NCAP_ANDV
ID NCAP_ANDV Reviewed; 428 AA.
AC O36307; Q80DP9;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Nucleoprotein;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q89462};
DE AltName: Full=Nucleocapsid protein;
DE Short=Protein N;
GN Name=N;
OS Andes orthohantavirus (ANDV) (Andes virus).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC Orthohantavirus.
OX NCBI_TaxID=1980456;
OH NCBI_TaxID=29094; Abrothrix longipilis (Long-haired grass mouse) (Akodon longipilis).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=89122; Loxodontomys micropus (Southern big-eared mouse) (Auliscomys micropus).
OH NCBI_TaxID=37015; Oligoryzomys chacoensis (Chacoan pygmy rice rat).
OH NCBI_TaxID=218824; Oligoryzomys flavescens (yellow pygmy rice rat).
OH NCBI_TaxID=137207; Oligoryzomys longicaudatus (Long-tailed pygmy rice rat).
OH NCBI_TaxID=37019; Oligoryzomys sp..
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=AH-1;
RX PubMed=9255937; DOI=10.1016/s0168-1702(97)00053-1;
RA Lopez N., Padula P., Rossi C., Miguel S., Edelstein A., Ramirez E.,
RA Franze-Fernandez M.T.;
RT "Genetic characterization and phylogeny of Andes virus and variants from
RT Argentina and Chile.";
RL Virus Res. 50:77-84(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=AH-1;
RX PubMed=12185264; DOI=10.1099/0022-1317-83-9-2117;
RA Padula P.J., Sanchez A.J., Edelstein A., Nichol S.T.;
RT "Complete nucleotide sequence of the M RNA segment of Andes virus and
RT analysis of the variability of the termini of the virus S, M and L RNA
RT segments.";
RL J. Gen. Virol. 83:2117-2122(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Chile-9717869;
RX PubMed=11907216; DOI=10.1128/jvi.76.8.3765-3773.2002;
RA Bohlman M.C., Morzunov S.P., Meissner J., Taylor M.B., Ishibashi K.,
RA Rowe J., Levis S., Enria D., St Jeor S.C.;
RT "Analysis of hantavirus genetic diversity in Argentina: S segment-derived
RT phylogeny.";
RL J. Virol. 76:3765-3773(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Chile-9717869;
RX PubMed=12367756; DOI=10.1016/s0168-1702(02)00129-6;
RA Meissner J.D., Rowe J.E., Borucki M.K., St Jeor S.C.;
RT "Complete nucleotide sequence of a Chilean hantavirus.";
RL Virus Res. 89:131-143(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=CHI-7913;
RX PubMed=14513715; DOI=10.4067/s0716-97602003000200010;
RA Tischler N.D., Fernandez J., Muller I., Martinez R., Galeno H.,
RA Villagra E., Mora J., Ramirez E., Rosemblatt M., Valenzuela P.D.;
RT "Complete sequence of the genome of the human isolate of Andes virus CHI-
RT 7913: comparative sequence and protein structure analysis.";
RL Biol. Res. 36:201-210(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Epilink/96_2/6/19 {ECO:0000312|EMBL:QNQ18240.1},
RC Epuyen/18-19_Patient_10_12/10/18 {ECO:0000312|EMBL:QNQ18246.1},
RC Epuyen/18-19_Patient_11_12/15/18 {ECO:0000312|EMBL:QNQ18247.1},
RC Epuyen/18-19_Patient_12_12/19/18 {ECO:0000312|EMBL:QNQ18248.1},
