STM1A_XENLA
ID STM1A_XENLA Reviewed; 145 AA.
AC Q09006; Q6GNQ3;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Stathmin-1-A;
DE AltName: Full=Stathmin clone XO35;
GN Name=stmn1-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RX PubMed=8344928; DOI=10.1016/s0021-9258(19)85437-6;
RA Maucuer A., Moreau J., Mechali M., Sobel A.;
RT "Stathmin gene family: phylogenetic conservation and developmental
RT regulation in Xenopus.";
RL J. Biol. Chem. 268:16420-16429(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the regulation of the microtubule (MT) filament
CC system by destabilizing microtubules. It prevents assembly and promotes
CC disassembly of microtubules (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to two alpha/beta-tubulin heterodimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Mostly abundant in brain and oocytes.
CC -!- DEVELOPMENTAL STAGE: Accumulates during oogenesis and remains stable as
CC a maternal product throughout early development.
CC -!- PTM: Different phosphorylated forms, from unphosphorylated to highly
CC phosphorylated, are found in the mature egg. Progressive
CC dephosphorylation from the mid-blastula to the tailbud stage.
CC -!- SIMILARITY: Belongs to the stathmin family. {ECO:0000305}.
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DR EMBL; X71431; CAA50562.1; -; mRNA.
DR EMBL; BC073451; AAH73451.1; -; mRNA.
DR PIR; I51706; I51706.
DR RefSeq; NP_001081627.1; NM_001088158.1.
DR RefSeq; XP_018100360.1; XM_018244871.1.
DR RefSeq; XP_018100361.1; XM_018244872.1.
DR AlphaFoldDB; Q09006; -.
DR SMR; Q09006; -.
DR DNASU; 397962; -.
DR GeneID; 397962; -.
DR KEGG; xla:397962; -.
DR CTD; 397962; -.
DR Xenbase; XB-GENE-6252151; stmn1.L.
DR OMA; MAFELVF; -.
DR OrthoDB; 1381987at2759; -.
DR Proteomes; UP000186698; Chromosome 2L.
DR Bgee; 397962; Expressed in blastula and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IEA:InterPro.
DR InterPro; IPR030514; Stathmin_CS.
DR InterPro; IPR000956; Stathmin_fam.
DR InterPro; IPR036002; Stathmin_sf.
DR PANTHER; PTHR10104; PTHR10104; 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 Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..145
FT /note="Stathmin-1-A"
FT /id="PRO_0000182394"
FT DOMAIN 4..145
FT /note="SLD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00998"
FT COILED 40..135
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 145 AA; 16789 MW; B9FE2D403C25C0F1 CRC64;
MCDSDIKVKQ LEKRASGQAF ELILSPPSMD AAPDLSITSP KKKECSLEEI QKKLEAAEER
RKLHEAEILK QLAEKREHEK EVLQKAIEEN NNFSKMAEEK LTTKMETIKE NREAQIAAKL
ERLREKDKKV EEIRKGKECK EPSEK
