STMN3_MOUSE
ID STMN3_MOUSE Reviewed; 180 AA.
AC O70166;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Stathmin-3;
DE AltName: Full=Hippocampus abundant transcript 3;
DE AltName: Full=SCG10-like protein;
DE AltName: Full=SCG10-related protein HiAT3;
GN Name=Stmn3; Synonyms=Sclip;
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/6J; TISSUE=Hippocampus;
RX PubMed=9714847; DOI=10.1016/s0378-1119(98)00324-2;
RA Matsuo N., Kawamoto S., Matsubara K., Okubo K.;
RT "A novel SCG10-related gene uniquely expressed in the nervous system.";
RL Gene 215:477-481(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9603203; DOI=10.1046/j.1471-4159.1998.70062386.x;
RA Ozon S., Byk T., Sobel A.;
RT "SCLIP: a novel SCG10-like protein of the stathmin family expressed in the
RT nervous system.";
RL J. Neurochem. 70:2386-2396(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND SER-68, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH STAT3.
RX PubMed=16401721; DOI=10.1083/jcb.200503021;
RA Ng D.C., Lin B.H., Lim C.P., Huang G., Zhang T., Poli V., Cao X.;
RT "Stat3 regulates microtubules by antagonizing the depolymerization activity
RT of stathmin.";
RL J. Cell Biol. 172:245-257(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-60; SER-65; SER-68;
RP SER-72 AND SER-73, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Exhibits microtubule-destabilizing activity, which is
CC antagonized by STAT3. {ECO:0000269|PubMed:16401721}.
CC -!- SUBUNIT: Interacts with STAT3. Interacts with CLU (secreted form); this
CC interaction may act as an important modulator during neuronal
CC differentiation (By similarity). {ECO:0000250|UniProtKB:Q9JHU6,
CC ECO:0000269|PubMed:16401721}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cell projection, growth cone.
CC Cell projection, axon. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9JHU6}.
CC -!- TISSUE SPECIFICITY: Neuron specific.
CC -!- PTM: N-terminal palmitoylation promotes specific anchoring to the
CC cytosolic leaflet of Golgi membranes and subsequent vesicular
CC trafficking along dendrites and axons. Neuronal Stathmins are
CC substrates for palmitoyltransferases ZDHHC3, ZDHHC7 and ZDHHC15 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the stathmin family. {ECO:0000305}.
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DR EMBL; AB007912; BAA28629.1; -; mRNA.
DR EMBL; AF069708; AAC21575.1; -; mRNA.
DR EMBL; BC057017; AAH57017.1; -; mRNA.
DR CCDS; CCDS17207.1; -.
DR RefSeq; NP_033159.1; NM_009133.3.
DR AlphaFoldDB; O70166; -.
DR SMR; O70166; -.
DR BioGRID; 203096; 13.
DR IntAct; O70166; 1.
DR STRING; 10090.ENSMUSP00000099334; -.
DR iPTMnet; O70166; -.
DR PhosphoSitePlus; O70166; -.
DR PaxDb; O70166; -.
DR PeptideAtlas; O70166; -.
DR PRIDE; O70166; -.
DR ProteomicsDB; 258765; -.
DR Antibodypedia; 29816; 201 antibodies from 29 providers.
DR Ensembl; ENSMUST00000103045; ENSMUSP00000099334; ENSMUSG00000027581.
DR GeneID; 20262; -.
DR KEGG; mmu:20262; -.
DR UCSC; uc008olt.1; mouse.
DR CTD; 50861; -.
DR MGI; MGI:1277137; Stmn3.
DR VEuPathDB; HostDB:ENSMUSG00000027581; -.
DR eggNOG; KOG1280; Eukaryota.
DR GeneTree; ENSGT01030000234597; -.
DR HOGENOM; CLU_102026_0_0_1; -.
DR InParanoid; O70166; -.
DR OMA; YSQPHPK; -.
DR OrthoDB; 1381987at2759; -.
DR PhylomeDB; O70166; -.
DR TreeFam; TF326935; -.
DR BioGRID-ORCS; 20262; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Stmn3; mouse.
DR PRO; PR:O70166; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O70166; protein.
DR Bgee; ENSMUSG00000027581; Expressed in facial nucleus and 248 other tissues.
DR ExpressionAtlas; O70166; baseline and differential.
DR Genevisible; O70166; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IPI:HGNC-UCL.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IDA:HGNC-UCL.
DR GO; GO:0007019; P:microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0035021; P:negative regulation of Rac protein signal transduction; IDA:HGNC-UCL.
DR GO; GO:0031175; P:neuron projection development; IDA:HGNC-UCL.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IDA:HGNC-UCL.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:HGNC-UCL.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IBA:GO_Central.
DR InterPro; IPR028835; Stathmin-3.
DR InterPro; IPR030514; Stathmin_CS.
DR InterPro; IPR000956; Stathmin_fam.
DR InterPro; IPR036002; Stathmin_sf.
DR PANTHER; PTHR10104; PTHR10104; 1.
DR PANTHER; PTHR10104:SF17; PTHR10104:SF17; 1.
DR Pfam; PF00836; Stathmin; 1.
DR PIRSF; PIRSF002285; Stathmin; 1.
DR PRINTS; PR00345; STATHMIN.
DR SUPFAM; SSF101494; SSF101494; 1.
DR PROSITE; PS00563; STATHMIN_1; 1.
DR PROSITE; PS01041; STATHMIN_2; 1.
DR PROSITE; PS51663; STATHMIN_3; 1.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Golgi apparatus; Lipoprotein;
KW Palmitate; Phosphoprotein; Reference proteome.
FT CHAIN 1..180
FT /note="Stathmin-3"
FT /id="PRO_0000182403"
FT DOMAIN 38..180
FT /note="SLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00998"
FT REGION 60..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 75..179
FT /evidence="ECO:0000255"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHU6"
FT LIPID 22
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 24
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 180 AA; 20954 MW; A7C0D35A6A684765 CRC64;
MASTVSAYKE KMKELSVLSL ICSCFYSQPH PNTIYQYGDM EVKQLDKRAS GQSFEVILKS
PSDLSPESPV LSSPPKRKDA SLEELQKRLE AAEERRKTQE AQVLKQLAER REHEREVLHK
ALEENNNFSR LAEEKLNYKM ELSKEIREAH LAALRERLRE KELHAAEVRR NKEQREEMSG
