STMN2_RAT
ID STMN2_RAT Reviewed; 179 AA.
AC P21818; Q9ERH2;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Stathmin-2;
DE AltName: Full=Superior cervical ganglion-10 protein;
DE Short=Protein SCG10;
GN Name=Stmn2; Synonyms=Scg10, Scgn10;
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].
RX PubMed=3272176; DOI=10.1016/0896-6273(88)90177-8;
RA Stein R., Mori N., Matthews K., Lo L.-C., Anderson D.J.;
RT "The NGF-inducible SCG10 mRNA encodes a novel membrane-bound protein
RT present in growth cones and abundant in developing neurons.";
RL Neuron 1:463-476(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Spinal ganglion;
RA Xiao H., Huang Q., Zhang F., Yang Z., Chen Z., Han Z., Zhang X.;
RT "Novel genes expressed in rat dorsal root ganglion.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION.
RX PubMed=9012855; DOI=10.1073/pnas.94.2.741;
RA Riederer B.M., Pellier V., Antonsson B., Di Paolo G., Stimpson S.A.,
RA Luetjens R., Catsicas S., Grenningloh G.;
RT "Regulation of microtubule dynamics by the neuronal growth-associated
RT protein SCG10.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:741-745(1997).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-62 AND SER-73,
RP INTERACTION WITH MAPK8, AND MUTAGENESIS OF SER-62 AND SER-73.
RX PubMed=16618812; DOI=10.1083/jcb.200511055;
RA Tararuk T., Ostman N., Li W., Bjorkblom B., Padzik A., Zdrojewska J.,
RA Hongisto V., Herdegen T., Konopka W., Courtney M.J., Coffey E.T.;
RT "JNK1 phosphorylation of SCG10 determines microtubule dynamics and
RT axodendritic length.";
RL J. Cell Biol. 173:265-277(2006).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21215777; DOI=10.1016/j.bbamcr.2010.12.023;
RA Sobczak A., Debowska K., Blazejczyk M., Kreutz M.R., Kuznicki J., Wojda U.;
RT "Calmyrin1 binds to SCG10 protein (stathmin2) to modulate neurite
RT outgrowth.";
RL Biochim. Biophys. Acta 1813:1025-1037(2011).
RN [7]
RP FUNCTION.
RX PubMed=21297631; DOI=10.1038/nn.2755;
RA Westerlund N., Zdrojewska J., Padzik A., Komulainen E., Bjorkblom B.,
RA Rannikko E., Tararuk T., Garcia-Frigola C., Sandholm J., Nguyen L.,
RA Kallunki T., Courtney M.J., Coffey E.T.;
RT "Phosphorylation of SCG10/stathmin-2 determines multipolar stage exit and
RT neuronal migration rate.";
RL Nat. Neurosci. 14:305-313(2011).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50 AND SER-62, 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: Regulator of microtubule stability. When phosphorylated by
CC MAPK8, stabilizes microtubules and consequently controls neurite length
CC in cortical neurons. In the developing brain, negatively regulates the
CC rate of exit from multipolar stage and retards radial migration from
CC the ventricular zone. {ECO:0000269|PubMed:16618812,
CC ECO:0000269|PubMed:21297631, ECO:0000269|PubMed:9012855}.
CC -!- SUBUNIT: Interacts with ITM2C (By similarity). Interacts with MAPK8.
CC Interacts with KIFBP (By similarity). Interacts (via the N-terminal
CC region) with CIB1 (via C-terminal region); the interaction is direct,
CC occurs in a calcium-dependent manner and attenuates the neurite
CC outgrowth inhibition of STMN2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region. Cell
CC projection, growth cone. Cell projection, axon. Membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}. Golgi apparatus. Endosome. Cell projection,
CC lamellipodium {ECO:0000250}. Note=Colocalized with CIB1 in the cell
CC body, neuritis and growth cones of neurons. Colocalized with CIB1 to
CC the leading edge of lamellipodia (By similarity). Associated with
CC punctate structures in the perinuclear cytoplasm, axons, and growth
CC cones of developing neurons. Exists in both soluble and membrane-bound
CC forms. Colocalized with CIB1 in neurites of developing hippocampal
CC primary neurons. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in neurons (at protein level). Present in
CC growth cones and abundant in developing neurons.
