KY_CAEEL
ID KY_CAEEL Reviewed; 723 AA.
AC G5EF51; A0A131MD24;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Lim and transglutaminase domain protein ltd-1 {ECO:0000305};
DE AltName: Full=Kyphoscoliosis inactive peptidase homolog ltd-1 {ECO:0000305};
GN Name=ltd-1 {ECO:0000303|PubMed:12204272, ECO:0000312|WormBase:K02C4.4a};
GN ORFNames=K02C4.4 {ECO:0000312|WormBase:K02C4.4a};
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|EMBL:AAN09795.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAN09795.1};
RX PubMed=12204272; DOI=10.1016/s0925-4773(02)00182-x;
RA Vargas J.D., Culetto E., Ponting C.P., Miguel-Aliaga I., Davies K.E.,
RA Sattelle D.B.;
RT "Cloning and developmental expression analysis of ltd-1, the Caenorhabditis
RT elegans homologue of the mouse kyphoscoliosis (ky) gene.";
RL Mech. Dev. 117:289-292(2002).
RN [2] {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).
CC -!- FUNCTION: Cytoskeleton-associated protein (Probable). May play a role
CC in hypodermal cell development (Probable). {ECO:0000305,
CC ECO:0000305|PubMed:12204272}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12204272}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:K02C4.4a};
CC IsoId=G5EF51-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:K02C4.4b};
CC IsoId=G5EF51-2; Sequence=VSP_061191;
CC -!- TISSUE SPECIFICITY: Expressed in the Y and U rectal epithelial cells,
CC in marginal cells of the terminal bulb and isthmus of the pharynx (at
CC protein level). {ECO:0000269|PubMed:12204272}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development (at protein
CC level). First expressed in two-fold stage embryos (at protein level)
CC (PubMed:12204272). During embryogenesis, expressed in the apical
CC regions of the dorsal and ventral hypodermis in tightly organized
CC circumferential filament bundles (at protein level) (PubMed:12204272).
CC Expressed in seam cells in embryos and at the larval stages (at protein
CC level) (PubMed:12204272). In L1 stage larvae, expressed in the apical
CC junction between hypodermal cells hyp 5, hyp 6 and hyp 7, and between
CC the seam cells and the P blast cells in the ventral midline (at protein
CC level) (PubMed:12204272). In L2 stage larvae, expressed in the Y and U
CC rectal epithelial cells (at protein level) (PubMed:12204272). In L3
CC stage larvae, expressed in the pharynx, socket cells, the processes
CC that link socket cells to the amphid, in marginal cells of the terminal
CC bulb and at the junction between the pharynx lumen and the hypodermis
CC (at protein level) (PubMed:12204272). In L4 stage larvae, expressed in
CC longitudinal filaments within the cytoplasm linking both extremities of
CC the elongating seam cells and in the alae formed by their fusion (at
CC protein level) (PubMed:12204272). {ECO:0000269|PubMed:12204272}.
CC -!- SIMILARITY: Belongs to the transglutaminase-like superfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Unlike the mammalian homolog KY, the residues forming the
CC catalytic triad in the putative transglutaminase-like domain of ltd-1
CC are not conserved, therefore it is likely that the protein lacks
CC protease activity. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF489839; AAN09795.1; -; mRNA.
DR EMBL; BX284602; CAA87787.2; -; Genomic_DNA.
DR EMBL; BX284602; CZR14489.1; -; Genomic_DNA.
DR PIR; T23237; T23237.
DR RefSeq; NP_495697.2; NM_063296.3.
DR AlphaFoldDB; G5EF51; -.
DR STRING; 6239.K02C4.4; -.
DR EPD; G5EF51; -.
DR PaxDb; G5EF51; -.
DR PeptideAtlas; G5EF51; -.
DR EnsemblMetazoa; K02C4.4a.1; K02C4.4a.1; WBGene00003089. [G5EF51-1]
DR EnsemblMetazoa; K02C4.4b.1; K02C4.4b.1; WBGene00003089. [G5EF51-2]
DR GeneID; 174301; -.
DR KEGG; cel:CELE_K02C4.4; -.
DR CTD; 174301; -.
DR WormBase; K02C4.4a; CE32687; WBGene00003089; ltd-1. [G5EF51-1]
DR WormBase; K02C4.4b; CE51496; WBGene00003089; ltd-1. [G5EF51-2]
DR eggNOG; KOG1700; Eukaryota.
DR eggNOG; KOG4575; Eukaryota.
DR GeneTree; ENSGT00940000172737; -.
DR HOGENOM; CLU_009339_1_0_1; -.
DR InParanoid; G5EF51; -.
DR OMA; VAIHCAR; -.
DR OrthoDB; 936224at2759; -.
DR PhylomeDB; G5EF51; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00003089; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; G5EF51; baseline and differential.
DR GO; GO:0005911; C:cell-cell junction; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0055120; C:striated muscle dense body; HDA:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061061; P:muscle structure development; ISS:WormBase.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002931; Transglutaminase-like.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 1.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; LIM domain; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..723
FT /note="Lim and transglutaminase domain protein ltd-1"
FT /id="PRO_0000453730"
FT DOMAIN 5..72
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT VAR_SEQ 1..234
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_061191"
SQ SEQUENCE 723 AA; 83080 MW; ADFB3F97B79A6BED CRC64;
MNSKQHCNRC GKQVYPTDKV GPLKDSTFFH QGCFKCYICG TRLALKTYCN NRNDINDKEV
YCSNHVPIAG PHDLPMASTN GSGKNLENNN HVKNGNWIDA GLSDMKIAHA MKATQVARPY
PKISHEGAKY VVDYDTQTRL ELLHRKDEDD LYESFQDKRV REAEEFEKEN TEEWEKALAE
FAKKYEKGQS NMKKDDLIRQ LTIKREKKLE TLHTKRKERE RHQTAELVDR QAKEMLELFK
ASRSEYSNLQ YPSTPPPPVP PSCSKREIYT TTDYFSSIDE VAIHCARNEV ASFTDLIRTL
SSGARSDVDV ARAIYRWITI KNLNTMIFDD SIQNDTPMGL LRGIKYGTES YHVLFKRLCS
YAGLHCVVIK GFSKSAGYQP GYSFDDHRFR NTWNAVFLDG SWRFVQCNWG ARHLVNAKDG
SHEAKTDGNL RYEYDDHYFM TDSEEFIYEF FPSDHAWQLL PRPLSLLQFE RIPFVRSLFF
KYNLSFIDNK LESTVYTDKS GAASISIRLP PKGDSLIFHY NLKFFDSEEN TISGMSLKRF
VMQSVTEDVV TFRVHAPSTR PLLLDIFANS VSSGAYLTGQ PIKFKSVCKF KVVCESLQVI
MVPLPECASG EWGPAKATRL FGLLPISHPD AIINTGRYVE IRFRMTRPLS EFVASLHRNR
TDDRALQACT RSALKGDMVY IQIEFPGEGQ YGLDIYTRQD DQLINGKQLL THCCKYLIHS
RNC
