STMN2_CHICK
ID STMN2_CHICK Reviewed; 179 AA.
AC Q90987;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Stathmin-2;
DE AltName: Full=Superior cervical ganglion-10 protein;
DE Short=Protein SCG10;
GN Name=STMN2; Synonyms=SCG10;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn; TISSUE=Cerebellum;
RX PubMed=8735217; DOI=10.1016/0306-4522(95)00593-5;
RA Hannan A.J., Henke R.C., Weinberger R.P., Sentry J.W., Jeffrey P.L.;
RT "Differential induction and intracellular localization of SCG10 messenger
RT RNA is associated with neuronal differentiation.";
RL Neuroscience 72:889-900(1996).
CC -!- FUNCTION: Is a key regulator of neurite extension through regulation of
CC microtubule instabilily. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, perinuclear
CC region {ECO:0000250}. Cell projection, growth cone {ECO:0000250}.
CC Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305};
CC Cytoplasmic side {ECO:0000305}. Cell projection, axon {ECO:0000250}.
CC Cell projection, lamellipodium {ECO:0000250}. Note=Associated with
CC punctate structures in the perinuclear cytoplasm, axons, and growth
CC cones of developing neurons. SCG10 exists in both soluble and membrane-
CC bound forms (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expression is neuron-specific and found in
CC cerebellum, forebrain, midbrain, tectum and spinal cord.
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; L14938; AAB19119.1; -; mRNA.
DR RefSeq; NP_990512.1; NM_205181.1.
DR AlphaFoldDB; Q90987; -.
DR SMR; Q90987; -.
DR STRING; 9031.ENSGALP00000025330; -.
DR PaxDb; Q90987; -.
DR Ensembl; ENSGALT00000061746; ENSGALP00000055841; ENSGALG00000039690.
DR GeneID; 396095; -.
DR KEGG; gga:396095; -.
DR CTD; 11075; -.
DR VEuPathDB; HostDB:geneid_396095; -.
DR eggNOG; ENOG502RENQ; Eukaryota.
DR GeneTree; ENSGT01030000234597; -.
DR InParanoid; Q90987; -.
DR OMA; HMAAMME; -.
DR OrthoDB; 1381987at2759; -.
DR PhylomeDB; Q90987; -.
DR TreeFam; TF326935; -.
DR PRO; PR:Q90987; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000039690; Expressed in brain and 11 other tissues.
DR ExpressionAtlas; Q90987; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0048306; F:calcium-dependent protein binding; IEA:Ensembl.
DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0007019; P:microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IEA:Ensembl.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0031117; P:positive regulation of microtubule depolymerization; IEA:Ensembl.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IBA:GO_Central.
DR InterPro; IPR026729; Stathmin-2.
DR InterPro; IPR030514; Stathmin_CS.
DR InterPro; IPR000956; Stathmin_fam.
DR InterPro; IPR036002; Stathmin_sf.
DR PANTHER; PTHR10104; PTHR10104; 1.
DR PANTHER; PTHR10104:SF18; PTHR10104:SF18; 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; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..179
FT /note="Stathmin-2"
FT /id="PRO_0000182399"
FT DOMAIN 38..179
FT /note="SLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00998"
FT REGION 1..26
FT /note="Membrane attachment"
FT /evidence="ECO:0000255"
FT REGION 39..96
FT /note="Regulatory/phosphorylation domain"
FT /evidence="ECO:0000255"
FT COILED 74..179
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 179 AA; 20882 MW; 55D57A1CF99330F2 CRC64;
MAKTAMAYKE KMKELSMLSL ICSCFYPEPR NMNIYKYDDM EVKQINKRAS GQAFELILKP
PSPVSEAPRT LASPKKKELS LEEIQKKLEA AEERRKSQEA QVLKHLAEKR EHEREVLQKA
LEENNNFSKM AEEKLILKME QIKENREANL AALIERLQEK ERHAAEVRRN KELQVELSG
