ID   STMN3_MACFA             Reviewed;         180 AA.
AC   Q4R4N5;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Stathmin-3;
GN   Name=STMN3; ORFNames=QccE-15529;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) 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}.
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DR   EMBL; AB169859; BAE01940.1; -; mRNA.
DR   RefSeq; NP_001270634.1; NM_001283705.1.
DR   RefSeq; XP_015313111.1; XM_015457625.1.
DR   AlphaFoldDB; Q4R4N5; -.
DR   SMR; Q4R4N5; -.
DR   STRING; 9541.XP_005569656.1; -.
DR   GeneID; 101865045; -.
DR   KEGG; mcf:101865045; -.
DR   CTD; 50861; -.
DR   VEuPathDB; HostDB:ENSMFAG00000044092; -.
DR   eggNOG; KOG1280; Eukaryota.
DR   OMA; YSQPHPK; -.
DR   OrthoDB; 1381987at2759; -.
DR   Proteomes; UP000233100; Chromosome 10.
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:0015631; F:tubulin binding; IEA:InterPro.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:InterPro.
DR   GO; GO:0031175; P:neuron projection development; IEA:InterPro.
DR   GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IEA:InterPro.
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_0000294077"
FT   DOMAIN          38..180
FT                   /note="SLD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00998"
FT   REGION          59..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;  21031 MW;  4C040F3B2C92C0D0 CRC64;
     MASTISAYKE KMKELSVLSL ICSCFYTQPH PNTIYQYGDM EVKQLDKRAS GQSFEVILKS
     PSDLSPESPM LSSPPKKKDT SLEELQKRLE AAEERRKTQE AQVLKQLAER REHEREVLHK
     ALEENNNFSR QAEEKLNYKM ELSKEIREAH LAALRERLRE KELHAAEVRR NKEQREEMSG