ID A0A2R8Z9S7_PANPA Unreviewed; 261 AA.
AC A0A2R8Z9S7;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=LIM and SH3 domain protein 1 {ECO:0000256|ARBA:ARBA00020662};
GN Name=LASP1 {ECO:0000313|Ensembl:ENSPPAP00000001616.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000001616.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000001616.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000001616.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00025477}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC {ECO:0000256|ARBA:ARBA00004544}.
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DR EMBL; AJFE02030454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02030455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02030456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02030457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02030458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02030459; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02030460; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02030461; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003809887.1; XM_003809839.2.
DR AlphaFoldDB; A0A2R8Z9S7; -.
DR SMR; A0A2R8Z9S7; -.
DR STRING; 9597.ENSPPAP00000001616; -.
DR Ensembl; ENSPPAT00000007919.1; ENSPPAP00000001616.1; ENSPPAG00000007025.1.
DR GeneID; 100995933; -.
DR KEGG; pps:100995933; -.
DR CTD; 3927; -.
DR GeneTree; ENSGT00940000154775; -.
DR OMA; KSRMGTP; -.
DR OrthoDB; 4243at2759; -.
DR Proteomes; UP000240080; Chromosome 17.
DR Bgee; ENSPPAG00000007025; Expressed in adult mammalian kidney and 6 other cell types or tissues.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR CDD; cd09447; LIM_LASP; 1.
DR CDD; cd11934; SH3_Lasp1_C; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 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 PANTHER; PTHR46218; LASP; 1.
DR PANTHER; PTHR46218:SF2; LIM AND SH3 DOMAIN PROTEIN 1; 1.
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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF50044; SH3-domain; 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 4: Predicted;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 3..63
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 202..261
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 111..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 261 AA; 29717 MW; 3B89B988605B3639 CRC64;
MNPNCARCGK IVYPTEKVNC LDKFWHKACF HCETCKMTLN MKNYKGYEKK PYCNAHYPKQ
SFTMVADTPE NLRLKQQSEL QSQVRYKEEF EKNKGKGFSV VADTPELQRI KKTQDQISNI
KYHEEFEKSR MGPSGGEGME PERRDSQDGS SYRRPLEQQQ PHHIPTSAPV YQQPQQQPVA
QSYGGYKEPA APVSIQRSAP GGGGKRYRAV YDYSAADEDE VSFQDGDTIV NVQQIDDGWM
YGTVERTGDT GMLPANYVEA I
//
