XIAP_MOUSE
ID XIAP_MOUSE Reviewed; 496 AA.
AC Q60989; A2BGY6; O08865;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=E3 ubiquitin-protein ligase XIAP;
DE EC=2.3.2.27;
DE AltName: Full=Baculoviral IAP repeat-containing protein 4;
DE AltName: Full=IAP homolog A;
DE AltName: Full=Inhibitor of apoptosis protein 3;
DE Short=IAP-3;
DE Short=mIAP-3;
DE Short=mIAP3;
DE AltName: Full=RING-type E3 ubiquitin transferase XIAP;
DE AltName: Full=X-linked inhibitor of apoptosis protein;
DE Short=X-linked IAP;
GN Name=Xiap; Synonyms=Aipa, Api3, Birc4, Miha;
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].
RC STRAIN=C57BL/6 X CBA; TISSUE=Liver;
RX PubMed=8643514; DOI=10.1073/pnas.93.10.4974;
RA Uren A.G., Pakusch M., Hawkins C.J., Puls K.L., Vaux D.L.;
RT "Cloning and expression of apoptosis inhibitory protein homologs that
RT function to inhibit apoptosis and/or bind tumor necrosis factor receptor-
RT associated factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:4974-4978(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Farahani R., Lefebvre C., Korneluk R.G., Mackenzie A.E.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP FUNCTION IN THE UBIQUITINATION OF MAP3K2/MEKK2, AND INTERACTION WITH
RP MAP3K2/MEKK2.
RX PubMed=18761086; DOI=10.1016/j.cellsig.2008.08.004;
RA Winsauer G., Resch U., Hofer-Warbinek R., Schichl Y.M., de Martin R.;
RT "XIAP regulates bi-phasic NF-kappaB induction involving physical
RT interaction and ubiquitination of MEKK2.";
RL Cell. Signal. 20:2107-2112(2008).
RN [7]
RP FUNCTION IN THE UBIQUITINATION OF PTEN, AND INTERACTION WITH PTEN.
RX PubMed=19473982; DOI=10.1074/jbc.c109.009522;
RA Van Themsche C., Leblanc V., Parent S., Asselin E.;
RT "X-linked inhibitor of apoptosis protein (XIAP) regulates PTEN
RT ubiquitination, content, and compartmentalization.";
RL J. Biol. Chem. 284:20462-20466(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Spleen;
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).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23788729; DOI=10.1126/science.1233029;
RA Fuchs Y., Brown S., Gorenc T., Rodriguez J., Fuchs E., Steller H.;
RT "Sept4/ARTS regulates stem cell apoptosis and skin regeneration.";
RL Science 341:286-289(2013).
RN [10]
RP FUNCTION, INTERACTION WITH SEPTIN4, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=30389919; DOI=10.1038/s41467-018-06941-4;
RA Koren E., Yosefzon Y., Ankawa R., Soteriou D., Jacob A., Nevelsky A.,
RA Ben-Yosef R., Bar-Sela G., Fuchs Y.;
RT "ARTS mediates apoptosis and regeneration of the intestinal stem cell
RT niche.";
RL Nat. Commun. 9:4582-4582(2018).
CC -!- FUNCTION: Multi-functional protein which regulates not only caspases
CC and apoptosis, but also modulates inflammatory signaling and immunity,
CC copper homeostasis, mitogenic kinase signaling, cell proliferation, as
CC well as cell invasion and metastasis. Acts as a direct caspase
CC inhibitor. Directly bind to the active site pocket of CASP3 and CASP7
CC and obstructs substrate entry. Inactivates CASP9 by keeping it in a
CC monomeric, inactive state. Inhibits apoptosis in intestinal crypt
CC cells, its activity it mitigated via its interaction with SEPTIN4
CC isoform ARTS (PubMed:30389919). Acts as an E3 ubiquitin-protein ligase
CC regulating NF-kappa-B signaling and the target proteins for its E3
CC ubiquitin-protein ligase activity include: RIPK1, CASP3, CASP7, CASP8,
CC CASP9, MAP3K2/MEKK2, DIABLO/SMAC, AIFM1, CCS and BIRC5/survivin.
