NRAP_MOUSE
ID NRAP_MOUSE Reviewed; 1728 AA.
AC Q80XB4; E9QN76; O35884; Q3UTY7; Q3UU10; Q80V40;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Nebulin-related-anchoring protein;
DE Short=N-RAP;
GN Name=Nrap {ECO:0000312|MGI:MGI:1098765};
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:AAC53323.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, INTERACTION WITH ACTIN,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9295142;
RX DOI=10.1002/(sici)1097-0169(1997)38:1<75::aid-cm7>3.0.co;2-g;
RA Luo G., Zhang J.Q., Nguyen T.P., Herrera A.H., Paterson B., Horowits R.;
RT "Complete cDNA sequence and tissue localization of N-RAP, a novel nebulin-
RT related protein of striated muscle.";
RL Cell Motil. Cytoskeleton 38:75-90(1997).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAO47075.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAO47075.1};
RC TISSUE=Heart muscle {ECO:0000312|EMBL:AAO47076.1}, and
RC Skeletal muscle {ECO:0000312|EMBL:AAO47075.1};
RX PubMed=12789664; DOI=10.1002/cm.10123;
RA Mohiddin S.A., Lu S., Cardoso J.-P., Carroll S., Jha S., Horowits R.,
RA Fananapazir L.;
RT "Genomic organization, alternative splicing, and expression of human and
RT mouse N-RAP, a nebulin-related LIM protein of striated muscle.";
RL Cell Motil. Cytoskeleton 55:200-212(2003).
RN [3]
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 [4] {ECO:0000305, ECO:0000312|EMBL:BAE23819.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-579 (ISOFORM 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1317-1728 (ISOFORMS 1/2/4).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE23819.1};
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 [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH ACTIN; TLN1 AND VCL.
RX PubMed=10320340; DOI=10.1021/bi982395t;
RA Luo G., Herrera A.H., Horowits R.;
RT "Molecular interactions of N-RAP, a nebulin-related protein of striated
RT muscle myotendon junctions and intercalated disks.";
RL Biochemistry 38:6135-6143(1999).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ALPHA-ACTININ, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11732910; DOI=10.1021/bi0107445;
RA Zhang J.Q., Elzey B., Williams G., Lu S., Law D.J., Horowits R.;
RT "Ultrastructural and biochemical localization of N-RAP at the interface
RT between myofibrils and intercalated disks in the mouse heart.";
RL Biochemistry 40:14898-14906(2001).
RN [7] {ECO:0000305}
RP INTERACTION WITH ALPHA-ACTININ AND KLHL41.
RX PubMed=12692149; DOI=10.1242/jcs.00425;
RA Lu S., Carroll S.L., Herrera A.H., Ozanne B., Horowits R.;
RT "New N-RAP-binding partners alpha-actinin, filamin and Krp1 detected by
RT yeast two-hybrid screening: implications for myofibril assembly.";
RL J. Cell Sci. 116:2169-2178(2003).
RN [8] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=15765519; DOI=10.1002/dvdy.20314;
RA Lu S., Borst D.E., Horowits R.;
RT "N-RAP expression during mouse heart development.";
RL Dev. Dyn. 233:201-212(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND SER-1078, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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: May be involved in anchoring the terminal actin filaments in
CC the myofibril to the membrane and in transmitting tension from the
CC myofibrils to the extracellular matrix. {ECO:0000269|PubMed:10320340,
CC ECO:0000269|PubMed:11732910, ECO:0000269|PubMed:9295142}.
CC -!- SUBUNIT: Interacts with actin, alpha-actinin, KLHL41, TLN1 and VCL.
CC Interacts with CSRP3. {ECO:0000250|UniProtKB:Q86VF7,
CC ECO:0000269|PubMed:10320340, ECO:0000269|PubMed:11732910,
CC ECO:0000269|PubMed:12692149, ECO:0000269|PubMed:9295142}.
