BIRC1_HUMAN
ID BIRC1_HUMAN Reviewed; 1403 AA.
AC Q13075; B9EG72; E9PHD1; O75857; Q13730; Q59GI6; Q8TDZ4; Q99796;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Baculoviral IAP repeat-containing protein 1;
DE AltName: Full=Neuronal apoptosis inhibitory protein;
GN Name=NAIP; Synonyms=BIRC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MET-535, AND POSSIBLE ROLE
RP IN THE PROTECTION FROM SPINAL MUSCULAR ATROPHY.
RC TISSUE=Fetal brain;
RX PubMed=7813013; DOI=10.1016/0092-8674(95)90461-1;
RA Roy N., Mahadevan M.S., McLean M., Shutler G., Yaraghi Z., Farahini R.,
RA Baird S., Besner-Johnston A., Lefebvre C., Kang X., Salih M., Aubry H.,
RA Tamai K., Guan X., Ioannou P., Crawford T.O., de Jong P.J., Surh L.,
RA Ikeda J., Korneluk R.G., Mackenzie A.;
RT "The gene for neuronal apoptosis inhibitory protein is partially deleted in
RT individuals with spinal muscular atrophy.";
RL Cell 80:167-178(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION, AND VARIANT MET-535.
RC TISSUE=Brain;
RX PubMed=9503025; DOI=10.1006/geno.1997.5141;
RA Chen Q., Baird S.D., Mahadevan M., Besner-Johnston A., Farahani R.,
RA Xuan J.-Y., Kang X., Lefebvre C., Ikeda J.-E., Korneluk R.G.,
RA MacKenzie A.E.;
RT "Sequence of a 131-kb region of 5q13.1 containing the spinal muscular
RT atrophy candidate genes SMN and NAIP.";
RL Genomics 48:121-127(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-535.
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-535.
RC TISSUE=Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1160 (ISOFORM 2), AND VARIANT MET-535.
RX PubMed=11955612; DOI=10.1016/s0167-4781(01)00343-8;
RA Xu M., Okada T., Sakai H., Miyamoto N., Yanagisawa Y., MacKenzie A.E.,
RA Hadano S., Ikeda J.-E.;
RT "Functional human NAIP promoter transcription regulatory elements for the
RT NAIP and PsiNAIP genes.";
RL Biochim. Biophys. Acta 1574:35-50(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 386-623 (ISOFORM 1/2).
RC TISSUE=Pre-B cell;
RX PubMed=7552146; DOI=10.1159/000472281;
RA van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J.,
RA Anzevino R., Velona I., Den Dunnen J.T., Scheffer H., Brahe C.,
RA van Ommen G.J.B., Buys C.H.C.M.;
RT "A provisional transcript map of the spinal muscular atrophy (SMA) critical
RT region.";
RL Eur. J. Hum. Genet. 3:87-95(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 567-1403 (ISOFORM 1/2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION.
RC TISSUE=Liver;
RX PubMed=8552191; DOI=10.1038/379349a0;
RA Liston P., Roy N., Tamai K., Lefebvre C., Baird S., Cherton-Horvat G.,
RA Farahani R., McLean M., Ikeda J., Mackenzie A., Korneluk R.G.;
RT "Suppression of apoptosis in mammalian cells by NAIP and a related family
RT of IAP genes.";
RL Nature 379:349-353(1996).
RN [9]
RP FUNCTION.
RX PubMed=11896143; DOI=10.1523/jneurosci.22-06-02035.2002;
RA Maier J.K., Lahoua Z., Gendron N.H., Fetni R., Johnston A., Davoodi J.,
RA Rasper D., Roy S., Slack R.S., Nicholson D.W., MacKenzie A.E.;
RT "The neuronal apoptosis inhibitory protein is a direct inhibitor of
RT caspases 3 and 7.";
RL J. Neurosci. 22:2035-2043(2002).
RN [10]
RP REVIEW ON FUNCTION.
RX PubMed=18414036; DOI=10.4161/cc.7.8.5783;
RA Dubrez-Daloz L., Dupoux A., Cartier J.;
RT "IAPs: more than just inhibitors of apoptosis proteins.";
RL Cell Cycle 7:1036-1046(2008).
