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Sterile alpha and TIR motif-containing protein 1 (Tir-1 homolog) (MyD88-5)

 SARM1_MOUSE             Reviewed;         724 AA.
Q6PDS3; Q5SYG5; Q5SYG6; Q6A054; Q6SZW0; Q8BRI9;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 122.
RecName: Full=Sterile alpha and TIR motif-containing protein 1;
AltName: Full=Tir-1 homolog;
Short=MyD88-5;
Flags: Precursor;
Name=Sarm1; Synonyms=Kiaa0524;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Bousson J.-C., Casteran C., Tiraby G.;
"SARM1 isoforms nucleotide sequence.";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Pancreatic islet;
PubMed=15368895; DOI=10.1093/dnares/11.3.205;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
IV. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 11:205-218(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain cortex;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MAPK10.
PubMed=17724133; DOI=10.1084/jem.20070868;
Kim Y., Zhou P., Qian L., Chuang J.Z., Lee J., Li C., Iadecola C.,
Nathan C., Ding A.;
"MyD88-5 links mitochondria, microtubules, and JNK3 in neurons and
regulates neuronal survival.";
J. Exp. Med. 204:2063-2074(2007).
[7]
REVIEW.
PubMed=18089857; DOI=10.1126/stke.4172007pe73;
Dalod M.;
"Studies of SARM1 uncover similarities between immune and neuronal
responses to danger.";
Sci. STKE 2007:PE73-PE73(2007).
[8]
FUNCTION.
PubMed=19587044; DOI=10.1128/JVI.00836-09;
Szretter K.J., Samuel M.A., Gilfillan S., Fuchs A., Colonna M.,
Diamond M.S.;
"The immune adaptor molecule SARM modulates tumor necrosis factor
alpha production and microglia activation in the brainstem and
restricts West Nile virus pathogenesis.";
J. Virol. 83:9329-9338(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548 AND SER-558, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH SDC2,
AND TISSUE SPECIFICITY.
PubMed=21555464; DOI=10.1083/jcb.201008050;
Chen C.Y., Lin C.W., Chang C.Y., Jiang S.T., Hsueh Y.P.;
"Sarm1, a negative regulator of innate immunity, interacts with
syndecan-2 and regulates neuronal morphology.";
J. Cell Biol. 193:769-784(2011).
[11]
REVIEW.
PubMed=22837513; DOI=10.1126/science.1226150;
Yu X.M., Luo L.;
"Neuroscience. dSarm-ing axon degeneration.";
Science 337:418-419(2012).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=22678360; DOI=10.1126/science.1223899;
Osterloh J.M., Yang J., Rooney T.M., Fox A.N., Adalbert R.,
Powell E.H., Sheehan A.E., Avery M.A., Hackett R., Logan M.A.,
MacDonald J.M., Ziegenfuss J.S., Milde S., Hou Y.J., Nathan C.,
Ding A., Brown R.H. Jr., Conforti L., Coleman M., Tessier-Lavigne M.,
Zuechner S., Freeman M.R.;
"dSarm/Sarm1 is required for activation of an injury-induced axon
death pathway.";
Science 337:481-484(2012).
-!- FUNCTION: Negative regulator of MYD88- and TRIF-dependent toll-
like receptor signaling pathway which plays a pivotal role in
activating axonal degeneration following injury. Promotes
Wallerian degeneration an injury-induced axonal death pathway
which involves degeneration of an axon distal to the injury site.
Can activate neuronal death in response to stress. Regulates
dendritic arborization through the MAPK4-JNK pathway. Involved in
innate immune response. Inhibits both TICAM1/TRIF- and MYD88-
dependent activation of JUN/AP-1, TRIF-dependent activation of NF-
kappa-B and IRF3, and the phosphorylation of MAPK14/p38. Can
restrict West Nile virus (WNV) pathogenesis.
{ECO:0000269|PubMed:17724133, ECO:0000269|PubMed:19587044,
ECO:0000269|PubMed:21555464, ECO:0000269|PubMed:22678360}.
-!- SUBUNIT: Interacts with TICAM1/TRIF and thereby interferes with
TICAM1/TRIF function (By similarity). Interacts with SDC2 (via
cytoplasmic domain) and MAPK10/JNK3. {ECO:0000250,
ECO:0000269|PubMed:17724133, ECO:0000269|PubMed:21555464}.
