCEHVI QTAMMASQTG KQRDKPTNLN EMPLNVSNVN LSSSKCTEQK ESKTVEEKLT
HRQVTTHPEA ATRNPVKPYQ EAKGEDGKMA PPSLKTRPPS PTFITIESTA RRAETSTKSE
LSQSPKNNRC IEPPPRRPVE HASGLPRSRT PPSPPRSRSE QLVRLKDTTA RLAKGTIPCS
PGTPVPIVEK RSEVVMSPAT LRRQIKIESR GGDSPPTITI PVSVNHVVSG SFRESVDAQE
AVKKTEKTET YVHKDKMNSV NRAMPETESY DAVEIIRKVE GPHLSEHTER FEATNQTVQR
AERFLNGHEN EINRWFREFE NDPVFRAKTE RGAYANGEIN HNMKQESHTF CKEEFGLASS
ETANFTGFSY RHPKVPAMQP RVHSEARSLN EHFSSVDAFD SQIVGSKVAT SSSRSTEAGR
SGFDFKHAPP TYEDVISGHI LDVADSPTNL RRNFQKTWQE SERVFQRVGY ETSDAHATEM
SRAFQEESAF LSDKEICIIC QKTVYPMECL IADKQNFHKS CFRCHHCSSK LSLGNYASLH
GRIYCKPHFK QLFKSKGNYD EGFGHKQHKD RWNCKNQSSL VDFIPSGEPD AHENPTADTL
LLGDLTTHPD ACNSKRQDND LRKWGDRGKL KIVWPPCQEM PKKNSPPEEE FKVNKAKWPP
EVTIPVPSDF KRESLTEHVK TLESQGQEQD SVPDLQPCKH VCQKEDITGI KEIKGYEERK
DEKEAKDTLK DAEGLRSKRK SGMEFNDHNA HAQSDGKEKN ALVNEADSAD VLQVANTDDE
GGPENHRENF NNNNNNSVAV SSLNNGRQKI SISERPRLLQ AVSEANYYTS EYQIKNFNNA
SKISELLGIF ESQKLSSKKV LALALERTAD RGTAGSPLQL VLEPGLQQGF SVKGENLAAS
PDVSPLHIKG NHENNKNVHL FFSNTVKITS FSKKHNILGC DLMDSVDQLK NMSCLYLREL
GKNVKCWHGE TAGAARHGGK MCFDAQSQGS AAKPVFPSMQ CQAQHLTVEE QIKRDRCYSD
SEAD