CC -!- SUBCELLULAR LOCATION: Note=Localized at the myotendinous junction in
CC skeletal muscle and at the intercalated disk in cardiac muscle.
CC {ECO:0000269|PubMed:11732910, ECO:0000269|PubMed:15765519,
CC ECO:0000269|PubMed:9295142}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000269|PubMed:12789664}; Synonyms=S
CC {ECO:0000269|PubMed:12789664};
CC IsoId=Q80XB4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:12789664}; Synonyms=C
CC {ECO:0000269|PubMed:12789664};
CC IsoId=Q80XB4-2; Sequence=VSP_052160;
CC Name=3 {ECO:0000269|PubMed:9295142};
CC IsoId=Q80XB4-3; Sequence=VSP_052160, VSP_052162;
CC Name=4 {ECO:0000269|PubMed:16141072};
CC IsoId=Q80XB4-4; Sequence=VSP_052159, VSP_052160;
CC -!- TISSUE SPECIFICITY: Expressed in cardiac and skeletal muscle. Not
CC detected in kidney, spleen, liver, brain, lung, stomach or uterus.
CC {ECO:0000269|PubMed:11732910, ECO:0000269|PubMed:9295142}.
CC -!- DEVELOPMENTAL STAGE: Expression significantly increased from 10.5 dpc
CC to 16.5 dpc, and subsequently remained constant until 21 days after
CC birth. In 9.5 dpc to 10.5 dpc embryonic heart, expression is primarily
CC associated with developing premyofibril structures containing alpha-
CC actinin. {ECO:0000269|PubMed:15765519}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC53323.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U76618; AAC53323.1; ALT_FRAME; mRNA.
DR EMBL; AY177622; AAO47075.1; -; mRNA.
DR EMBL; AY177623; AAO47076.1; -; mRNA.
DR EMBL; AC115771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK138925; BAE23819.1; -; mRNA.
DR EMBL; AK138975; BAE23843.1; -; mRNA.
DR CCDS; CCDS29913.1; -. [Q80XB4-1]
DR CCDS; CCDS29914.1; -. [Q80XB4-2]
DR PIR; T37192; T37192.
DR RefSeq; NP_001273481.1; NM_001286552.1.
DR RefSeq; NP_032759.3; NM_008733.4. [Q80XB4-1]
DR RefSeq; NP_932307.2; NM_198059.3. [Q80XB4-2]
DR RefSeq; XP_006526811.1; XM_006526748.3. [Q80XB4-4]
DR AlphaFoldDB; Q80XB4; -.
DR SMR; Q80XB4; -.
DR BioGRID; 201842; 8.
DR STRING; 10090.ENSMUSP00000073228; -.
DR iPTMnet; Q80XB4; -.
DR PhosphoSitePlus; Q80XB4; -.
DR MaxQB; Q80XB4; -.
DR PaxDb; Q80XB4; -.
DR PRIDE; Q80XB4; -.
DR ProteomicsDB; 293891; -. [Q80XB4-1]
DR ProteomicsDB; 293892; -. [Q80XB4-2]
DR ProteomicsDB; 293893; -. [Q80XB4-3]
DR ProteomicsDB; 293894; -. [Q80XB4-4]
DR Antibodypedia; 51692; 78 antibodies from 18 providers.
DR DNASU; 18175; -.
DR Ensembl; ENSMUST00000040711; ENSMUSP00000048364; ENSMUSG00000049134. [Q80XB4-2]
DR Ensembl; ENSMUST00000073536; ENSMUSP00000073228; ENSMUSG00000049134. [Q80XB4-1]
DR Ensembl; ENSMUST00000095947; ENSMUSP00000093640; ENSMUSG00000049134. [Q80XB4-4]
DR GeneID; 18175; -.
DR KEGG; mmu:18175; -.
DR UCSC; uc008hyu.3; mouse. [Q80XB4-1]
DR UCSC; uc008hyv.3; mouse. [Q80XB4-2]
DR UCSC; uc012bnr.3; mouse. [Q80XB4-4]
DR CTD; 4892; -.