RC Epuyen/18-19_Patient_13_12/24/18 {ECO:0000312|EMBL:QNQ18249.1},
RC Epuyen/18-19_Patient_14_12/26/18 {ECO:0000312|EMBL:QNQ18250.1},
RC Epuyen/18-19_Patient_15_12/26/18 {ECO:0000312|EMBL:QNQ18251.1},
RC Epuyen/18-19_Patient_16_12/28/18 {ECO:0000312|EMBL:QNQ18252.1},
RC Epuyen/18-19_Patient_17_12/31/18 {ECO:0000312|EMBL:QNQ18253.1},
RC Epuyen/18-19_Patient_18_12/31/18 {ECO:0000312|EMBL:QNQ18254.1},
RC Epuyen/18-19_Patient_19_1/2/19 {ECO:0000312|EMBL:QNQ18255.1},
RC Epuyen/18-19_Patient_1_11/3/18 {ECO:0000312|EMBL:QNQ18256.1},
RC Epuyen/18-19_Patient_20_1/1/19 {ECO:0000312|EMBL:QNQ18257.1},
RC Epuyen/18-19_Patient_22_1/1/19 {ECO:0000312|EMBL:QNQ18258.1},
RC Epuyen/18-19_Patient_23_1/7/19 {ECO:0000312|EMBL:QNQ18259.1},
RC Epuyen/18-19_Patient_24_1/3/19 {ECO:0000312|EMBL:QNQ18260.1},
RC Epuyen/18-19_Patient_25_1/6/19 {ECO:0000312|EMBL:QNQ18261.1},
RC Epuyen/18-19_Patient_26_1/4/19 {ECO:0000312|EMBL:QNQ18262.1},
RC Epuyen/18-19_Patient_27_1/8/19 {ECO:0000312|EMBL:QNQ18263.1},
RC Epuyen/18-19_Patient_28_1/6/19 {ECO:0000312|EMBL:QNQ18264.1},
RC Epuyen/18-19_Patient_29_1/14/19 {ECO:0000312|EMBL:QNQ18265.1},
RC Epuyen/18-19_Patient_2_11/23/18 {ECO:0000312|EMBL:QNQ18266.1},
RC Epuyen/18-19_Patient_3_11/20/18 {ECO:0000312|EMBL:QNQ18267.1},
RC Epuyen/18-19_Patient_4_11/27/18 {ECO:0000312|EMBL:QNQ18268.1},
RC Epuyen/18-19_Patient_5_11/26/18 {ECO:0000312|EMBL:QNQ18269.1},
RC Epuyen/18-19_Patient_6_11/25/18 {ECO:0000312|EMBL:QNQ18270.1},
RC Epuyen/18-19_Patient_8_12/13/18 {ECO:0000312|EMBL:QNQ18272.1},
RC Epuyen/18-19_Patient_9_12/12/18 {ECO:0000312|EMBL:QNQ18273.1},
RC NRC-2/97_06/01/1996 {ECO:0000312|EMBL:QNQ18241.1},
RC NRC-3/18_06/01/1997 {ECO:0000312|EMBL:QNQ18242.1},
RC NRC-4/18_06/01/2018 {ECO:0000312|EMBL:QNQ18243.1},
RC NRC-5/18_06/01/2018 {ECO:0000312|EMBL:QNQ18244.1}, and
RC NRC-6/18_05/21/18 {ECO:0000312|EMBL:QNQ18245.1};
RA Martinez V.P., Perez-Sautu U., Alonso D.O., Di Paola N., Bellomo C.M.,
RA Iglesias A.A., Coelho R.M., Periolo N., Nagle E.R., Chitty J.A.,
RA Pratt C.B., Wiley M.R., Diaz J., Biondo E., Lewis L., Anselmo C.,
RA Pontoriero F., Lavarra E., Kuhn J.H., Sanchez-Lockhart M., Edelstein A.,
RA Cisterna D., Campos J., Kaler M., Rubinstein A., Perandones C.,
RA Palacios G.;
RT "A lethal person-to-person outbreak of Andes virus Hantavirus Pulmonary
RT Syndrome was driven by super-spreader transmission events.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=AREB14/P1 {ECO:0000312|EMBL:QIQ51415.1},
RC AREB14/P2 {ECO:0000312|EMBL:QIQ51416.1},
RC AREB14/P3 {ECO:0000312|EMBL:QIQ51417.1}, and
RC ARLA17/NRC2 {ECO:0000312|EMBL:QIQ51419.1};
RX PubMed=32186494; DOI=10.3201/eid2604.190799;
RA Alonso D.O., Perez-Sautu U., Bellomo C.M., Prieto K., Iglesias A.,
RA Coelho R., Periolo N., Domenech I., Talmon G., Hansen R., Palacios G.,
RA Martinez V.P.;
RT "Person-to-Person Transmission of Andes Virus in Hantavirus Pulmonary
RT Syndrome, Argentina, 2014.";
RL Emerg. Infect. Dis. 26:756-759(2020).
