ID   SPTB2_CAPHI             Reviewed;          31 AA.
AC   P85986;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Spectrin beta chain, non-erythrocytic 1;
DE   Flags: Fragments;
GN   Name=SPTBN1;
OS   Capra hircus (Goat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Capra.
OX   NCBI_TaxID=9925;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBUNIT.
RC   TISSUE=Brain;
RX   PubMed=20564227; DOI=10.1002/jcb.22647;
RA   Thomas N.E., Shashikala S., Sengupta S.;
RT   "Cytoplasmic gamma-tubulin complex from brain contains nonerythroid
RT   spectrin.";
RL   J. Cell. Biochem. 110:1334-1341(2010).
CC   -!- FUNCTION: Fodrin, which seems to be involved in secretion, interacts
CC       with calmodulin in a calcium-dependent manner and is thus candidate for
CC       the calcium-dependent movement of the cytoskeleton at the membrane.
CC       Plays a critical role in central nervous system development and
CC       function. {ECO:0000250|UniProtKB:Q01082}.
CC   -!- SUBUNIT: Interacts with ANK2 (By similarity). Interacts with CPNE4 (via
CC       VWFA domain). Like erythrocyte spectrin, the spectrin-like proteins are
CC       capable to form dimers which can further associate to tetramers.
CC       Associates with the gamma-tubulin complex in brain, but not in kidney,
CC       liver, sperm, or uterus (PubMed:20564227). Interacts with CAMSAP1. Can
CC       form heterodimers with SPTAN1. {ECO:0000250|UniProtKB:Q01082,
CC       ECO:0000250|UniProtKB:Q62261, ECO:0000269|PubMed:20564227}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:Q62261}. Cytoplasm, myofibril, sarcomere, M line
CC       {ECO:0000250|UniProtKB:Q62261}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q01082}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q01082}. Note=Colocalizes with ANK2 in a
CC       distinct intracellular compartment of neonatal cardiomyocytes.
CC       {ECO:0000250|UniProtKB:Q62261}.
CC   -!- SIMILARITY: Belongs to the spectrin family.
CC       {ECO:0000250|UniProtKB:Q62261}.
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   AlphaFoldDB; P85986; -.
DR   Proteomes; UP000291000; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005200; F:structural constituent of cytoskeleton; ISS:UniProtKB.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR   GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR   GO; GO:0021556; P:central nervous system formation; ISS:UniProtKB.
PE   1: Evidence at protein level;
KW   Actin capping; Actin-binding; Calmodulin-binding; Cell membrane; Cytoplasm;
KW   Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat.
FT   CHAIN           <1..>31
FT                   /note="Spectrin beta chain, non-erythrocytic 1"
FT                   /id="PRO_0000349156"
FT   REPEAT          <1..>10
FT                   /note="Spectrin 3"
FT                   /evidence="ECO:0000250|UniProtKB:Q62261"
FT   REPEAT          <11..>19
FT                   /note="Spectrin 6"
FT                   /evidence="ECO:0000250|UniProtKB:Q62261"
FT   REPEAT          <20..>31
FT                   /note="Spectrin 15"
FT                   /evidence="ECO:0000250|UniProtKB:Q62261"
FT   MOD_RES         27
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62261"
FT   NON_CONS        10..11
FT                   /evidence="ECO:0000305"
FT   NON_CONS        19..20
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         31
SQ   SEQUENCE   31 AA;  3581 MW;  EFB67932199E15B5 CRC64;
     VLLLSQDYGK YKEVAELTRT QILAASYELH K