DR MGI; MGI:1098765; Nrap.
DR VEuPathDB; HostDB:ENSMUSG00000049134; -.
DR eggNOG; KOG1702; Eukaryota.
DR GeneTree; ENSGT00940000158418; -.
DR HOGENOM; CLU_003010_1_0_1; -.
DR InParanoid; Q80XB4; -.
DR OMA; NKGYSMN; -.
DR OrthoDB; 1549538at2759; -.
DR PhylomeDB; Q80XB4; -.
DR TreeFam; TF313758; -.
DR BioGRID-ORCS; 18175; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Nrap; mouse.
DR PRO; PR:Q80XB4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q80XB4; protein.
DR Bgee; ENSMUSG00000049134; Expressed in tarsal region and 86 other tissues.
DR ExpressionAtlas; Q80XB4; baseline and differential.
DR Genevisible; Q80XB4; MM.
DR GO; GO:0005916; C:fascia adherens; IDA:UniProtKB.
DR GO; GO:0005927; C:muscle tendon junction; IDA:UniProtKB.
DR GO; GO:0030016; C:myofibril; IDA:MGI.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IDA:UniProtKB.
DR GO; GO:0017166; F:vinculin binding; IPI:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:MGI.
DR GO; GO:0071691; P:cardiac muscle thin filament assembly; IBA:GO_Central.
DR InterPro; IPR013998; Nebulin-like.
DR InterPro; IPR000900; Nebulin_repeat.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF00880; Nebulin; 8.
DR PRINTS; PR00510; NEBULIN.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00227; NEBU; 42.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS51216; NEBULIN; 41.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; LIM domain; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc.
FT CHAIN 1..1728
FT /note="Nebulin-related-anchoring protein"
FT /id="PRO_0000248859"
FT DOMAIN 4..64
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REPEAT 173..200
FT /note="Nebulin 1"
FT /evidence="ECO:0000255"
FT REPEAT 201..235
FT /note="Nebulin 2"
FT /evidence="ECO:0000255"
FT REPEAT 244..271
FT /note="Nebulin 3"
FT /evidence="ECO:0000255"
FT REPEAT 313..340
FT /note="Nebulin 4"
FT /evidence="ECO:0000255"
FT REPEAT 345..379
FT /note="Nebulin 5"
FT /evidence="ECO:0000255"
FT REPEAT 386..414
FT /note="Nebulin 6"
FT /evidence="ECO:0000255"
FT REPEAT 416..450
FT /note="Nebulin 7"
FT /evidence="ECO:0000255"
FT REPEAT 484..518
FT /note="Nebulin 8"
FT /evidence="ECO:0000255"
FT REPEAT 519..553
FT /note="Nebulin 9"
FT /evidence="ECO:0000255"
FT REPEAT 555..589
FT /note="Nebulin 10"
FT /evidence="ECO:0000255"
FT REPEAT 599..623
FT /note="Nebulin 11"
FT /evidence="ECO:0000255"
FT REPEAT 624..658
FT /note="Nebulin 12"
FT /evidence="ECO:0000255"
FT REPEAT 659..689
FT /note="Nebulin 13"
FT /evidence="ECO:0000255"
FT REPEAT 699..721
FT /note="Nebulin 14"
