GRDN_CAEEL
ID GRDN_CAEEL Reviewed; 1319 AA.
AC F3Y5P4; F3Y5P5; Q9XXR1;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Girdin homolog {ECO:0000312|WormBase:Y51A2D.15a};
DE AltName: Full=Coiled-coil domain-containing protein grdn-1 {ECO:0000305};
GN Name=grdn-1 {ECO:0000303|PubMed:27623382, ECO:0000312|WormBase:Y51A2D.15a};
GN ORFNames=Y51A2D.15 {ECO:0000312|WormBase:Y51A2D.15a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DOMAIN, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF SER-1095.
RX PubMed=27623382; DOI=10.1016/j.devcel.2016.07.013;
RA Nechipurenko I.V., Olivier-Mason A., Kazatskaya A., Kennedy J.,
RA McLachlan I.G., Heiman M.G., Blacque O.E., Sengupta P.;
RT "A Conserved role for girdin in basal body positioning and ciliogenesis.";
RL Dev. Cell 38:493-506(2016).
CC -!- FUNCTION: Scaffolding protein that plays a role in ciliogenesis, cilium
CC positioning and dendrite anchoring in sensory amphid neurons including
CC AWB, AWA, AWC, ADL and ASI and the phasmid neurons PHA and PHB. Its
CC role in cilium positioning may be through regulation of the
CC localization of cell adhesion proteins such as the apical junction
CC protein ajm-1, and the ciliary scaffolding protein Rootletin/che-10.
CC {ECO:0000269|PubMed:27623382}.
CC -!- SUBCELLULAR LOCATION: [Isoform a]: Cytoplasm, cytoskeleton, cilium
CC basal body {ECO:0000269|PubMed:27623382}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:27623382}. Note=Enriched at the proximal ends of
CC centrioles. {ECO:0000269|PubMed:27623382}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=a {ECO:0000312|WormBase:Y51A2D.15a};
CC IsoId=F3Y5P4-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y51A2D.15b};
CC IsoId=F3Y5P4-2; Sequence=VSP_058703, VSP_058704;
CC Name=c {ECO:0000312|WormBase:Y51A2D.15c};
CC IsoId=F3Y5P4-3; Sequence=VSP_058702;
CC -!- DEVELOPMENTAL STAGE: [Isoform a]: Broadly expressed during
CC embryogenesis with high expression at the presumptive nose during the
CC 1.5-fold stage of embryogenesis. Expressed in AWB sensory neurons in
CC larvae and in PHA/PHB tail neurons at the L1 stage of larval
CC development. {ECO:0000269|PubMed:27623382}.
CC -!- DOMAIN: The C-terminal domain is required for localization to the
CC cilium basal body and role in ciliogenesis.
CC {ECO:0000269|PubMed:27623382}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal with few malformed larvae that
CC develop to the L1 stage of larval development.
CC {ECO:0000269|PubMed:27623382}.
CC -!- SIMILARITY: Belongs to the CCDC88 family. {ECO:0000305}.
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DR EMBL; BX284605; CAA16402.2; -; Genomic_DNA.
DR EMBL; BX284605; CCA65668.1; -; Genomic_DNA.
DR EMBL; BX284605; CCA65669.1; -; Genomic_DNA.
DR PIR; T27074; T27074.
DR RefSeq; NP_001256816.1; NM_001269887.1. [F3Y5P4-1]
DR RefSeq; NP_001256817.1; NM_001269888.1.
DR RefSeq; NP_001256818.1; NM_001269889.1. [F3Y5P4-3]
DR AlphaFoldDB; F3Y5P4; -.
DR SMR; F3Y5P4; -.
DR DIP; DIP-26318N; -.
DR IntAct; F3Y5P4; 1.
DR STRING; 6239.Y51A2D.15a; -.
DR EPD; F3Y5P4; -.
DR PaxDb; F3Y5P4; -.
DR PeptideAtlas; F3Y5P4; -.
DR EnsemblMetazoa; Y51A2D.15a.1; Y51A2D.15a.1; WBGene00013082. [F3Y5P4-1]
DR EnsemblMetazoa; Y51A2D.15b.1; Y51A2D.15b.1; WBGene00013082. [F3Y5P4-2]
DR EnsemblMetazoa; Y51A2D.15c.1; Y51A2D.15c.1; WBGene00013082. [F3Y5P4-3]
DR GeneID; 190137; -.
DR KEGG; cel:CELE_Y51A2D.15; -.
DR UCSC; Y51A2D.15; c. elegans.
DR CTD; 190137; -.
DR WormBase; Y51A2D.15a; CE46096; WBGene00013082; grdn-1. [F3Y5P4-1]
DR WormBase; Y51A2D.15b; CE32531; WBGene00013082; grdn-1. [F3Y5P4-2]
DR WormBase; Y51A2D.15c; CE46015; WBGene00013082; grdn-1. [F3Y5P4-3]
DR eggNOG; KOG4643; Eukaryota.
DR GeneTree; ENSGT00940000168948; -.
DR InParanoid; F3Y5P4; -.
DR OMA; YRKLDSC; -.
DR OrthoDB; 262562at2759; -.
DR PhylomeDB; F3Y5P4; -.
