LASP1_BOVIN
ID LASP1_BOVIN Reviewed; 260 AA.
AC Q3B7M5;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=LIM and SH3 domain protein 1;
DE Short=LASP-1;
GN Name=LASP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Reticulocyte;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in the regulation of dynamic actin-
CC based, cytoskeletal activities. Agonist-dependent changes in LASP1
CC phosphorylation may also serve to regulate actin-associated ion
CC transport activities, not only in the parietal cell but also in certain
CC other F-actin-rich secretory epithelial cell types (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with F-actin (By similarity). Interacts with
CC ANKRD54. Interacts with KBTBD10 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Note=Associated with the F-actin rich
CC cortical cytoskeleton. {ECO:0000250}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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DR EMBL; BC107542; AAI07543.1; -; mRNA.
DR RefSeq; NP_001030471.1; NM_001035394.1.
DR AlphaFoldDB; Q3B7M5; -.
DR SMR; Q3B7M5; -.
DR STRING; 9913.ENSBTAP00000040793; -.
DR PaxDb; Q3B7M5; -.
DR PeptideAtlas; Q3B7M5; -.
DR PRIDE; Q3B7M5; -.
DR Ensembl; ENSBTAT00000043205; ENSBTAP00000040793; ENSBTAG00000030587.
DR GeneID; 532851; -.
DR KEGG; bta:532851; -.
DR CTD; 3927; -.
DR VEuPathDB; HostDB:ENSBTAG00000030587; -.
DR VGNC; VGNC:30798; LASP1.
DR eggNOG; KOG1702; Eukaryota.
DR GeneTree; ENSGT00940000154775; -.
DR HOGENOM; CLU_026811_0_1_1; -.
DR InParanoid; Q3B7M5; -.
DR OMA; QIEYVEY; -.
DR OrthoDB; 1549538at2759; -.
DR TreeFam; TF319104; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000030587; Expressed in omental fat pad and 106 other tissues.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR CDD; cd11934; SH3_Lasp1_C; 1.
DR InterPro; IPR035630; Lasp1_SH3.
DR InterPro; IPR000900; Nebulin_repeat.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF00880; Nebulin; 2.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00227; NEBU; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS51216; NEBULIN; 2.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Actin-binding; Cytoplasm; Cytoskeleton; Ion transport;
KW LIM domain; Metal-binding; Methylation; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain; Transport; Zinc.
FT CHAIN 1..260
FT /note="LIM and SH3 domain protein 1"
FT /id="PRO_0000223474"
FT DOMAIN 5..56
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REPEAT 61..95
FT /note="Nebulin 1"
FT REPEAT 97..131
FT /note="Nebulin 2"
FT DOMAIN 201..260
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 123..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 42
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 68
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 75
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 99
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 112
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61792"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
SQ SEQUENCE 260 AA; 29677 MW; 6572DF3BF3ADA430 CRC64;
MNPNCARCCK IVYPTEKVNC LDKFWHKACF HCETCKMTLN MKNYKGYEKK PYCNAHYPKQ
SFTMVADTPE NLRLKQQSEL QSQVRYKEEF EKNKGKGFSV VADTPELQRI KKTQDQISNI
KYHEEFEKSR MGPSGGEGLE CERRDPQESS YRRPQEQQQP HHIPASTPVY QQPQQQPAAQ
SYGGYKEPAA PASIQRSAPG GGGKRYRAVY DYSAADEDEV SFQDGDTIVN VQQIDDGWMY
GTVERTGDTG MLPANYVEAI