FT /evidence="ECO:0000255"
FT REPEAT 723..757
FT /note="Nebulin 15"
FT /evidence="ECO:0000255"
FT REPEAT 758..792
FT /note="Nebulin 16"
FT /evidence="ECO:0000255"
FT REPEAT 794..828
FT /note="Nebulin 17"
FT /evidence="ECO:0000255"
FT REPEAT 841..866
FT /note="Nebulin 18"
FT /evidence="ECO:0000255"
FT REPEAT 867..893
FT /note="Nebulin 19"
FT /evidence="ECO:0000255"
FT REPEAT 898..932
FT /note="Nebulin 20"
FT /evidence="ECO:0000255"
FT REPEAT 943..960
FT /note="Nebulin 21"
FT /evidence="ECO:0000255"
FT REPEAT 966..1000
FT /note="Nebulin 22"
FT /evidence="ECO:0000255"
FT REPEAT 1001..1035
FT /note="Nebulin 23"
FT /evidence="ECO:0000255"
FT REPEAT 1037..1071
FT /note="Nebulin 24"
FT /evidence="ECO:0000255"
FT REPEAT 1075..1109
FT /note="Nebulin 25"
FT /evidence="ECO:0000255"
FT REPEAT 1110..1136
FT /note="Nebulin 26"
FT /evidence="ECO:0000255"
FT REPEAT 1141..1175
FT /note="Nebulin 27"
FT /evidence="ECO:0000255"
FT REPEAT 1180..1203
FT /note="Nebulin 28"
FT /evidence="ECO:0000255"
FT REPEAT 1209..1243
FT /note="Nebulin 29"
FT /evidence="ECO:0000255"
FT REPEAT 1244..1278
FT /note="Nebulin 30"
FT /evidence="ECO:0000255"
FT REPEAT 1280..1314
FT /note="Nebulin 31"
FT /evidence="ECO:0000255"
FT REPEAT 1318..1352
FT /note="Nebulin 32"
FT /evidence="ECO:0000255"
FT REPEAT 1353..1379
FT /note="Nebulin 33"
FT /evidence="ECO:0000255"
FT REPEAT 1384..1418
FT /note="Nebulin 34"
FT /evidence="ECO:0000255"
FT REPEAT 1425..1446
FT /note="Nebulin 35"
FT /evidence="ECO:0000255"
FT REPEAT 1452..1478
FT /note="Nebulin 36"
FT /evidence="ECO:0000255"
FT REPEAT 1487..1521
FT /note="Nebulin 37"
FT /evidence="ECO:0000255"
FT REPEAT 1523..1557
FT /note="Nebulin 38"
FT /evidence="ECO:0000255"
FT REPEAT 1561..1595
FT /note="Nebulin 39"
FT /evidence="ECO:0000255"
FT REPEAT 1596..1630
FT /note="Nebulin 40"
FT /evidence="ECO:0000255"
FT REPEAT 1637..1661
FT /note="Nebulin 41"
FT /evidence="ECO:0000255"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1078
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_052159"
FT VAR_SEQ 368..402
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12789664,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9295142"
FT /id="VSP_052160"
FT VAR_SEQ 1443..1650
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9295142"
FT /id="VSP_052162"
FT CONFLICT 51
FT /note="K -> M (in Ref. 1; AAC53323)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="G -> R (in Ref. 2; AAO47075)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="A -> T (in Ref. 1; AAC53323)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="P -> A (in Ref. 1; AAC53323)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="N -> T (in Ref. 1; AAC53323)"
