ID   STMN3_PONAB             Reviewed;         180 AA.
AC   Q5R8C6;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Stathmin-3;
GN   Name=STMN3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR859827; CAH91984.1; -; mRNA.
DR   RefSeq; NP_001127491.1; NM_001134019.1.
DR   AlphaFoldDB; Q5R8C6; -.
DR   SMR; Q5R8C6; -.
DR   STRING; 9601.ENSPPYP00000012561; -.
DR   Ensembl; ENSPPYT00000013057; ENSPPYP00000012561; ENSPPYG00000011243.
DR   GeneID; 100174566; -.
DR   KEGG; pon:100174566; -.
DR   CTD; 50861; -.
DR   eggNOG; KOG1280; Eukaryota.
DR   GeneTree; ENSGT01030000234597; -.
DR   InParanoid; Q5R8C6; -.
DR   OrthoDB; 1381987at2759; -.
DR   Proteomes; UP000001595; Chromosome 20.
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:0019904; F:protein domain specific binding; IEA:Ensembl.
DR   GO; GO:0015631; F:tubulin binding; IEA:InterPro.
DR   GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR   GO; GO:0031122; P:cytoplasmic microtubule organization; IEA:Ensembl.
DR   GO; GO:0035021; P:negative regulation of Rac protein signal transduction; IEA:Ensembl.
DR   GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR   GO; GO:0043087; P:regulation of GTPase activity; IEA:Ensembl.
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_0000294078"
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;  21017 MW;  52F5E8A605FE10D0 CRC64;
     MASTISAYKE KMKELSVLSL ICSCFYTQPH PNTVYQYGDM EVKQLDKRAS GQSFEVILKS
     PSDLSPESPM LSSPPKKKDT SLEELQKRLE AAEERRKTQE AQVLKQLAER REHEREVLHK
     ALEENNNFSR QAEEKLNYKM ELSKEIREAH LAALRERLRE KELHAAEVRR NKEQREEMSG