CC Ubiquitinion of CCS leads to enhancement of its chaperone activity
CC toward its physiologic target, SOD1, rather than proteasomal
CC degradation. Ubiquitinion of MAP3K2/MEKK2 and AIFM1 does not lead to
CC proteasomal degradation. Plays a role in copper homeostasis by
CC ubiquitinating COMMD1 and promoting its proteasomal degradation. Can
CC also function as E3 ubiquitin-protein ligase of the NEDD8 conjugation
CC pathway, targeting effector caspases for neddylation and inactivation.
CC Ubiquitinates and therefore mediates the proteosomal degradation of
CC BCL2 in response to apoptosis (By similarity). Regulates the BMP
CC signaling pathway and the SMAD and MAP3K7/TAK1 dependent pathways
CC leading to NF-kappa-B and JNK activation. Acts as an important
CC regulator of innate immune signaling via regulation of Nodlike
CC receptors (NLRs). Protects cells from spontaneous formation of the
CC ripoptosome, a large multi-protein complex that has the capability to
CC kill cancer cells in a caspase-dependent and caspase-independent
CC manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and
CC CASP8. Acts as a positive regulator of Wnt signaling and ubiquitinates
CC TLE1, TLE2, TLE3, TLE4 and AES. Ubiquitination of TLE3 results in
CC inhibition of its interaction with TCF7L2/TCF4 thereby allowing
CC efficient recruitment and binding of the transcriptional coactivator
CC beta-catenin to TCF7L2/TCF4 that is required to initiate a Wnt-specific
CC transcriptional program. Positive regulator of dermal wound repair,
CC potentially via its interaction with SEPTIN4 (PubMed:23788729).
CC {ECO:0000250|UniProtKB:P98170, ECO:0000269|PubMed:18761086,
CC ECO:0000269|PubMed:19473982, ECO:0000269|PubMed:23788729,
CC ECO:0000269|PubMed:30389919}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- SUBUNIT: Monomer, and homodimer. Interacts (via BIR3 domain) with
CC DIABLO/SMAC; the interaction inhibits apoptotic suppressor activity (By
CC similarity). Interacts with HTRA2/PRSS25; the interaction inhibits
CC apoptotic suppressor activity. Interacts with TAB1/MAP3K7IP1 and AIFM1.
CC Interaction with DIABLO/SMAC hinders binding of TAB1/MAP3K7IP1 and
CC AIFM1. Interacts with TCF25 and COMMD1. Interacts (via BIR3 domain)
CC with SEPTIN4 (PubMed:30389919). Interacts with RIP1, RIP2, RIP3, RIP4,
CC CCS and USP19. Interacts (via BIR 2 domain and BIR 3 domain) with HAX1
CC (via C-terminus) and this interaction blocks ubiquitination of
CC XIAP/BIRC4. Interacts with the monomeric form of BIRC5/survivin (By
CC similarity). Interacts with TLE3 and TCF7L2/TCF4 (By similarity).
CC Interacts (via BIR 3 and RING domains) with PDCL3 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P98170,
CC ECO:0000269|PubMed:30389919}.
CC -!- INTERACTION:
CC Q60989; P53702: Hccs; NbExp=5; IntAct=EBI-517478, EBI-8579982;
CC Q60989; Q9JIY5: Htra2; NbExp=2; IntAct=EBI-517478, EBI-2365838;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=TLE3 promotes its nuclear localization. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in small intestine crypts (at protein
CC level) (PubMed:30389919). Expressed in bulge hair follicle stem cells,
CC sebaceous glands and dermal papillae (at protein level)
CC (PubMed:23788729). {ECO:0000269|PubMed:23788729,
CC ECO:0000269|PubMed:30389919}.
CC -!- DOMAIN: The first BIR domain is involved in interaction with
CC TAB1/MAP3K7IP1 and is important for dimerization. The second BIR domain
CC is sufficient to inhibit caspase-3 and caspase-7, while the third BIR
CC is involved in caspase-9 inhibition. The interactions with DIABLO/SMAC
CC and HTRA2/PRSS25 are mediated by the second and third BIR domains (By
CC similarity). {ECO:0000250}.