RN [8]
RP FUNCTION.
RX PubMed=24549848; DOI=10.1128/mbio.01088-13;
RA Cimica V., Dalrymple N.A., Roth E., Nasonov A., Mackow E.R.;
RT "An innate immunity-regulating virulence determinant is uniquely encoded by
RT the Andes virus nucleocapsid protein.";
RL MBio 5:0-0(2014).
RN [9]
RP FUNCTION.
RC STRAIN=Chile-9717869;
RX PubMed=25410857; DOI=10.1128/jvi.02347-14;
RA Wang Z., Mir M.A.;
RT "Andes virus nucleocapsid protein interrupts protein kinase R dimerization
RT to counteract host interference in viral protein synthesis.";
RL J. Virol. 89:1628-1639(2015).
RN [10]
RP FUNCTION, MUTAGENESIS OF SER-386, AND PHOSPHORYLATION AT SER-386.
RX PubMed=30867297; DOI=10.1128/jvi.00338-19;
RA Simons M.J., Gorbunova E.E., Mackow E.R.;
RT "Unique Interferon Pathway Regulation by the Andes Virus Nucleocapsid
RT Protein Is Conferred by Phosphorylation of Serine 386.";
RL J. Virol. 93:0-0(2019).
RN [11] {ECO:0007744|PDB:2K48}
RP STRUCTURE BY NMR OF 1-74, DOMAIN, AND COILED COIL.
RX PubMed=18687679; DOI=10.1074/jbc.m804869200;
RA Wang Y., Boudreaux D.M., Estrada D.F., Egan C.W., St Jeor S.C.,
RA De Guzman R.N.;
RT "NMR structure of the N-terminal coiled coil domain of the Andes hantavirus
RT nucleocapsid protein.";
RL J. Biol. Chem. 283:28297-28304(2008).
RN [12] {ECO:0007744|PDB:5E04}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 117-399, SUBUNIT, AND MUTAGENESIS
RP OF LEU-102; VAL-104; ILE-107; LEU-405; LEU-408 AND LEU-412.
RX PubMed=26559827; DOI=10.1128/jvi.02523-15;
RA Guo Y., Wang W., Sun Y., Ma C., Wang X., Wang X., Liu P., Shen S., Li B.,
RA Lin J., Deng F., Wang H., Lou Z.;
RT "Crystal Structure of the Core Region of Hantavirus Nucleocapsid Protein
RT Reveals the Mechanism for Ribonucleoprotein Complex Formation.";
RL J. Virol. 90:1048-1061(2016).
CC -!- FUNCTION: Encapsidates the genome protecting it from nucleases
CC (Probable). The encapsidated genomic RNA is termed the nucleocapsid
CC (NC) and serves as template for transcription and replication
CC (Probable). The nucleocapsid has a left-handed helical structure (By
CC similarity). As a trimer, specifically binds and acts as a chaperone to
CC unwind the panhandle structure formed by the viral RNA (vRNA) termini
CC (By similarity). Involved in the transcription and replication
CC initiation of vRNA by mediating primer annealing (By similarity). Plays
CC a role in cap snatching by sequestering capped RNAs in P bodies for use
CC by the viral RdRp during transcription initiation (By similarity).