RN [11]
RP FUNCTION, INTERACTION WITH APAF1, DOMAIN BIR3 AND NACHT, AND MUTAGENESIS OF
RP LYS-476.
RX PubMed=21371431; DOI=10.1016/j.bbrc.2011.02.130;
RA Karimpour S., Davoodi J., Ghahremani M.H.;
RT "Integrity of ATP binding site is essential for effective inhibition of the
RT intrinsic apoptosis pathway by NAIP.";
RL Biochem. Biophys. Res. Commun. 407:158-162(2011).
RN [12]
RP FUNCTION IN INFLAMMASOME, AND INTERACTION WITH C.VIOLACEUM CPRI.
RX PubMed=21918512; DOI=10.1038/nature10510;
RA Zhao Y., Yang J., Shi J., Gong Y.N., Lu Q., Xu H., Liu L., Shao F.;
RT "The NLRC4 inflammasome receptors for bacterial flagellin and type III
RT secretion apparatus.";
RL Nature 477:596-600(2011).
RN [13]
RP FUNCTION IN INFLAMMASOME.
RX PubMed=22504023; DOI=10.1016/j.micinf.2012.03.006;
RA Katagiri N., Shobuike T., Chang B., Kukita A., Miyamoto H.;
RT "The human apoptosis inhibitor NAIP induces pyroptosis in macrophages
RT infected with Legionella pneumophila.";
RL Microbes Infect. 14:1123-1132(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 141-244 IN COMPLEX WITH ZINC IONS.
RX PubMed=19923725; DOI=10.1107/s1744309109038597;
RA Herman M.D., Moche M., Flodin S., Welin M., Tresaugues L., Johansson I.,
RA Nilsson M., Nordlund P., Nyman T.;
RT "Structures of BIR domains from human NAIP and cIAP2.";
RL Acta Crystallogr. F 65:1091-1096(2009).
CC -!- FUNCTION: Anti-apoptotic protein which acts by inhibiting the
CC activities of CASP3, CASP7 and CASP9. Can inhibit the autocleavage of
CC pro-CASP9 and cleavage of pro-CASP3 by CASP9. Capable of inhibiting
CC CASP9 autoproteolysis at 'Asp-315' and decreasing the rate of auto
CC proteolysis at 'Asp-330'. Acts as a mediator of neuronal survival in
CC pathological conditions. Prevents motor-neuron apoptosis induced by a
CC variety of signals. Possible role in the prevention of spinal muscular
CC atrophy that seems to be caused by inappropriate persistence of motor-
CC neuron apoptosis: mutated or deleted forms of NAIP have been found in
CC individuals with severe spinal muscular atrophy.
CC -!- FUNCTION: Acts as a sensor component of the NLRC4 inflammasome that
CC specifically recognizes and binds needle protein CprI from pathogenic
CC bacteria C.violaceum. Association of pathogenic bacteria proteins
CC drives in turn drive assembly and activation of the NLRC4 inflammasome,
CC promoting caspase-1 activation, cytokine production and macrophage
CC pyroptosis. The NLRC4 inflammasome is activated as part of the innate
CC immune response to a range of intracellular bacteria such as
CC C.violaceum and L.pneumophila.
CC -!- SUBUNIT: Interacts (via NACHT domain) with APAF1 (via CARD and NACHT
CC domains). Interacts with C.violaceum needle protein CprI.
CC {ECO:0000269|PubMed:19923725, ECO:0000269|PubMed:21371431,
CC ECO:0000269|PubMed:21918512}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13075-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13075-2; Sequence=VSP_047196, VSP_047197;
CC -!- TISSUE SPECIFICITY: Expressed in motor neurons, but not in sensory
CC neurons. Found in liver and placenta, and to a lesser extent in spinal
CC cord.
CC -!- DOMAIN: Both the BIR and NACHT domains are essential for effective
CC inhibition of pro-CASP9 cleavage. BIR3 domain binds to procaspase-9 and
CC the NACHT domain interacts with the NACHT domain of APAF1 forming a
CC bridge between pro-CASP9 and APAF1. {ECO:0000269|PubMed:21371431}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC62261.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U19251; AAC52045.1; -; mRNA.
