SARM1_CAEEL
ID SARM1_CAEEL Reviewed; 981 AA.
AC Q86DA5; O17801; O17802; Q19373; Q7JMF4; Q7JMF5;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-OCT-2020, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=NAD(+) hydrolase tir-1 {ECO:0000305};
DE Short=NADase tir-1 {ECO:0000305};
DE EC=3.2.2.6 {ECO:0000269|PubMed:31439792};
DE AltName: Full=Neuronal symmetry protein 2;
DE AltName: Full=SARM1 homolog;
DE AltName: Full=Sterile alpha and TIR motif-containing protein tir-1 {ECO:0000303|PubMed:15048112};
GN Name=tir-1 {ECO:0000303|PubMed:15048112, ECO:0000312|WormBase:F13B10.1c};
GN Synonyms=nsy-2 {ECO:0000312|WormBase:F13B10.1c};
GN ORFNames=F13B10.1 {ECO:0000312|WormBase:F13B10.1c};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, HOMODIMERIZATION, AND INTERACTION WITH RAB-1
RP AND PAL-1.
RX PubMed=15048112; DOI=10.1038/ni1060;
RA Couillault C., Pujol N., Reboul J., Sabatier L., Guichou J.-F., Kohara Y.,
RA Ewbank J.J.;
RT "TLR-independent control of innate immunity in Caenorhabditis elegans by
RT the TIR domain adaptor protein TIR-1, an ortholog of human SARM.";
RL Nat. Immunol. 5:488-494(2004).
RN [3]
RP FUNCTION.
RX PubMed=15123841; DOI=10.1073/pnas.0308625101;
RA Liberati N.T., Fitzgerald K.A., Kim D.H., Feinbaum R., Golenbock D.T.,
RA Ausubel F.M.;
RT "Requirement for a conserved Toll/interleukin-1 resistance domain protein
RT in the Caenorhabditis elegans immune response.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:6593-6598(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH
RP UNC-43.
RX PubMed=15625192; DOI=10.1101/gad.1276505;
RA Chuang C.-F., Bargmann C.I.;
RT "A Toll-interleukin 1 repeat protein at the synapse specifies asymmetric
RT odorant receptor expression via ASK1 MAPKKK signaling.";
RL Genes Dev. 19:270-281(2005).
RN [5]
RP REVIEW.
RX PubMed=18089857; DOI=10.1126/stke.4172007pe73;
RA Dalod M.;
RT "Studies of SARM1 uncover similarities between immune and neuronal
RT responses to danger.";
RL Sci. STKE 2007:PE73-PE73(2007).
RN [6]
RP FUNCTION.
RX PubMed=18394898; DOI=10.1016/j.cub.2008.02.079;
RA Pujol N., Cypowyj S., Ziegler K., Millet A., Astrain A., Goncharov A.,
RA Jin Y., Chisholm A.D., Ewbank J.J.;
RT "Distinct innate immune responses to infection and wounding in the C.
RT elegans epidermis.";
RL Curr. Biol. 18:481-489(2008).
RN [7]
RP FUNCTION.
RX PubMed=21212236; DOI=10.1534/genetics.110.124883;
RA Hayakawa T., Kato K., Hayakawa R., Hisamoto N., Matsumoto K., Takeda K.,
RA Ichijo H.;
RT "Regulation of anoxic death in Caenorhabditis elegans by mammalian
RT apoptosis signal-regulating kinase (ASK) family proteins.";
RL Genetics 187:785-792(2011).
RN [8]
RP FUNCTION.
RX PubMed=22363008; DOI=10.1126/science.1215156;
RA Blum E.S., Abraham M.C., Yoshimura S., Lu Y., Shaham S.;
RT "Control of nonapoptotic developmental cell death in Caenorhabditis elegans
RT by a polyglutamine-repeat protein.";
RL Science 335:970-973(2012).
RN [9]
RP FUNCTION.
RX PubMed=23505381; DOI=10.1371/journal.pgen.1003324;
RA Xie Y., Moussaif M., Choi S., Xu L., Sze J.Y.;
RT "RFX transcription factor DAF-19 regulates 5-HT and innate immune responses
RT to pathogenic bacteria in Caenorhabditis elegans.";
RL PLoS Genet. 9:e1003324-e1003324(2013).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25204677; DOI=10.1186/s12915-014-0064-6;
RA Crook-McMahon H.M., Olahova M., Button E.L., Winter J.J., Veal E.A.;
RT "Genome-wide screening identifies new genes required for stress-induced
RT phase 2 detoxification gene expression in animals.";
RL BMC Biol. 12:64-64(2014).