FT /evidence="ECO:0000305"
FT CONFLICT 908
FT /note="V -> A (in Ref. 1; AAC53323)"
FT /evidence="ECO:0000305"
FT CONFLICT 924
FT /note="R -> G (in Ref. 2; AAO47076)"
FT /evidence="ECO:0000305"
FT CONFLICT 956
FT /note="K -> E (in Ref. 2; AAO47076)"
FT /evidence="ECO:0000305"
FT CONFLICT 1158
FT /note="H -> R (in Ref. 2; AAO47075)"
FT /evidence="ECO:0000305"
FT CONFLICT 1383
FT /note="H -> R (in Ref. 1; AAC53323)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1728 AA; 195756 MW; FD21BDD3925FFE4F CRC64;
MNVQACSRCG YGVYPAEKIS CIDQTWHKAC FHCEVCKMML SVNNFVSHQK KPYCHAHNPK
NNTFTSVYHT PLNLTLKKSV AAMGGIDGKE DGEPFKSVLH WDMKSKAGAG AASRLMNERD
YWPGYAEGNT WCPGALPDPE IVRMVEARQS LGEGYTEDRE QQQGKGSFPA MITPAYQRAK
AANQLASQVQ YKRGHDERVS TFTPVADTPE LLRAKAGGQL QNDVRYTEDG GQQRGKGSFP
AMITPAYQIA KRATELASDV RYHQQYHREM KGMASPVGAE GGMTKDSVDR CGQVYSEECD
EPRGKGSFPA MITPAYQNAK KANELVSDIK YRQDFHKMKG AAHFHSLAAQ DNLVLKRAQS
VSKLVSEVEY KKGLENSKGH SINYCETPQF RNVSKISKFT SDNKYKENYQ TQLRGHYDGV
GMDRRMLHAL KVGSLASNVA YKADYKHDVV DYNYLATATP FYQTTMRLVP LKDVNYRQNI
DRMKFSSVTN TPQIVQAKIN AQQLSHVNYR ADYERNKLNY TLPQDAPQLL KAKANAELFS
EVKYKEGWQK TKGKGFEMKL DAMSLLAAKA SGELASSVKY KEEYEKMKGR ALGATDSKLL
HSLQVAKMSS EVEYKKGFEE SKTHFNLPMD MVNLRHAKKA QALASDLDYR KKLHDYTVLP
EDMKTQWAKK AYGLQSELQY KADLAWMRGV GWLTEGSLNL EQAKKAGQLI SEKNYRQRVD
ELKFTSVADS SQMEHAKKSQ GLQNAVAYKA GNEQSVHQYT ISKDEPLFLR ARANAAQLSE
TLYKSSWEKQ KAKGFELRLD SLAFLTAKAK RDLASEVKYK EDYERSRGKL IGAKSAQGDS
QMSHSLQMSK LQSDLEYKKG FEDTRSQCHI SLDMVHLVHA RQAQHLATDV GYRTASHCFT
ALPTDMKVEW AKKAYGLQSD NQYRADMKWM KGTGWVATGS LHVEQAKKAG ELISEKKYRQ
HPDALKFTSI KDTPEMVQAR ISYTQAVDRL YREQGENVKH HYTQTADLPE VLLAKLNAMN
ISETRYKESW SRLRDGGYKL RLDALPFQAA KASSEVISDY KYKEAFERMK GQMLGSRSLE
DDLSLAHSVH ATSLQSDVNY KKGFEHAKAH FHLPLDMVTL VHAKKAQTLA SDQDYRHPLP
QHTVLAEDLR LSCAKKAHKL QSENLYRSDL NFMRGVPCVV PGTLEIEGRK KASELISESK
YRQHPGSFKY TAVTDTPNLL HAKYSNQITN ERLYKAAGED ARHQYTMTLG LPEFIRAKTN
AANLSEAKYK EAWHNLRAQG YKLTIDALPF QAARASGDIA SDFLYRHEFV KERGQLIGVR
NVSDDPRLLH CLRMGQLQSE NQYRKEAASS QAQCHLPMDM MYLVHARKAQ ALASDHDYRT
QCHEFTALPE DLKMAWAKKA HALQSEFRYK ADLMGMKGTG WLALQSPQIE SAKKAGDLIS
ETKYRKKPDS IKFTTVVDSP DLIHAKESYM HCNERLYRLG DAASLHRYTP IPDHPDFTRA
RMNAMHLSDK VYRNAWEQSR AGGYDFRLDA IPFQTARVSR DIASDFRYKE AFLRDRGLQI
GYRSISDDPR TTHFLRVGRL QSDNEYRKAF AKGRSQFHSR ADQPGFLQAK RSQQLASDVL
YRQPLPQHTS DPEQLGLKHA RKAHQLQSDV KYKSDLNLTR GVGWTPPGSY KVEMARRAAE
LANRRGPGIR GASVEPEAAA ALGDHQSRGV NPDASEILHI HKKKTLLM