DR EMBL; U80017; AAC52047.1; -; Genomic_DNA.
DR EMBL; AC005031; AAC62261.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC044797; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136273; AAI36274.1; -; mRNA.
DR EMBL; AB048534; BAB87181.1; -; mRNA.
DR EMBL; AH003063; AAA64504.1; -; mRNA.
DR EMBL; AB209123; BAD92360.1; -; mRNA.
DR CCDS; CCDS4009.1; -. [Q13075-1]
DR CCDS; CCDS43327.1; -. [Q13075-2]
DR RefSeq; NP_001333799.1; NM_001346870.1. [Q13075-1]
DR RefSeq; NP_004527.2; NM_004536.2. [Q13075-1]
DR RefSeq; NP_075043.1; NM_022892.1. [Q13075-2]
DR PDB; 2VM5; X-ray; 1.80 A; A=141-244.
DR PDBsum; 2VM5; -.
DR AlphaFoldDB; Q13075; -.
DR SMR; Q13075; -.
DR BioGRID; 110752; 10.
DR ComplexPortal; CPX-4144; NLRC4 inflammasome.
DR CORUM; Q13075; -.
DR DIP; DIP-59150N; -.
DR IntAct; Q13075; 5.
DR MINT; Q13075; -.
DR STRING; 9606.ENSP00000428657; -.
DR MEROPS; I32.001; -.
DR iPTMnet; Q13075; -.
DR PhosphoSitePlus; Q13075; -.
DR BioMuta; NAIP; -.
DR DMDM; 109940027; -.
DR jPOST; Q13075; -.
DR MassIVE; Q13075; -.
DR PaxDb; Q13075; -.
DR PeptideAtlas; Q13075; -.
DR PRIDE; Q13075; -.
DR ProteomicsDB; 20510; -.
DR ProteomicsDB; 59135; -. [Q13075-1]
DR ProteomicsDB; 74380; -.
DR Antibodypedia; 47753; 208 antibodies from 33 providers.
DR DNASU; 4671; -.
DR Ensembl; ENST00000194097.8; ENSP00000443944.1; ENSG00000249437.8. [Q13075-1]
DR Ensembl; ENST00000503719.6; ENSP00000424913.2; ENSG00000249437.8. [Q13075-2]
DR Ensembl; ENST00000517649.6; ENSP00000428657.2; ENSG00000249437.8. [Q13075-1]
DR Ensembl; ENST00000523981.5; ENSP00000428363.1; ENSG00000249437.8. [Q13075-2]
DR Ensembl; ENST00000612328.4; ENSP00000484107.1; ENSG00000278613.4.
DR Ensembl; ENST00000620988.4; ENSP00000484731.1; ENSG00000278613.4.
DR GeneID; 4671; -.
DR KEGG; hsa:4671; -.
DR MANE-Select; ENST00000517649.6; ENSP00000428657.2; NM_004536.3; NP_004527.2.
DR UCSC; uc003kar.2; human. [Q13075-1]
DR CTD; 4671; -.
DR DisGeNET; 4671; -.
DR GeneCards; NAIP; -.
DR HGNC; HGNC:7634; NAIP.
DR HPA; ENSG00000249437; Tissue enriched (lymphoid).
DR MalaCards; NAIP; -.
DR MIM; 600355; gene.
DR neXtProt; NX_Q13075; -.
DR OpenTargets; ENSG00000249437; -.
DR Orphanet; 83330; Proximal spinal muscular atrophy type 1.
DR Orphanet; 83418; Proximal spinal muscular atrophy type 2.
DR Orphanet; 83419; Proximal spinal muscular atrophy type 3.
DR PharmGKB; PA162396805; -.
DR VEuPathDB; HostDB:ENSG00000249437; -.
DR eggNOG; KOG1101; Eukaryota.
DR GeneTree; ENSGT00940000163559; -.
DR InParanoid; Q13075; -.
DR OMA; FENWPFY; -.
DR OrthoDB; 268914at2759; -.
DR PhylomeDB; Q13075; -.
DR TreeFam; TF105356; -.