RN [11]
RP FUNCTION, AND SUBUNIT.
RX PubMed=27671644; DOI=10.1073/pnas.1601506113;
RA Summers D.W., Gibson D.A., DiAntonio A., Milbrandt J.;
RT "SARM1-specific motifs in the TIR domain enable NAD+ loss and regulate
RT injury-induced SARM1 activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E6271-E6280(2016).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31439792; DOI=10.1126/science.aax1911;
RA Horsefield S., Burdett H., Zhang X., Manik M.K., Shi Y., Chen J., Qi T.,
RA Gilley J., Lai J.S., Rank M.X., Casey L.W., Gu W., Ericsson D.J., Foley G.,
RA Hughes R.O., Bosanac T., von Itzstein M., Rathjen J.P., Nanson J.D.,
RA Boden M., Dry I.B., Williams S.J., Staskawicz B.J., Coleman M.P., Ve T.,
RA Dodds P.N., Kobe B.;
RT "NAD+ cleavage activity by animal and plant TIR domains in cell death
RT pathways.";
RL Science 365:793-799(2019).
CC -!- FUNCTION: NAD(+) hydrolase, which plays a key role in non-apoptotic
CC cell death by regulating NAD(+) metabolism (PubMed:27671644). In
CC response to stress, homooligomerizes and catalyzes cleavage of NAD(+)
CC into ADP-D-ribose (ADPR) and nicotinamide; NAD(+) cleavage promoting
CC non-apoptotic neuronal cell death (PubMed:31439792). In males, involved
CC in non-apoptotic death of the linker cell which guides gonad elongation
CC during larval development (PubMed:22363008). Required for both innate
CC immune response and specification of AWC(OFF) neuron (PubMed:15048112,
CC PubMed:15123841, PubMed:15625192). During late embryogenesis, it acts
CC downstream of CAMKII (unc-43) to regulate specification of asymmetric
CC odorant receptors in AWC(OFF) neuron via the nsy-1/ASK1 pmk-1/p38 MAP
CC kinase signaling cascade. Required to localize nsy-1 to postsynaptic
CC regions of AWC neuron, suggesting that it may act by assembling a
CC signaling complex that regulate odorant receptor expression
CC (PubMed:15625192). Also plays a central role in resistance to infection
CC to a broad range of bacterial and fungi pathogens, possibly by
CC activating pmk-1, independently of the NF-kappa-B pathway. Required for
CC expression of antimicrobial peptides nlp-29 and nlp-31
CC (PubMed:15048112, PubMed:15123841). Its role in immune response and
CC neuron specification may be mediated by the same nsy-1/ASK1 pmk-1/p38
CC MAP kinase cascade signaling pathway (PubMed:15048112, PubMed:15123841,
CC PubMed:15625192). Involved in the response to anoxic conditions
CC probably by activating the p38 pathway composed of nsy-1/sek-1/pmk-1
CC (PubMed:21212236). Involved in regulation of the serotonergic response
CC of ADF neurons to pathogenic food (PubMed:23505381). In addition, plays
CC a role in the up-regulation of gcs-1 upon arsenite treatment, most
CC likely through activation of pmk-1, to confer protection against
CC toxicity induced by heavy metals (PubMed:25204677).
CC {ECO:0000269|PubMed:15048112, ECO:0000269|PubMed:15123841,
CC ECO:0000269|PubMed:15625192, ECO:0000269|PubMed:21212236,
CC ECO:0000269|PubMed:22363008, ECO:0000269|PubMed:23505381,
CC ECO:0000269|PubMed:25204677, ECO:0000269|PubMed:27671644,
CC ECO:0000269|PubMed:31439792}.
CC -!- FUNCTION: [Isoform b]: Regulates expression of antimicrobial peptide
CC nlp-29 in response to fungal infection or physical injury.
