SPTN1_CAPHI
ID SPTN1_CAPHI Reviewed; 46 AA.
AC P85985;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 25.
DE RecName: Full=Spectrin alpha chain, non-erythrocytic 1;
DE AltName: Full=Alpha-II spectrin {ECO:0000250|UniProtKB:Q13813};
DE AltName: Full=Fodrin alpha chain {ECO:0000250|UniProtKB:Q13813};
DE Flags: Fragments;
GN Name=SPTAN1;
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 {ECO:0000250|UniProtKB:Q13813}.
CC -!- SUBUNIT: Associates with the gamma-tubulin complex in brain, but not in
CC kidney, liver, sperm, or uterus. Like erythrocyte spectrin, the
CC spectrin-like proteins are capable of forming dimers which can further
CC associate to tetramers. Interacts with isoform 1 of ACP1. Interacts
CC with CALM and EMD (By similarity). Interacts (via C-terminal spectrin
CC repeats) with TRPC4 (By similarity). Identified in a complex with
CC ACTN4, CASK, IQGAP1, MAGI2, NPHS1 and SPTBN1 (By similarity). Interacts
CC with CLN3; this interaction regulates the fodrin localization at the
CC plasma membrane (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q13813}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q13813}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q13813}. Note=Expressed along the cell membrane
CC in podocytes and presumptive tubule cells during glomerulogenesis and
CC is expressed along lateral cell margins in tubule cells. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the spectrin family. {ECO:0000255}.
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; P85985; -.
DR SMR; P85985; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Actin capping; Actin-binding; Calcium; Calmodulin-binding; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Reference proteome; Repeat.
FT CHAIN <1..>46
FT /note="Spectrin alpha chain, non-erythrocytic 1"
FT /id="PRO_0000349155"
FT REPEAT <1..5
FT /note="Spectrin 6"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT REPEAT 7..>14
FT /note="Spectrin 7"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT REPEAT <15..20
FT /note="Spectrin 13"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT REPEAT 21..>26
FT /note="Spectrin 14"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT REPEAT <27..>35
FT /note="Spectrin 19"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT REPEAT 39..>46
FT /note="Spectrin 22"
FT /evidence="ECO:0000250|UniProtKB:Q13813"
FT NON_CONS 14..15
FT /evidence="ECO:0000305"
FT NON_CONS 26..27
FT /evidence="ECO:0000305"
FT NON_CONS 35..36
FT /evidence="ECO:0000305"
FT NON_TER 1
FT NON_TER 46
SQ SEQUENCE 46 AA; 5446 MW; 0F8577FA5A98CC51 CRC64;
AQLADSFHLQ QFFRSQLLGS AHEVQRLAQF VEHWKKVEDL FLTFAK