CC -!- PTM: S-Nitrosylation down-regulates its E3 ubiquitin-protein ligase
CC activity. {ECO:0000250|UniProtKB:P98170}.
CC -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:P98170}.
CC -!- DISRUPTION PHENOTYPE: In knockout mice decreased number of Paneth cells
CC in intestinal crypts, decreased proliferation and increased goblet
CC cells in the intestinal villi (PubMed:30389919). Increased weight loss
CC following intestinal wounding, increased inflammation, distorted tissue
CC architecture, muscle thickening and greater crypt loss
CC (PubMed:30389919). Delayed dermal wound repair (PubMed:23788729).
CC SEPTIN4 and XIAP double knockout mice show delayed dermal wound repair
CC and hair follicle regeneration, via increased apoptosis of hair
CC follicle stem cells (PubMed:23788729). {ECO:0000269|PubMed:23788729,
CC ECO:0000269|PubMed:30389919}.
CC -!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
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DR EMBL; U36842; AAC52594.1; -; mRNA.
DR EMBL; U88990; AAB58376.1; -; mRNA.
DR EMBL; BX530028; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466570; EDL29039.1; -; Genomic_DNA.
DR EMBL; CH466570; EDL29040.1; -; Genomic_DNA.
DR EMBL; BC138528; AAI38529.1; -; mRNA.
DR EMBL; BC145861; AAI45862.1; -; mRNA.
DR CCDS; CCDS30098.1; -.
DR RefSeq; NP_001288568.1; NM_001301639.1.
DR RefSeq; NP_001288570.1; NM_001301641.1.
DR RefSeq; NP_033818.2; NM_009688.3.
DR RefSeq; XP_006541488.1; XM_006541425.1.
DR RefSeq; XP_006541490.1; XM_006541427.1.
DR RefSeq; XP_011249279.1; XM_011250977.2.
DR RefSeq; XP_017173848.1; XM_017318359.1.
DR RefSeq; XP_017173849.1; XM_017318360.1.
DR RefSeq; XP_017173850.1; XM_017318361.1.
DR RefSeq; XP_017173851.1; XM_017318362.1.
DR AlphaFoldDB; Q60989; -.
DR SMR; Q60989; -.
DR BioGRID; 198149; 11.
DR DIP; DIP-33721N; -.
DR IntAct; Q60989; 8.
DR MINT; Q60989; -.
DR STRING; 10090.ENSMUSP00000110746; -.
DR MEROPS; I32.004; -.
DR iPTMnet; Q60989; -.
DR PhosphoSitePlus; Q60989; -.
DR EPD; Q60989; -.
DR MaxQB; Q60989; -.
DR PaxDb; Q60989; -.
DR PeptideAtlas; Q60989; -.
DR PRIDE; Q60989; -.
DR ProteomicsDB; 299705; -.
DR Antibodypedia; 3975; 739 antibodies from 44 providers.
DR DNASU; 11798; -.
DR Ensembl; ENSMUST00000026978; ENSMUSP00000026978; ENSMUSG00000025860.
DR Ensembl; ENSMUST00000055483; ENSMUSP00000061074; ENSMUSG00000025860.
DR Ensembl; ENSMUST00000115094; ENSMUSP00000110746; ENSMUSG00000025860.
DR Ensembl; ENSMUST00000115095; ENSMUSP00000110747; ENSMUSG00000025860.
DR GeneID; 11798; -.
DR KEGG; mmu:11798; -.
DR UCSC; uc009tas.2; mouse.
DR CTD; 331; -.
DR MGI; MGI:107572; Xiap.
DR VEuPathDB; HostDB:ENSMUSG00000025860; -.
DR eggNOG; KOG1101; Eukaryota.
DR GeneTree; ENSGT00940000158743; -.
DR HOGENOM; CLU_016347_1_1_1; -.
DR InParanoid; Q60989; -.
DR OMA; CMDENIA; -.
DR OrthoDB; 1340284at2759; -.
DR PhylomeDB; Q60989; -.
DR TreeFam; TF105356; -.
DR Reactome; R-MMU-111459; Activation of caspases through apoptosome-mediated cleavage.
DR Reactome; R-MMU-111463; SMAC (DIABLO) binds to IAPs.