DR PRO; PR:F3Y5P4; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00013082; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0003391; P:amphid sensory organ dendrite retrograde extension; IMP:UniProtKB.
DR GO; GO:1905349; P:ciliary transition zone assembly; IMP:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0030705; P:cytoskeleton-dependent intracellular transport; IBA:GO_Central.
DR GO; GO:0045724; P:positive regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:1903861; P:positive regulation of dendrite extension; IMP:UniProtKB.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:UniProtKB.
DR GO; GO:1903566; P:positive regulation of protein localization to cilium; IMP:UniProtKB.
DR GO; GO:1904491; P:protein localization to ciliary transition zone; IMP:UniProtKB.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR043936; HOOK_N.
DR Pfam; PF19047; HOOK_N; 1.
DR PROSITE; PS50021; CH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Reference proteome.
FT CHAIN 1..1319
FT /note="Girdin homolog"
FT /evidence="ECO:0000305"
FT /id="PRO_0000438682"
FT DOMAIN 6..118
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 166..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1112..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1289..1308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 141..173
FT /evidence="ECO:0000255"
FT COILED 218..690
FT /evidence="ECO:0000255"
FT COILED 732..1096
FT /evidence="ECO:0000255"
FT COMPBIAS 189..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..166
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_058702"
FT VAR_SEQ 1144..1222
FT /note="TNEDVDHLPPTCSSSDDHDVISPDFSAKNPLLRSRNDFMGGSVRSPRRYGND
FT HDGHIYTSPFLPPRVPIRNSPMTSSLR -> NSTCSVSTSSDSTPDECPLHGSRSFSKI
FT SALKIQSSPSPSSSFSRFLSLRRTAKPSLLQGAYTNPNVRKMIDYHYNCSD (in
FT isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058703"
FT VAR_SEQ 1223..1319
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_058704"
FT MUTAGEN 1095
FT /note="S->A: Ciliary defects in the AWB sensory neuron."
FT /evidence="ECO:0000269|PubMed:27623382"
SQ SEQUENCE 1319 AA; 153656 MW; 006BB21A6C09890C CRC64;
MKEKHENWSH PLAFWLCDCA AIIPNPATQN FAKNDFLDGL LMLNLMKFIN PHFSENEKNG
QSLYEELLNQ ISQFYEKNLD QVIVCKMPEI SILESSGEID EITFEELKKL LLLLLGCAIQ
SDHKKVFVDR ITGFDQTIQA ELAACIQKLT ESDEIVQNLE DFERRKMKET DEVGGGGGSI
EDVDSDDMES STTSSSNGEI AIKQQDQSFL MSRSTSPTSE LRHQTLQIAN LQHEMRQMRT
QAENRDEECQ KLELDNEEKA QKIKILENER LKLVDFKKKW KSVNDDLQEA NCKIEKLQNL
VGIEKKYREA RDGKELYKSK YDIVVKKNLE MEETITTLEK NLKTLQMEMK EKFGVEDNLQ
RMRNTIDDLE AEISKKNLEI EDFLDEKHRM DREIKELKEI VHQMEVPSTT TTPRIMDSLA
DQLENAKQDE FEMMKAEIRK LRAQTEGATP ETTIIQCNQD LDTLRSQLST EQHQTAQLHL
EIQKMQVEKE QIDGNMERIG IELEEMSAQV ENLNLERDEA VKQLLEARRK FGEFQMGQSR
DLEEKWSKEV EKSNKISKKC EILEEKLQES DFLLAKSRDE AKKLQFELDE ALEETSHVTR
SLSSEKNTLK AKLLELQDQV EAQTLELLNQ KNCGKRLEDR DQMISNLHNL KNELENDLKT
CQTQLELESK KLQRLREDLV LEKSRRADLI GRIHSLCTTL SLNGANFEKI NNDDELIDNI
DDIMMNALVA VKRERDDLRI QGNQQIQELH DLKRDIEKLR RSESESLNES DDRVRELTRE
NMHTKEQVFM LQEKLRELNL ELSTKNDEID MVKASIEELN RNSTASCTSN AEIARLQVSI
RNSQIQEDLV KQENTKLRDE LQEMQKMSKK RSQNLDELEN MHKTLLVDHS RLQQLHNLLT
RDYDEAKKES MELRQKVQNI PRQQAVFMNA NIRELEAKLS EEISRREQLE KEHKMCRIHC
ENLRRDITEL VQTRDELSLE LRRAHDTCHN KNNQIDELKK QLNQKISEVN KLSSKIEALS
QLNRTYNEEN RNLSRQLEIL LTQNKELLQR ALHDKDQYHL EMKDFQDQLS ALRRHKEKLE
DKIMDQYRTM ENKKSTPERK QPLVKRAAKA LINRRRATSN GGSTTEDSSV YSADERSSPP
LAGTNEDVDH LPPTCSSSDD HDVISPDFSA KNPLLRSRND FMGGSVRSPR RYGNDHDGHI
YTSPFLPPRV PIRNSPMTSS LRSRPPPPPY NRSPAHKIEQ NSSFFEPIAH STPNSSILEE
RRVVGEGEKR ELVRDKEERI DKTLSYYENV NLPQNPPDLP ENSDLKPNES TIWHEYGCV