-!- INTERACTION:
Q96A33:CCDC47 (xeno); NbExp=2; IntAct=EBI-6117196, EBI-720151;
Q9H3K2:GHITM (xeno); NbExp=2; IntAct=EBI-6117196, EBI-2868909;
O43187:IRAK2 (xeno); NbExp=2; IntAct=EBI-6117196, EBI-447733;
Q86UT6:NLRX1 (xeno); NbExp=2; IntAct=EBI-6117196, EBI-3893071;
P46977:STT3A (xeno); NbExp=2; IntAct=EBI-6117196, EBI-719212;
-!- SUBCELLULAR LOCATION: Cytoplasm. Cell projection, axon. Cell
projection, dendrite. Cell junction, synapse. Mitochondrion.
Note=Associated with microtubules.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q6PDS3-1; Sequence=Displayed;
Name=2;
IsoId=Q6PDS3-2; Sequence=VSP_013604;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q6PDS3-3; Sequence=VSP_013605;
Name=4;
IsoId=Q6PDS3-4; Sequence=VSP_013606, VSP_013607;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed in the brain and neurons (at
protein level). {ECO:0000269|PubMed:21555464}.
-!- DISRUPTION PHENOTYPE: Severed Sarm1 null axons are able to persist
up to 72 hrs after axotomy, whereas wild-type axons degenerate
within 8 hrs. Similarly, axons appear to be protected from
degeneration in a sciatic nerve lesion model, lasting up to 14
days compared with 3 days for wild type.
{ECO:0000269|PubMed:22678360}.
-!- SEQUENCE CAUTION:
Sequence=BAD32242.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAI25546.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AY444167; AAR17521.1; -; mRNA.
EMBL; AK172964; BAD32242.1; ALT_INIT; Transcribed_RNA.
EMBL; AK044113; BAC31784.1; -; mRNA.
EMBL; AL591177; CAI25544.1; -; Genomic_DNA.
EMBL; AL591177; CAI25545.1; -; Genomic_DNA.
EMBL; AL591177; CAI25546.1; ALT_SEQ; Genomic_DNA.
EMBL; BC058534; AAH58534.1; -; mRNA.
EMBL; BC080850; AAH80850.1; -; mRNA.
CCDS; CCDS25105.1; -. [Q6PDS3-1]
CCDS; CCDS48857.1; -. [Q6PDS3-3]
RefSeq; NP_001161993.1; NM_001168521.1. [Q6PDS3-3]
RefSeq; NP_766383.2; NM_172795.3. [Q6PDS3-1]
UniGene; Mm.210332; -.
ProteinModelPortal; Q6PDS3; -.
BioGrid; 231917; 1.
IntAct; Q6PDS3; 11.
MINT; MINT-4997481; -.
iPTMnet; Q6PDS3; -.
PhosphoSitePlus; Q6PDS3; -.
PeptideAtlas; Q6PDS3; -.
PRIDE; Q6PDS3; -.
Ensembl; ENSMUST00000061174; ENSMUSP00000051059; ENSMUSG00000050132. [Q6PDS3-1]
Ensembl; ENSMUST00000108287; ENSMUSP00000103922; ENSMUSG00000050132. [Q6PDS3-3]
GeneID; 237868; -.
KEGG; mmu:237868; -.
UCSC; uc007kjh.2; mouse. [Q6PDS3-4]
UCSC; uc007kji.2; mouse. [Q6PDS3-1]
UCSC; uc007kjj.2; mouse. [Q6PDS3-3]
CTD; 23098; -.
MGI; MGI:2136419; Sarm1.
GeneTree; ENSGT00390000004155; -.
HOGENOM; HOG000008460; -.
HOVERGEN; HBG079166; -.
InParanoid; Q6PDS3; -.
OMA; CIAAFYL; -.
OrthoDB; EOG091G01TX; -.
PhylomeDB; Q6PDS3; -.
TreeFam; TF315263; -.
PRO; PR:Q6PDS3; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000050132; -.
Genevisible; Q6PDS3; MM.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IMP:UniProtKB.