CC {ECO:0000269|PubMed:18394898}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000269|PubMed:31439792};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000269|PubMed:31439792};
CC -!- SUBUNIT: Homodimer (PubMed:15048112, PubMed:27671644). Interacts with
CC rab-1, pal-1 and unc-43 (PubMed:15048112, PubMed:15625192).
CC {ECO:0000269|PubMed:15048112, ECO:0000269|PubMed:15625192,
CC ECO:0000269|PubMed:27671644}.
CC -!- INTERACTION:
CC Q86DA5; Q86DA5: tir-1; NbExp=3; IntAct=EBI-319472, EBI-319472;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15625192}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=c {ECO:0000312|WormBase:F13B10.1c};
CC IsoId=Q86DA5-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F13B10.1a};
CC IsoId=Q86DA5-2; Sequence=VSP_060730, VSP_060731;
CC Name=b {ECO:0000312|WormBase:F13B10.1b};
CC IsoId=Q86DA5-3; Sequence=VSP_060732;
CC Name=d {ECO:0000312|WormBase:F13B10.1d};
CC IsoId=Q86DA5-4; Sequence=VSP_013613;
CC Name=e {ECO:0000312|WormBase:F13B10.1e};
CC IsoId=Q86DA5-5; Sequence=VSP_060733, VSP_060731;
CC -!- TISSUE SPECIFICITY: Highly expressed in hypodermis. Localizes to
CC postsynaptic regions of axons. {ECO:0000269|PubMed:15048112,
CC ECO:0000269|PubMed:15625192}.
CC -!- DOMAIN: The SAM domains mediate the localization to postsynaptic
CC regions of neurons. {ECO:0000269|PubMed:15625192}.
CC -!- DOMAIN: The TIR domain mediates NAD(+) hydrolase (NADase) activity.
CC Self-association of TIR domains is required for NADase activity.
CC {ECO:0000250|UniProtKB:Q6SZW1}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in reduced
CC survival and reduced pmk-1 phosphorylation in response to the heavy
CC metal arsenite. {ECO:0000269|PubMed:25204677}.
CC -!- SIMILARITY: Belongs to the SARM1 family. {ECO:0000305}.
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DR EMBL; BX284603; CAA90181.1; -; Genomic_DNA.
DR EMBL; BX284603; CAA90182.1; -; Genomic_DNA.
DR EMBL; BX284603; CAD90174.1; -; Genomic_DNA.
DR EMBL; BX284603; CAE47466.1; -; Genomic_DNA.
DR EMBL; BX284603; CAE47467.1; -; Genomic_DNA.
DR PIR; T20816; T20816.
DR PIR; T20817; T20817.
DR RefSeq; NP_001021251.2; NM_001026080.3. [Q86DA5-1]
DR RefSeq; NP_001021252.1; NM_001026081.2.
DR RefSeq; NP_001021253.1; NM_001026082.2.
DR RefSeq; NP_497784.1; NM_065383.1. [Q86DA5-2]
DR RefSeq; NP_497785.1; NM_065384.4. [Q86DA5-3]
DR AlphaFoldDB; Q86DA5; -.
DR SMR; Q86DA5; -.
DR BioGRID; 40740; 26.
DR DIP; DIP-26569N; -.
DR IntAct; Q86DA5; 18.
DR STRING; 6239.F13B10.1c; -.
DR iPTMnet; Q86DA5; -.
DR EPD; Q86DA5; -.
DR PaxDb; Q86DA5; -.
DR PeptideAtlas; Q86DA5; -.
DR PRIDE; Q86DA5; -.
DR EnsemblMetazoa; F13B10.1a.1; F13B10.1a.1; WBGene00006575. [Q86DA5-2]
DR EnsemblMetazoa; F13B10.1a.2; F13B10.1a.2; WBGene00006575. [Q86DA5-2]
DR EnsemblMetazoa; F13B10.1b.1; F13B10.1b.1; WBGene00006575. [Q86DA5-3]
DR EnsemblMetazoa; F13B10.1c.1; F13B10.1c.1; WBGene00006575. [Q86DA5-1]
DR EnsemblMetazoa; F13B10.1d.1; F13B10.1d.1; WBGene00006575. [Q86DA5-4]
DR EnsemblMetazoa; F13B10.1d.2; F13B10.1d.2; WBGene00006575. [Q86DA5-4]
DR EnsemblMetazoa; F13B10.1d.3; F13B10.1d.3; WBGene00006575. [Q86DA5-4]
DR EnsemblMetazoa; F13B10.1e.1; F13B10.1e.1; WBGene00006575. [Q86DA5-5]
DR EnsemblMetazoa; F13B10.1e.2; F13B10.1e.2; WBGene00006575. [Q86DA5-5]
DR EnsemblMetazoa; F13B10.1e.3; F13B10.1e.3; WBGene00006575. [Q86DA5-5]
DR GeneID; 175502; -.
