ID   LASP1_PONAB             Reviewed;         261 AA.
AC   Q5R5W0;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=LIM and SH3 domain protein 1;
DE            Short=LASP-1;
GN   Name=LASP1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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; CR860742; CAH92856.1; -; mRNA.
DR   RefSeq; NP_001126670.1; NM_001133198.1.
DR   AlphaFoldDB; Q5R5W0; -.
DR   SMR; Q5R5W0; -.
DR   STRING; 9601.ENSPPYP00000009551; -.
DR   Ensembl; ENSPPYT00000035487; ENSPPYP00000039924; ENSPPYG00000008500.
DR   GeneID; 100173670; -.
DR   KEGG; pon:100173670; -.
DR   CTD; 3927; -.
DR   eggNOG; KOG1702; Eukaryota.
DR   GeneTree; ENSGT00940000154775; -.
DR   HOGENOM; CLU_026811_0_1_1; -.
DR   InParanoid; Q5R5W0; -.
DR   OrthoDB; 1549538at2759; -.
DR   Proteomes; UP000001595; Chromosome 17.
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; 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: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..261
FT                   /note="LIM and SH3 domain protein 1"
FT                   /id="PRO_0000223475"
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          202..261
FT                   /note="SH3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
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"
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   261 AA;  29747 MW;  94E4143EBB369B8F CRC64;
     MNPNCARCGK IVYPTEKVNC LDKFWHKACF HCETCKMTLN MKNYKGYEKK PYCNAHYPKQ
     SFTMVADTPE NLRLKQQSEL QSQVRYKEEF EKNKGKGFSV VADTPELQRI KKTQDQISNI
     KYHEEFEKSR MGPSGGEGME PERRDSQDSS SYRRPLEQQQ PHHIPTSAPV YQQPQQQPVA
     QSYGGYKEPA APVSIQRSAP GGGGKRYRAV YDYSAADEDE VSFQDGDTIV NVQQIDDGWM
     YGTVERTGDT GMLPANYVEA I