CC {ECO:0000269|PubMed:21215777}.
CC -!- DEVELOPMENTAL STAGE: In the developing cerebellum, maximal levels occur
CC at postnatal day 7 and correlate with the onset of neuronal
CC differentiation.
CC -!- INDUCTION: By nerve growth factor.
CC -!- PTM: Sumoylated. {ECO:0000250}.
CC -!- PTM: Pphosphorylated by MAPK9 and MAPK10 in the developing brain cortex
CC (By similarity). Phosphorylated mostly by MAPK8. {ECO:0000250,
CC ECO:0000269|PubMed:16618812}.
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; AF306458; AAG33230.1; -; mRNA.
DR EMBL; BC087660; AAH87660.1; -; mRNA.
DR PIR; A36110; A36110.
DR RefSeq; NP_445892.1; NM_053440.2.
DR AlphaFoldDB; P21818; -.
DR SMR; P21818; -.
DR STRING; 10116.ENSRNOP00000015720; -.
DR iPTMnet; P21818; -.
DR PhosphoSitePlus; P21818; -.
DR SwissPalm; P21818; -.
DR jPOST; P21818; -.
DR PaxDb; P21818; -.
DR PRIDE; P21818; -.
DR ABCD; P21818; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000015720; ENSRNOP00000015720; ENSRNOG00000011705.
DR GeneID; 84510; -.
DR KEGG; rno:84510; -.
DR UCSC; RGD:68947; rat.
DR CTD; 11075; -.
DR RGD; 68947; Stmn2.
DR eggNOG; ENOG502RENQ; Eukaryota.
DR GeneTree; ENSGT01030000234597; -.
DR HOGENOM; CLU_102026_0_0_1; -.
DR InParanoid; P21818; -.
DR OMA; HMAAMME; -.
DR OrthoDB; 1381987at2759; -.
DR Reactome; R-RNO-9696273; RND1 GTPase cycle.
DR PRO; PR:P21818; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000011705; Expressed in cerebellum and 18 other tissues.
DR Genevisible; P21818; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:RGD.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:0031117; P:positive regulation of microtubule depolymerization; ISO:RGD.
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 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Endosome; Golgi apparatus;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..179
FT /note="Stathmin-2"
FT /id="PRO_0000182398"
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 75..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:0007744|PubMed:22673903"
FT MOD_RES 62
FT /note="Phosphoserine; by MAPK8"
FT /evidence="ECO:0000269|PubMed:16618812,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 73
FT /note="Phosphoserine; by MAPK8"
FT /evidence="ECO:0000269|PubMed:16618812"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHU6, ECO:0000255"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16949, ECO:0000255"
FT LIPID 22
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 24
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT MUTAGEN 62
FT /note="S->A: Partial loss of phosphorylation. Complete loss
FT of phosphorylation by MAPK8, increased microtubule
FT solubility, and reduced neurite length; when associated
FT with A-73."
FT /evidence="ECO:0000269|PubMed:16618812"
FT MUTAGEN 62
FT /note="S->D: Increased microtubule stability but no effect
FT on neurite length; when associated with A-73."
FT /evidence="ECO:0000269|PubMed:16618812"
FT MUTAGEN 73
FT /note="S->A: Partial loss of phosphorylation. Complete loss
FT of phosphorylation by MAPK8, increased microtubule
FT solubility, and reduced neurite length; when associated
FT with A-62."
FT /evidence="ECO:0000269|PubMed:16618812"
FT MUTAGEN 73
FT /note="S->D: Increased microtubule stability but no effect
FT on neurite length; when associated with A-62."
FT /evidence="ECO:0000269|PubMed:16618812"
FT CONFLICT 59
FT /note="K -> L (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 179 AA; 20756 MW; 8B827AA3977E61B8 CRC64;
MAKTAMAYKE KMKELSMLSL ICSCFYPEPR NINIYTYDDM EVKQINKRAS GQAFELILKP
PSPISEAPRT LASPKKKDLS LEEIQKKLEA AEGRRKSQEA QVLKQLAEKR EHEREVLQKA
LEENNNFSKM AEEKLILKME QIKENREANL AAIIERLQEK ERHAAEVRRN KELQVELSG
