ID G5EFG1_CAEEL Unreviewed; 684 AA.
AC G5EFG1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=PDZ and LIM domain protein Zasp {ECO:0000313|EMBL:CAJ43909.1};
GN Name=alp-1 {ECO:0000313|EMBL:CAJ43909.1,
GN ECO:0000313|WormBase:T11B7.4e};
GN ORFNames=CELE_T11B7.4 {ECO:0000313|EMBL:CAJ43909.1}, T11B7.4
GN {ECO:0000313|WormBase:T11B7.4e};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAJ43909.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAJ43909.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAJ43909.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- SIMILARITY: Belongs to the paxillin family.
CC {ECO:0000256|ARBA:ARBA00005813}.
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DR EMBL; BX284604; CAJ43909.1; -; Genomic_DNA.
DR RefSeq; NP_001040987.1; NM_001047522.2.
DR AlphaFoldDB; G5EFG1; -.
DR SMR; G5EFG1; -.
DR PeptideAtlas; G5EFG1; -.
DR EnsemblMetazoa; T11B7.4e.1; T11B7.4e.1; WBGene00001132.
DR GeneID; 177701; -.
DR AGR; WB:WBGene00001132; -.
DR WormBase; T11B7.4e; CE39401; WBGene00001132; alp-1.
DR OrthoDB; 370973at2759; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001132; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or tissues.
DR ExpressionAtlas; G5EFG1; baseline.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0031941; C:filamentous actin; IBA:GO_Central.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0055120; C:striated muscle dense body; IDA:WormBase.
DR GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008340; P:determination of adult lifespan; IMP:WormBase.
DR GO; GO:0061061; P:muscle structure development; IBA:GO_Central.
DR GO; GO:0043050; P:nematode pharyngeal pumping; IMP:WormBase.
DR CDD; cd09455; LIM1_Enigma_like_1; 1.
DR CDD; cd09461; LIM3_Enigma_like_1; 1.
DR CDD; cd09360; LIM_ALP_like; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR006643; Zasp-like_motif.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR24214; PDZ AND LIM DOMAIN PROTEIN ZASP; 1.
DR PANTHER; PTHR24214:SF38; PDZ AND LIM DOMAIN PROTEIN ZASP; 1.
DR Pfam; PF00412; LIM; 4.
DR SMART; SM00132; LIM; 4.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00735; ZM; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 4.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW ProRule:PRU00125}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW Proteomics identification {ECO:0007829|EPD:G5EFG1,
KW ECO:0007829|PeptideAtlas:G5EFG1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT DOMAIN 5..84
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 218..278
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 570..629
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT DOMAIN 630..684
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000259|PROSITE:PS50023"
FT REGION 315..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 684 AA; 74594 MW; BDD621B487DB076B CRC64;
MERVTVRMAR SDRRTPWGFG VTEAPDGAVL IVNVIGGSLA DRAGLRNGDV VDRLEDLDNL
DINAVDRLLV TAHEKIELIV TRQPSGAATR IWRPEVTENT GPGQDQTPYR VNLQHSSDTR
PPQGFNNSAL PFETDQRVKH MQYNSPLGIY SDKSAAEQYV QQTQGLGDNS GARAAAQRQD
EPAYLRSETL RLLKEQEHGS AGGAGTTLSN HPNPSGLPVC FMCTRPILGV MARAAGKNLH
GDCLSCATCG NSLRNVGHHF IEDKFYCDIH GTQRKHGGRP GMDPNIFVKS SPTAAQPVHI
QDSPRAAYHP QVNTARPVSV SPAPSAGSKT VTTHYHTPKT QGILSPGQRG VPTAAFGADL
SKSVTYGGGV GPGGTHYDSN RLSPAPSQYS TQSRNQSQQH YQQHVVQAPP PVPSNPPPSN
DTTAEDSRNF LASRLGQVMI DENKKAGGSN GSSQHHNQQG SSYTKTSFER TTTETRPQQN
TGAPRAGDFR GTGHLTTTTT TQQNGGRAPF CESCKQQIRG AFVLATGKSW CPEHFVCANS
SCRRRLLECG FVEEDGQKFC ESCFEQHIAP RCNKCSKPII SDCLNALQKK WHPTCFTCAH
CQKPFGNSAF YLEQGLPYCE QDWNALFTTK CVSCRYPIEA GDRWVEALGN AFHSNCFTCA
RCNHNLEGES FFAKNGQPFC RLHA
//