DR PathwayCommons; Q13075; -.
DR SignaLink; Q13075; -.
DR SIGNOR; Q13075; -.
DR BioGRID-ORCS; 4671; 42 hits in 1074 CRISPR screens.
DR ChiTaRS; NAIP; human.
DR EvolutionaryTrace; Q13075; -.
DR GeneWiki; NAIP_(gene); -.
DR GenomeRNAi; 4671; -.
DR Pharos; Q13075; Tbio.
DR PRO; PR:Q13075; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q13075; protein.
DR Bgee; ENSG00000249437; Expressed in monocyte and 146 other tissues.
DR ExpressionAtlas; Q13075; baseline and differential.
DR Genevisible; Q13075; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0061702; C:inflammasome complex; IC:ComplexPortal.
DR GO; GO:0072557; C:IPAF inflammasome complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IMP:UniProtKB.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0120283; F:protein serine/threonine kinase binding; IPI:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IBA:GO_Central.
DR GO; GO:0016045; P:detection of bacterium; IBA:GO_Central.
DR GO; GO:0046456; P:icosanoid biosynthetic process; IC:ComplexPortal.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; TAS:UniProtKB.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IC:ComplexPortal.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IC:ComplexPortal.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IC:ComplexPortal.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:UniProtKB.
DR GO; GO:0070269; P:pyroptosis; IBA:GO_Central.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0032268; P:regulation of cellular protein metabolic process; IEA:UniProt.
DR CDD; cd00022; BIR; 3.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR001370; BIR_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR028789; Naip.
DR InterPro; IPR040535; NLRC4_HD.
DR InterPro; IPR041075; NOD2_WH.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR46914; PTHR46914; 1.
DR Pfam; PF00653; BIR; 3.
DR Pfam; PF05729; NACHT; 1.
DR Pfam; PF17889; NLRC4_HD; 1.
DR Pfam; PF17779; NOD2_WH; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00238; BIR; 3.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS01282; BIR_REPEAT_1; 3.
DR PROSITE; PS50143; BIR_REPEAT_2; 3.
DR PROSITE; PS50837; NACHT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; ATP-binding; Immunity;
KW Inflammatory response; Innate immunity; Metal-binding; Nucleotide-binding;
KW Protease inhibitor; Reference proteome; Repeat; Thiol protease inhibitor;
KW Zinc.
FT CHAIN 1..1403
FT /note="Baculoviral IAP repeat-containing protein 1"
FT /id="PRO_0000122341"
FT REPEAT 60..127
FT /note="BIR 1"
FT REPEAT 159..227
FT /note="BIR 2"
FT REPEAT 278..345
FT /note="BIR 3"
FT DOMAIN 464..758
FT /note="NACHT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00136"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 342
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 473..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q3UP24"
FT VAR_SEQ 1..61
FT /note="MATQQKASDERISQFDHNLLPELSALLGLDAVQLAKELEEEEQKERAKMQKG
FT YNSQMRSEA -> MPLHIGDFVWDSKVHSLQSSLNIFSLLPTKGRTEHLFFSHILSFHW
FT PAFSSIRLELWINLR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11955612"
FT /id="VSP_047196"
FT VAR_SEQ 62..223
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11955612"
FT /id="VSP_047197"
FT VARIANT 535
FT /note="V -> M (in dbSNP:rs1423904967)"
FT /evidence="ECO:0000269|PubMed:11955612,
FT ECO:0000269|PubMed:15372022, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:7813013, ECO:0000269|PubMed:9503025"
FT /id="VAR_026477"
FT MUTAGEN 476
FT /note="K->T: Prevents the proper cleavage of pro-CASP9, but
FT does not inhibit the cleavage of pro-CASP3 by CASP9."