CC Substitutes for the cellular cap-binding complex (eIF4F) to
CC preferentially facilitate the translation of capped mRNAs (By
CC similarity). Initiates the translation by specifically binding to the
CC cap and 40S ribosomal subunit (By similarity). Prevents the viral
CC glycoprotein N (Gn) from autophagy-dependent breakdown maybe by
CC blocking autophagosome formation (By similarity). Inhibits host
CC EIF2AK2/PKR dimerization to prevent PKR-induced translational shutdown
CC in cells and thus the activation of the antiviral state
CC (PubMed:25410857). Inhibits IFN signaling responses directed by the
CC dsRNA sensors DDX58/RIG-I and IFIH1/MDA5, probably by interacting with
CC host E3 ubiquitin ligase TRIM21 (PubMed:24549848). As a consequence,
CC TBK1-directed IRF3 phosphorylation and TBK1 autophosphorylation are
CC inhibited (PubMed:24549848, PubMed:30867297). Also displays sequence-
CC unspecific DNA endonuclease activity (By similarity).
CC {ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462,
CC ECO:0000269|PubMed:24549848, ECO:0000269|PubMed:25410857,
CC ECO:0000269|PubMed:30867297, ECO:0000305}.
CC -!- SUBUNIT: Homotrimer (By similarity). Homomultimer (PubMed:26559827).
CC Homomultimerizes and binds to viral genomic RNA to form the
CC nucleocapsid (By similarity). Interacts with host MAP1LC3B; this
CC interaction participates to the protection of Gn from virus-triggered
CC autophagy (By similarity). Interacts with host SNAP29; this interaction
CC participates to the protection of glycoprotein N from virus-triggered
CC autophagy (By similarity). Interacts (via N-terminus) with host RPS19;
CC this interaction probably mediates the loading of the 40S ribosomal
CC subunit on viral capped mRNA during N-mediated translation initiation
CC (By similarity). Interacts with the viral RdRp (By similarity).
CC Interacts with host SUMO1 (via N-terminus) (By similarity). Interacts
CC with host DAXX (By similarity). Interacts with the viral glycoprotein N
CC (via C-terminus) (By similarity). Interacts with the viral glycoprotein
CC C (via C-terminus) (By similarity). {ECO:0000250|UniProtKB:P05133,
CC ECO:0000250|UniProtKB:P27313, ECO:0000250|UniProtKB:Q88918,
CC ECO:0000250|UniProtKB:Q89462, ECO:0000269|PubMed:26559827}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P05133}. Host
CC cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P05133}. Host
CC Golgi apparatus, host cis-Golgi network {ECO:0000250|UniProtKB:P05133}.
CC Note=Internal protein of virus particle.
CC {ECO:0000250|UniProtKB:P05133}.
CC -!- DOMAIN: The N-terminus is required for chaperone activity and, in
CC trimeric form, this region likely serves in high affinity vRNA
CC panhandle recognition (By similarity). The N-terminus also contains a
CC coiled coil region, which probably participates in but is insufficient
CC to initiate N trimerization (PubMed:18687679). The YxxL motif is
CC indispensable for the interaction with host MAP1LC3B (By similarity).
CC The central region is involved in specific RNA-binding (By similarity).
CC Has distinct cap- and RNA-binding sites so it can bind simultaneously
CC both the vRNA and mRNA cap (By similarity).
CC {ECO:0000250|UniProtKB:P05133, ECO:0000250|UniProtKB:Q89462,
CC ECO:0000269|PubMed:18687679}.
CC -!- SIMILARITY: Belongs to the hantavirus nucleocapsid protein family.
CC {ECO:0000305}.
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DR EMBL; AF004660; AAB69170.1; -; Genomic_RNA.
DR EMBL; AF291702; AAG22531.1; -; Genomic_RNA.
DR EMBL; AF324902; AAK14323.1; -; Genomic_RNA.
DR EMBL; AY228237; AAO86636.1; -; Genomic_RNA.
DR EMBL; MN850083; QIQ51415.1; -; Viral_cRNA.
DR EMBL; MN850084; QIQ51416.1; -; Viral_cRNA.
DR EMBL; MN850085; QIQ51417.1; -; Viral_cRNA.
DR EMBL; MN850087; QIQ51419.1; -; Viral_cRNA.
DR EMBL; MN258223; QNQ18240.1; -; Viral_cRNA.
