LASP1_RABIT
ID LASP1_RABIT Reviewed; 263 AA.
AC O77506;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=LIM and SH3 domain protein 1;
DE Short=LASP-1;
DE AltName: Full=40 kDa phosphoprotein;
DE Short=pp40;
GN Name=LASP1;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 128-133, PHOSPHORYLATION,
RP AND TISSUE SPECIFICITY.
RC STRAIN=New Zealand white; TISSUE=Gastric mucosa;
RX PubMed=9688835; DOI=10.1152/ajpcell.1998.275.1.c56;
RA Chew C.S., Parente J.A. Jr., Zhou C.-J., Baranco E., Chen X.;
RT "Lasp-1 is a regulated phosphoprotein within the cAMP signaling pathway in
RT the gastric parietal cell.";
RL Am. J. Physiol. 275:C56-C67(1998).
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 -!- TISSUE SPECIFICITY: Widely expressed with highest levels in mucosal
CC tissues throughout the gastrointestinal tract as well as in heart,
CC lung, liver, kidney, adrenal and smooth muscle. Lowest level is
CC observed in skeletal muscle. {ECO:0000269|PubMed:9688835}.
CC -!- PTM: Phosphorylated on serine residues after stimulation with
CC histamine. {ECO:0000269|PubMed:9688835}.
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DR EMBL; AF017438; AAC39264.1; -; mRNA.
DR RefSeq; NP_001076247.1; NM_001082778.1.
DR AlphaFoldDB; O77506; -.
DR SMR; O77506; -.
DR STRING; 9986.ENSOCUP00000022303; -.
DR iPTMnet; O77506; -.
DR PRIDE; O77506; -.
DR GeneID; 100009568; -.
DR KEGG; ocu:100009568; -.
DR CTD; 3927; -.
DR eggNOG; KOG1702; Eukaryota.
DR InParanoid; O77506; -.
DR OrthoDB; 1549538at2759; -.
DR Proteomes; UP000001811; Unplaced.
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: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 1: Evidence at protein level;
KW Acetylation; Actin-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Ion transport; LIM domain; Metal-binding;
KW Methylation; Phosphoprotein; Reference proteome; Repeat; SH3 domain;
KW Transport; Zinc.
FT CHAIN 1..263
FT /note="LIM and SH3 domain protein 1"
FT /id="PRO_0000223476"
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 204..263
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 123..209
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 169..185
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"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14847"
SQ SEQUENCE 263 AA; 29935 MW; F7FBD59E1CB88193 CRC64;
MNPNCARCGK IVYPTEKVNC LDKFWHKACF HCETCKMTLN MKNYKGYEKK PYCNAHYPKQ
SFTMVADTPE NLRLKQQSEL QSQVRYKEEF EKNKGRGFSV VADTPELQRI KKTQDQISNI
KYHEEFEKSR MGPSGGEGAE PERRDSQDSS NYRRPPEQQQ PPQPHHIPTS TPAYQQPQPQ
QVAQSYGYKE PAAPVSTQRG APGGGGKRYR AVFDYSAADE DEVSFQDGDT IVNVQQIDDG
WMYGTVERTG DTGMLPANYV EAI