FT /evidence="ECO:0000269|PubMed:21371431"
FT CONFLICT 386..387
FT /note="VP -> ST (in Ref. 6; AAA64504)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="Y -> H (in Ref. 6; AAA64504)"
FT /evidence="ECO:0000305"
FT CONFLICT 567..568
FT /note="IQ -> FK (in Ref. 7; BAD92360)"
FT /evidence="ECO:0000305"
FT CONFLICT 919
FT /note="P -> S (in Ref. 7; BAD92360)"
FT /evidence="ECO:0000305"
FT CONFLICT 1066
FT /note="S -> T (in Ref. 7; BAD92360)"
FT /evidence="ECO:0000305"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:2VM5"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:2VM5"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:2VM5"
FT HELIX 178..183
FT /evidence="ECO:0007829|PDB:2VM5"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:2VM5"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:2VM5"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:2VM5"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:2VM5"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:2VM5"
FT HELIX 225..231
FT /evidence="ECO:0007829|PDB:2VM5"
SQ SEQUENCE 1403 AA; 159582 MW; C1CE163D55900C6D CRC64;
MATQQKASDE RISQFDHNLL PELSALLGLD AVQLAKELEE EEQKERAKMQ KGYNSQMRSE
AKRLKTFVTY EPYSSWIPQE MAAAGFYFTG VKSGIQCFCC SLILFGAGLT RLPIEDHKRF
HPDCGFLLNK DVGNIAKYDI RVKNLKSRLR GGKMRYQEEE ARLASFRNWP FYVQGISPCV
LSEAGFVFTG KQDTVQCFSC GGCLGNWEEG DDPWKEHAKW FPKCEFLRSK KSSEEITQYI
QSYKGFVDIT GEHFVNSWVQ RELPMASAYC NDSIFAYEEL RLDSFKDWPR ESAVGVAALA
KAGLFYTGIK DIVQCFSCGG CLEKWQEGDD PLDDHTRCFP NCPFLQNMKS SAEVTPDLQS
RGELCELLET TSESNLEDSI AVGPIVPEMA QGEAQWFQEA KNLNEQLRAA YTSASFRHMS
LLDISSDLAT DHLLGCDLSI ASKHISKPVQ EPLVLPEVFG NLNSVMCVEG EAGSGKTVLL
KKIAFLWASG CCPLLNRFQL VFYLSLSSTR PDEGLASIIC DQLLEKEGSV TEMCVRNIIQ
QLKNQVLFLL DDYKEICSIP QVIGKLIQKN HLSRTCLLIA VRTNRARDIR RYLETILEIK
AFPFYNTVCI LRKLFSHNMT RLRKFMVYFG KNQSLQKIQK TPLFVAAICA HWFQYPFDPS
FDDVAVFKSY MERLSLRNKA TAEILKATVS SCGELALKGF FSCCFEFNDD DLAEAGVDED
EDLTMCLMSK FTAQRLRPFY RFLSPAFQEF LAGMRLIELL DSDRQEHQDL GLYHLKQINS
PMMTVSAYNN FLNYVSSLPS TKAGPKIVSH LLHLVDNKES LENISENDDY LKHQPEISLQ
MQLLRGLWQI CPQAYFSMVS EHLLVLALKT AYQSNTVAAC SPFVLQFLQG RTLTLGALNL
QYFFDHPESL SLLRSIHFPI RGNKTSPRAH FSVLETCFDK SQVPTIDQDY ASAFEPMNEW
ERNLAEKEDN VKSYMDMQRR ASPDLSTGYW KLSPKQYKIP CLEVDVNDID VVGQDMLEIL
MTVFSASQRI ELHLNHSRGF IESIRPALEL SKASVTKCSI SKLELSAAEQ ELLLTLPSLE
SLEVSGTIQS QDQIFPNLDK FLCLKELSVD LEGNINVFSV IPEEFPNFHH MEKLLIQISA
EYDPSKLVKL IQNSPNLHVF HLKCNFFSDF GSLMTMLVSC KKLTEIKFSD SFFQAVPFVA
SLPNFISLKI LNLEGQQFPD EETSEKFAYI LGSLSNLEEL ILPTGDGIYR VAKLIIQQCQ
QLHCLRVLSF FKTLNDDSVV EIAKVAISGG FQKLENLKLS INHKITEEGY RNFFQALDNM
PNLQELDISR HFTECIKAQA TTVKSLSQCV LRLPRLIRLN MLSWLLDADD IALLNVMKER
HPQSKYLTIL QKWILPFSPI IQK
