ID   STM1B_XENLA             Reviewed;          71 AA.
AC   Q09005;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Stathmin-1-B;
DE   AltName: Full=Stathmin clone XO20;
DE   Flags: Fragment;
GN   Name=stmn1-b;
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).
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: From unphosphorylated forms to highly phosphorylated ones in the
CC       mature egg, followed by progressive dephosphorylation from the mid-
CC       blastula to the tailbud stage.
CC   -!- SIMILARITY: Belongs to the stathmin family. {ECO:0000305}.
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DR   EMBL; X71432; CAA50563.1; -; mRNA.
DR   PIR; I51705; I51705.
DR   AlphaFoldDB; Q09005; -.
DR   SMR; Q09005; -.
DR   Proteomes; UP000186698; Genome assembly.
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; IPR000956; Stathmin_fam.
DR   InterPro; IPR036002; Stathmin_sf.
DR   PANTHER; PTHR10104; PTHR10104; 1.
DR   Pfam; PF00836; Stathmin; 1.
DR   PRINTS; PR00345; STATHMIN.
DR   SUPFAM; SSF101494; SSF101494; 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..71
FT                   /note="Stathmin-1-B"
FT                   /id="PRO_0000182395"
FT   DOMAIN          1..71
FT                   /note="SLD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00998"
FT   COILED          <1..67
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   71 AA;  8474 MW;  6A0AD840C77AAE09 CRC64;
     KREHEKEVLQ KAIEENNNFS KMAEEKLTTK MEAIKENREA QMAAKLERLR EKDKKLEEIR
     KGKECKEPSE D