DR EMBL; MN258224; QNQ18241.1; -; Viral_cRNA.
DR EMBL; MN258225; QNQ18242.1; -; Viral_cRNA.
DR EMBL; MN258226; QNQ18243.1; -; Viral_cRNA.
DR EMBL; MN258227; QNQ18244.1; -; Viral_cRNA.
DR EMBL; MN258228; QNQ18245.1; -; Viral_cRNA.
DR EMBL; MN258229; QNQ18246.1; -; Viral_cRNA.
DR EMBL; MN258230; QNQ18247.1; -; Viral_cRNA.
DR EMBL; MN258231; QNQ18248.1; -; Viral_cRNA.
DR EMBL; MN258232; QNQ18249.1; -; Viral_cRNA.
DR EMBL; MN258233; QNQ18250.1; -; Viral_cRNA.
DR EMBL; MN258234; QNQ18251.1; -; Viral_cRNA.
DR EMBL; MN258235; QNQ18252.1; -; Viral_cRNA.
DR EMBL; MN258236; QNQ18253.1; -; Viral_cRNA.
DR EMBL; MN258237; QNQ18254.1; -; Viral_cRNA.
DR EMBL; MN258238; QNQ18255.1; -; Viral_cRNA.
DR EMBL; MN258239; QNQ18256.1; -; Viral_cRNA.
DR EMBL; MN258240; QNQ18257.1; -; Viral_cRNA.
DR EMBL; MN258241; QNQ18258.1; -; Viral_cRNA.
DR EMBL; MN258242; QNQ18259.1; -; Viral_cRNA.
DR EMBL; MN258243; QNQ18260.1; -; Viral_cRNA.
DR EMBL; MN258244; QNQ18261.1; -; Viral_cRNA.
DR EMBL; MN258245; QNQ18262.1; -; Viral_cRNA.
DR EMBL; MN258246; QNQ18263.1; -; Viral_cRNA.
DR EMBL; MN258247; QNQ18264.1; -; Viral_cRNA.
DR EMBL; MN258248; QNQ18265.1; -; Viral_cRNA.
DR EMBL; MN258249; QNQ18266.1; -; Viral_cRNA.
DR EMBL; MN258250; QNQ18267.1; -; Viral_cRNA.
DR EMBL; MN258251; QNQ18268.1; -; Viral_cRNA.
DR EMBL; MN258252; QNQ18269.1; -; Viral_cRNA.
DR EMBL; MN258253; QNQ18270.1; -; Viral_cRNA.
DR EMBL; MN258255; QNQ18272.1; -; Viral_cRNA.
DR EMBL; MN258256; QNQ18273.1; -; Viral_cRNA.
DR PDB; 2K48; NMR; -; A=1-74.
DR PDB; 5E04; X-ray; 2.25 A; A/B=117-399.
DR PDBsum; 2K48; -.
DR PDBsum; 5E04; -.
DR SMR; O36307; -.
DR EvolutionaryTrace; O36307; -.
DR Proteomes; UP000204348; Genome.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0044220; C:host cell perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-UniRule.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
DR InterPro; IPR002214; Hanta_nucleocap.
DR Pfam; PF00846; Hanta_nucleocap; 1.
DR PIRSF; PIRSF003949; N_HantaV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Coiled coil; Endonuclease; Host cytoplasm;
KW Host Golgi apparatus; Host-virus interaction; Hydrolase;
KW Inhibition of host innate immune response by virus;
KW Inhibition of host RLR pathway by virus; Nuclease; Phosphoprotein;
KW Ribonucleoprotein; RNA-binding; Viral immunoevasion; Viral nucleoprotein;
KW Virion.