GO; GO:0031315; C:extrinsic component of mitochondrial outer membrane; IDA:MGI.
GO; GO:0005874; C:microtubule; IDA:UniProtKB.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0045202; C:synapse; IDA:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:UniProtKB.
GO; GO:1901214; P:regulation of neuron death; IMP:UniProtKB.
GO; GO:0009749; P:response to glucose; IMP:MGI.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
Gene3D; 1.25.10.10; -; 1.
Gene3D; 3.40.50.10140; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed.
InterPro; IPR000157; TIR_dom.
InterPro; IPR035897; Toll_tir_struct_dom_sf.
Pfam; PF07647; SAM_2; 2.
Pfam; PF13676; TIR_2; 1.
SMART; SM00454; SAM; 2.
SMART; SM00255; TIR; 1.
SUPFAM; SSF47769; SSF47769; 2.
SUPFAM; SSF48371; SSF48371; 1.
SUPFAM; SSF52200; SSF52200; 1.
PROSITE; PS50105; SAM_DOMAIN; 2.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell projection;
Complete proteome; Cytoplasm; Differentiation; Immunity;
Innate immunity; Mitochondrion; Neurogenesis; Phosphoprotein;
Reference proteome; Repeat; Synapse; Transit peptide.
TRANSIT 1 27 Mitochondrion. {ECO:0000250}.
CHAIN 28 724 Sterile alpha and TIR motif-containing
protein 1.
/FTId=PRO_0000097590.
DOMAIN 412 476 SAM 1. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
DOMAIN 486 548 SAM 2. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
DOMAIN 559 657 TIR.
MOD_RES 548 548 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 558 558 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 536 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_013606.
VAR_SEQ 435 439 Missing (in isoform 2).
{ECO:0000303|PubMed:15368895}.
/FTId=VSP_013604.
VAR_SEQ 537 543 RILSAAR -> MSLSLAP (in isoform 4).
{ECO:0000305}.
/FTId=VSP_013607.
VAR_SEQ 543 543 R -> RGHFAQTGLRSLRRPSLHDDGPRDKQWGRATLTSMS
LSLAP (in isoform 3).
{ECO:0000303|Ref.1}.
/FTId=VSP_013605.
CONFLICT 61 61 V -> A (in Ref. 1; AAR17521).
{ECO:0000305}.
SEQUENCE 724 AA; 79606 MW; 9A5BF03ED22E6102 CRC64;
MVLTLLFSAY KLCRFFTMSG PRPGADRLTV PGPDRSGGAS PWWAAGGRGS REVSPGVGTE
VQGALERSLP ELQQALSELK QASAARAVGA GLAEVFQLVE EAWLLPAVGR EVAQGLCDAI
RLDGGLDLLL RLLQAPELET RVQAARLLEQ ILVAENRDRV ARIGLGVILN LAKEREPVEL
ARSVAGILEH MFKHSEETCQ RLVAAGGLDA VLYWCRRTDP ALLRHCALAL ANCALHGGQT
VQRCMVEKRA AEWLFPLAFS KEDELLRLHA CLAVAVLATN KEVEREVEHS GTLALVEPLV
ASLDPGRFAR CLVDASDTSQ GRGPDDLQSL VLLLDSSRLE AQCIGAFYLC AEAAIKSLQG
KTKVFSDIGA IQSLKRLVSY STNGTTSALA KRALRLLGEE VPRRILPCVA SWKEAEVQTW
LQQIGFSQYC ENFREQQVDG DLLLRLTDEE LQTDLGMKSS ITRKRFFREL TELKTFASYA
TCDRSNLADW LGSLDPRFRQ YTYGLVSCGL DRSLLHRVSE QQLLEDCGIR LGVHRTRILS
AAREMLHSPL PCTGGKLSGD TPDVFISYRR NSGSQLASLL KVHLQLHGFS VFIDVEKLEA
GKFEDKLIQS VIAARNFVLV LSAGALDKCM QDHDCKDWVH KEIVTALSCG KNIVPIIDGF
EWPEPQALPE DMQAVLTFNG IKWSHEYQEA TIEKIIRFLQ GRPSQDSSAG SDTSLEGATP
MGLP


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