DR UCSC; F13B10.1e.2; c. elegans. [Q86DA5-1]
DR CTD; 175502; -.
DR WormBase; F13B10.1a; CE20681; WBGene00006575; tir-1. [Q86DA5-2]
DR WormBase; F13B10.1b; CE15818; WBGene00006575; tir-1. [Q86DA5-3]
DR WormBase; F13B10.1c; CE50801; WBGene00006575; tir-1. [Q86DA5-1]
DR WormBase; F13B10.1d; CE35712; WBGene00006575; tir-1. [Q86DA5-4]
DR WormBase; F13B10.1e; CE35713; WBGene00006575; tir-1. [Q86DA5-5]
DR eggNOG; KOG3678; Eukaryota.
DR GeneTree; ENSGT00390000004155; -.
DR InParanoid; Q86DA5; -.
DR PhylomeDB; Q86DA5; -.
DR SignaLink; Q86DA5; -.
DR PRO; PR:Q86DA5; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006575; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q86DA5; baseline and differential.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:1904115; C:axon cytoplasm; IDA:WormBase.
DR GO; GO:0044297; C:cell body; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0003953; F:NAD+ nucleosidase activity; IDA:UniProtKB.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0019901; F:protein kinase binding; IPI:WormBase.
DR GO; GO:0035591; F:signaling adaptor activity; IDA:WormBase.
DR GO; GO:0031267; F:small GTPase binding; IPI:WormBase.
DR GO; GO:0045168; P:cell-cell signaling involved in cell fate commitment; IMP:WormBase.
DR GO; GO:0042742; P:defense response to bacterium; IMP:WormBase.
DR GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0019677; P:NAD catabolic process; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0034128; P:negative regulation of MyD88-independent toll-like receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:1901216; P:positive regulation of neuron death; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:1902097; P:positive regulation of transcription from RNA polymerase II promoter involved in defense response to Gram-negative bacterium; IMP:WormBase.
DR GO; GO:0008104; P:protein localization; IMP:WormBase.
DR GO; GO:1901214; P:regulation of neuron death; IBA:GO_Central.
DR GO; GO:0048678; P:response to axon injury; IMP:WormBase.
DR GO; GO:0042427; P:serotonin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR Gene3D; 1.10.150.50; -; 2.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR039184; SARM1.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR22998; PTHR22998; 1.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF13676; TIR_2; 1.
DR SMART; SM00454; SAM; 2.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF47769; SSF47769; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF52200; SSF52200; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW Hydrolase; Immunity; Innate immunity; NAD; Neurogenesis;
KW Reference proteome; Repeat.