DR Reactome; R-MMU-111464; SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes.
DR Reactome; R-MMU-111469; SMAC, XIAP-regulated apoptotic response.
DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-MMU-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-MMU-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-MMU-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-MMU-5675482; Regulation of necroptotic cell death.
DR Reactome; R-MMU-5676594; TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway.
DR Reactome; R-MMU-8948747; Regulation of PTEN localization.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-MMU-9627069; Regulation of the apoptosome activity.
DR BioGRID-ORCS; 11798; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Xiap; mouse.
DR PRO; PR:Q60989; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q60989; protein.
DR Bgee; ENSMUSG00000025860; Expressed in left lung lobe and 253 other tissues.
DR ExpressionAtlas; Q60989; baseline and differential.
DR Genevisible; Q60989; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0120283; F:protein serine/threonine kinase binding; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
DR GO; GO:1990001; P:inhibition of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI.
DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR GO; GO:1902530; P:positive regulation of protein linear polyubiquitination; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IBA:GO_Central.
DR GO; GO:0060785; P:regulation of apoptosis involved in tissue homeostasis; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00022; BIR; 3.
DR CDD; cd14395; UBA_BIRC4_8; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001370; BIR_rpt.
DR InterPro; IPR042579; XIAP/BIRC8_UBA.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00653; BIR; 3.
DR SMART; SM00238; BIR; 3.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS01282; BIR_REPEAT_1; 3.
DR PROSITE; PS50143; BIR_REPEAT_2; 3.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; S-nitrosylation; Transferase;
KW Ubl conjugation; Ubl conjugation pathway; Wnt signaling pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..496
FT /note="E3 ubiquitin-protein ligase XIAP"
FT /id="PRO_0000122353"
FT REPEAT 26..93
FT /note="BIR 1"
FT REPEAT 163..230
FT /note="BIR 2"
FT REPEAT 264..329
FT /note="BIR 3"
FT ZN_FING 449..484
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 141..149
FT /note="Interaction with caspase-7"
FT /evidence="ECO:0000250"
FT REGION 449..496
FT /note="Required for anti-apoptotic activity"
FT /evidence="ECO:0000269|PubMed:23788729"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00029"
FT MOD_RES 449
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P98170"
FT CROSSLNK 321
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P98170"
FT CROSSLNK 327
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P98170"
FT CONFLICT 208
FT /note="K -> E (in Ref. 1; AAC52594)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="E -> D (in Ref. 2; AAB58376)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="W -> C (in Ref. 2; AAB58376)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="S -> P (in Ref. 2; AAB58376)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="S -> P (in Ref. 2; AAB58376)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="I -> L (in Ref. 2; AAB58376)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="C -> S (in Ref. 2; AAB58376)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="V -> F (in Ref. 2; AAB58376)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="V -> A (in Ref. 2; AAB58376)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="K -> N (in Ref. 2; AAB58376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 496 AA; 56079 MW; EE5D242D3C3DF12E CRC64;
MTFNSFEGTR TFVLADTNKD EEFVEEFNRL KTFANFPSSS PVSASTLARA GFLYTGEGDT
VQCFSCHAAI DRWQYGDSAV GRHRRISPNC RFINGFYFEN GAAQSTNPGI QNGQYKSENC
VGNRNPFAPD RPPETHADYL LRTGQVVDIS DTIYPRNPAM CSEEARLKSF QNWPDYAHLT
PRELASAGLY YTGADDQVQC FCCGGKLKNW EPCDRAWSEH RRHFPNCFFV LGRNVNVRSE
SGVSSDRNFP NSTNSPRNPA MAEYEARIVT FGTWTSSVNK EQLARAGFYA LGEGDKVKCF
HCGGGLTDWK PSEDPWEQHA KWYPGCKYLL DEKGQEYINN IHLTHSLEES LGRTAEKTPS
LTKKIDDTIF QNPMVQEAIR MGFSFKDIKK TMEEKIQTSG SSYLSLEVLI ADLVSAQKDN
TEDESSQTSL QKDISTEEQL RRLQEEKLCK ICMDRNIAIV FVPCGHLVTC KQCAEAVDKC
PMCYTVITFK QKIFMS
