STMN3_RAT
ID STMN3_RAT Reviewed; 180 AA.
AC Q9JHU6;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Stathmin-3;
DE AltName: Full=SCG10-like protein;
GN Name=Stmn3; Synonyms=Sclip;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Xiao H., Huang Q., Zhang F., Yang Z., Chen Z., Han Z., Zhang X.;
RT "Novel genes expression in rat brain.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP INTERACTION WITH CLU, AND SUBCELLULAR LOCATION.
RX PubMed=16038898; DOI=10.1016/j.yexcr.2005.06.012;
RA Kang S.W., Shin Y.J., Shim Y.J., Jeong S.Y., Park I.S., Min B.H.;
RT "Clusterin interacts with SCLIP (SCG10-like protein) and promotes neurite
RT outgrowth of PC12 cells.";
RL Exp. Cell Res. 309:305-315(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-68 AND SER-81, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Exhibits microtubule-destabilizing activity, which is
CC antagonized by STAT3. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with STAT3. Interacts with CLU (secreted form); this
CC interaction may act as an important modulator during neuronal
CC differentiation (PubMed:16038898). {ECO:0000250,
CC ECO:0000269|PubMed:16038898}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cell projection,
CC growth cone {ECO:0000250}. Cell projection, axon {ECO:0000250}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:16038898}.
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; AY004290; AAF86617.1; -; mRNA.
DR RefSeq; NP_077322.1; NM_024346.1.
DR AlphaFoldDB; Q9JHU6; -.
DR SMR; Q9JHU6; -.
DR BioGRID; 247922; 2.
DR STRING; 10116.ENSRNOP00000018697; -.
DR iPTMnet; Q9JHU6; -.
DR PhosphoSitePlus; Q9JHU6; -.
DR SwissPalm; Q9JHU6; -.
DR PRIDE; Q9JHU6; -.
DR GeneID; 29246; -.
DR KEGG; rno:29246; -.
DR CTD; 50861; -.
DR RGD; 3628; Stmn3.
DR eggNOG; KOG1280; Eukaryota.
DR InParanoid; Q9JHU6; -.
DR OrthoDB; 1381987at2759; -.
DR PRO; PR:Q9JHU6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0001835; P:blastocyst hatching; ISO:RGD.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:HGNC-UCL.
DR GO; GO:0007019; P:microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0035021; P:negative regulation of Rac protein signal transduction; ISS:HGNC-UCL.
DR GO; GO:0031175; P:neuron projection development; ISS:HGNC-UCL.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; ISS:HGNC-UCL.
DR GO; GO:0043087; P:regulation of GTPase activity; ISS: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_0000182404"
FT DOMAIN 38..180
FT /note="SLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00998"
FT REGION 58..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:0000250|UniProtKB:O70166"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70166"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70166"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70166"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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; 20895 MW; A7C0D0D7DCB0A765 CRC64;
MASTVSAYKE KMKELSVLSL ICSCFYSQPH PNTIYQYGDM EVKQLDKRAS GQSFEVILKS
PSDLSPESPV LSSPPKRKDA SLEELQKRLE AAEERRKTQE AQVLKQLAER REHEREVLHK
ALEENNNFSP LAEEKLNYKM ELSKEIREAH LAALRERLRE KELHAAEVRR NKEQREEMSG