FT CHAIN 1..981
FT /note="NAD(+) hydrolase tir-1"
FT /id="PRO_0000097587"
FT DOMAIN 614..678
FT /note="SAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 684..750
FT /note="SAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 760..857
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 908..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..128
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 842
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT BINDING 769..770
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_note="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT VAR_SEQ 1..638
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_013613"
FT VAR_SEQ 1..569
FT /note="MLPNRKPPRPSPSFQSLNNNNQRFPLRRSLKIAQAHSLPTVPSEDAKDDDLI
FT TPELSTDFDFREIQHRYLMALQNEQDGETTSTDDAFFELDDDDDLSSPSVPGSPVDPPS
FT ISVPLPPKSAPPCPTQPAPLTNGDLYPTILSNGTPIPNGRITPALSTVSVSLIHEARLQ
FT QSLSTPCNGSEEEMHNGQVRKESEYRRFKSEGSTAGASLPAAEKTHMDELSPVDQRSTS
FT GTARFLIQQDSVVNPSTKMSNTEQVAMMHTLKTKLSKYQAMMDKAFEEIAKVEDANIIE
FT GCTIVRKLMRKVWNTPKVSADLANALCDYLRDRDYFDKLIKMFISPNTAACDQVRMECG
FT KVLEECTSSANLEYIVNKSYTKKIMIVAMKLNKTPDQQRLSLSLIGNLFKHSNAVSLSL
FT IETDVIDHIILTFKRAPECPDILRHAALALANILLYTCFEGKKKIIQKKIPEWLFFLAS
FT QADDVTRYYACIAVCTIVSVKEFEPLVRKSDTMKLVEPFLQVHDPATFARDYHKYAQGN
FT TKEWLERLLPMLQPSRRREARSVAAFHFTLEATIKKEQNKLDVFQ -> MCALVSSPMV
FT SLPFNENVAPECRRNLLPRFAAVSPRPKAAVTPFVSTPSSSSITSFPYSLKLSNSNSNC
FT SSLSRPSSLTDLPILLRDVEDQMYDDDETPIIPCGSPSSSNSMLAQIQFHPPPTEMNSP
FT LKTSLKKLPMKTALVIRPQMFVKENSVQLERFRKSKTRRFFHPYAK (in isoform
FT b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060732"
FT VAR_SEQ 1..183
FT /note="Missing (in isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_060733"
FT VAR_SEQ 1..83
FT /note="MLPNRKPPRPSPSFQSLNNNNQRFPLRRSLKIAQAHSLPTVPSEDAKDDDLI
FT TPELSTDFDFREIQHRYLMALQNEQDGETTS -> MGEEILTERNQLSRQDASCFRSPR
FT SPLGR (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_060730"
FT VAR_SEQ 954
FT /note="F -> FFSV (in isoform a and isoform e)"
FT /evidence="ECO:0000305"
FT /id="VSP_060731"
SQ SEQUENCE 981 AA; 110556 MW; B114E320A3FF6CCA CRC64;
MLPNRKPPRP SPSFQSLNNN NQRFPLRRSL KIAQAHSLPT VPSEDAKDDD LITPELSTDF
DFREIQHRYL MALQNEQDGE TTSTDDAFFE LDDDDDLSSP SVPGSPVDPP SISVPLPPKS
APPCPTQPAP LTNGDLYPTI LSNGTPIPNG RITPALSTVS VSLIHEARLQ QSLSTPCNGS
EEEMHNGQVR KESEYRRFKS EGSTAGASLP AAEKTHMDEL SPVDQRSTSG TARFLIQQDS
VVNPSTKMSN TEQVAMMHTL KTKLSKYQAM MDKAFEEIAK VEDANIIEGC TIVRKLMRKV
WNTPKVSADL ANALCDYLRD RDYFDKLIKM FISPNTAACD QVRMECGKVL EECTSSANLE
YIVNKSYTKK IMIVAMKLNK TPDQQRLSLS LIGNLFKHSN AVSLSLIETD VIDHIILTFK
RAPECPDILR HAALALANIL LYTCFEGKKK IIQKKIPEWL FFLASQADDV TRYYACIAVC
TIVSVKEFEP LVRKSDTMKL VEPFLQVHDP ATFARDYHKY AQGNTKEWLE RLLPMLQPSR
RREARSVAAF HFTLEATIKK EQNKLDVFQE IGAIQALKEV ASSPDEVAAK FASEALTVIG
EEVPYKLAQQ VPGWTCADVQ YWVKKIGFEE YVEKFAKQMV DGDLLLQLTE NDLKHDVGMI
SGLHRKRFLR ELQTLKVAAD YSSVDESNLD NFLMGLSPEL SVYTYQMLTN GVNRSLLSSL
TDEMMQNACG ITNPIHRLKL TQAFETAKHP DDVEVAMLSK QIDVFISYRR STGNQLASLI
KVLLQLRGYR VFIDVDKLYA GKFDSSLLKN IQAAKHFILV LTPNSLDRLL NDDNCEDWVH
KELKCAFEHQ KNIIPIFDTA FEFPTKEDQI PNDIRMITKY NGVKWVHDYQ DACMAKVVRF
ITGELNRTTP TTKEMPSISR KTTQQRWQTT NTVSRTGPSR SIGGPRMEPP TPTFTPTGSQ
ERATSTRRKI QPSASTTSDR N
