STMN3_BOVIN
ID STMN3_BOVIN Reviewed; 180 AA.
AC A4IFK9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Stathmin-3;
GN Name=STMN3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9JHU6}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. Cell projection,
CC growth cone {ECO:0000250}. Cell projection, axon {ECO:0000250}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JHU6}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC134627; AAI34628.1; -; mRNA.
DR RefSeq; NP_001077135.1; NM_001083666.1.
DR AlphaFoldDB; A4IFK9; -.
DR SMR; A4IFK9; -.
DR STRING; 9913.ENSBTAP00000048555; -.
DR PaxDb; A4IFK9; -.
DR PRIDE; A4IFK9; -.
DR Ensembl; ENSBTAT00000057292; ENSBTAP00000048555; ENSBTAG00000038974.
DR GeneID; 511110; -.
DR KEGG; bta:511110; -.
DR CTD; 50861; -.
DR VEuPathDB; HostDB:ENSBTAG00000038974; -.
DR VGNC; VGNC:35405; STMN3.
DR eggNOG; KOG1280; Eukaryota.
DR GeneTree; ENSGT01030000234597; -.
DR HOGENOM; CLU_102026_0_0_1; -.
DR InParanoid; A4IFK9; -.
DR OMA; YSQPHPK; -.
DR OrthoDB; 1381987at2759; -.
DR TreeFam; TF326935; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000038974; Expressed in Ammon's horn and 62 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISS: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; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:Ensembl.
DR GO; GO:0007019; P:microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0035021; P:negative regulation of Rac protein signal transduction; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
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 2: Evidence at transcript 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_0000294076"
FT DOMAIN 38..180
FT /note="SLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00998"
FT REGION 58..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 76..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:0000250|UniProtKB:O70166"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70166"
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: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; 21016 MW; 62549074EF68FDC1 CRC64;
MASTISAYKE KMKELSVLSL ICSCFYSQPH PNTVYQYGDM EVKQLDKRAS GQSFEVILKS
PSDLSPESPM LSSPPKRKDT SLEELQKRLE AAEERRKTQE AQVLKQLAER REHEREVLHK
ALEENNNFSR LAEEKLNYKM ELSKEIREAH LAALRERLRE KELHAAEVRR NKEQREEMSG