FT CHAIN 1..428
FT /note="Nucleoprotein"
FT /id="PRO_0000455186"
FT REGION 1..175
FT /note="Viral panhandle binding"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
FT REGION 1..100
FT /note="Chaperone activity"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
FT REGION 1..79
FT /note="Homomultimerization"
FT /evidence="ECO:0000250|UniProtKB:Q88918"
FT REGION 1..50
FT /note="RdRP binding"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
FT REGION 80..248
FT /note="Interaction with glycoprotein N"
FT /evidence="ECO:0000250|UniProtKB:Q88918"
FT REGION 100..125
FT /note="Homomultimerization"
FT /evidence="ECO:0000305|PubMed:26559827"
FT REGION 150..175
FT /note="Interaction with host RPS19"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
FT REGION 175..217
FT /note="Viral RNA-binding"
FT /evidence="ECO:0000250|UniProtKB:P05133"
FT REGION 188..191
FT /note="Interaction with host UBE2I/UBC9"
FT /evidence="ECO:0000250|UniProtKB:P05133"
FT REGION 252..296
FT /note="Involved in the inhibition of IFN induction"
FT /evidence="ECO:0000269|PubMed:30867297"
FT REGION 372..428
FT /note="Interaction with host DAXX"
FT /evidence="ECO:0000250|UniProtKB:P27313"
FT REGION 372..420
FT /note="Homomultimerization"
FT /evidence="ECO:0000305|PubMed:26559827"
FT COILED 4..71
FT /evidence="ECO:0000269|PubMed:18687679"
FT MOTIF 178..181
FT /note="YxxL"
FT /evidence="ECO:0000250|UniProtKB:P05133"
FT SITE 88
FT /note="Important for the endonuclease activity"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
FT SITE 103
FT /note="Important for the endonuclease activity"
FT /evidence="ECO:0000250|UniProtKB:Q89462"
FT SITE 386
FT /note="Involved in the inhibition of IFN induction"
FT /evidence="ECO:0000269|PubMed:30867297"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:30867297"
FT VARIANT 46
FT /note="S -> N (in strain: CHI-7913)"
FT VARIANT 148
FT /note="T -> A (in strain: CHI-7913)"
FT MUTAGEN 102
FT /note="L->A: Loss of homotypic contacts."
FT /evidence="ECO:0000269|PubMed:26559827"
FT MUTAGEN 104
FT /note="V->A: Loss of homotypic contacts."
FT /evidence="ECO:0000269|PubMed:26559827"
FT MUTAGEN 107
FT /note="I->A: Loss of homotypic contacts."
FT /evidence="ECO:0000269|PubMed:26559827"
FT MUTAGEN 386
FT /note="S->H: Complete loss of inhibition of MDA5-directed
FT ISRE or IFN transcriptional responses."
FT /evidence="ECO:0000269|PubMed:30867297"
FT MUTAGEN 405
FT /note="L->A: Loss of homotypic contacts."
FT /evidence="ECO:0000269|PubMed:26559827"
FT MUTAGEN 408
FT /note="L->A: Loss of homotypic contacts."
FT /evidence="ECO:0000269|PubMed:26559827"
FT MUTAGEN 412
FT /note="L->A: Loss of homotypic contacts."
FT /evidence="ECO:0000269|PubMed:26559827"
SQ SEQUENCE 428 AA; 48042 MW; 6D44BE6D1F14990C CRC64;
MSTLQELQEN ITAHEQQLVT ARQKLKDAEK AVEVDPDDVN KSTLQSRRAA VSTLETKLGE
LKRQLADLVA AQKLATKPVD PTGLEPDDHL KEKSSLRYGN VLDVNSIDLE EPSGQTADWK
AIGAYILGFA IPIILKALYM LSTRGRQTVK DNKGTRIRFK DDSSFEEVNG IRKPKHLYVS
MPTAQSTMKA EEITPGRFRT IACGLFPAQV KARNIISPVM GVIGFGFFVK DWMDRIEEFL
AAECPFLPKP KVASEAFMST NKMYFLNRQR QVNESKVQDI IDLIDHAETE SATLFTEIAT
PHSVWVFACA PDRCPPTALY VAGVPELGAF FSILQDMRNT IMASKSVGTA EEKLKKKSAF
YQSYLRRTQS MGIQLDQKII ILYMLSWGKE AVNHFHLGDD MDPELRQLAQ SLIDTKVKEI
SNQEPLKL
