ID ZIG6_CAEEL Reviewed; 243 AA.
AC Q22125;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 27-MAR-2024, entry version 155.
DE RecName: Full=Zwei Ig domain protein zig-6 {ECO:0000303|PubMed:11809975};
DE AltName: Full=2 Ig domain protein zig-6 {ECO:0000303|PubMed:11809975};
DE Flags: Precursor;
GN Name=zig-6 {ECO:0000312|WormBase:T03G11.8};
GN ORFNames=T03G11.8 {ECO:0000312|WormBase:T03G11.8};
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 TISSUE SPECIFICITY.
RX PubMed=11809975; DOI=10.1126/science.1066642;
RA Aurelio O., Hall D., Hobert O.;
RT "Immunoglobulin-domain proteins required for maintenance of ventral nerve
RT cord organization.";
RL Science 295:686-690(2002).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19737747; DOI=10.1534/genetics.109.107441;
RA Benard C., Tjoe N., Boulin T., Recio J., Hobert O.;
RT "The small, secreted immunoglobulin protein ZIG-3 maintains axon position
RT in Caenorhabditis elegans.";
RL Genetics 183:917-927(2009).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22829780; DOI=10.1371/journal.pgen.1002819;
RA Benard C.Y., Blanchette C., Recio J., Hobert O.;
RT "The secreted immunoglobulin domain proteins ZIG-5 and ZIG-8 cooperate with
RT L1CAM/SAX-7 to maintain nervous system integrity.";
RL PLoS Genet. 8:E1002819-E1002819(2012).
CC -!- FUNCTION: Probably not involved in maintaining the position of ASI and
CC ASH head neuron cell bodies and ventral nerve cord axons of PVQ, PVP,
CC RMEV, AVK and HSN neurons. {ECO:0000269|PubMed:19737747,
CC ECO:0000269|PubMed:22829780}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in head and tail body wall muscles.
CC {ECO:0000269|PubMed:11809975}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:19737747,
CC PubMed:22829780). No defect in the positioning of ASI and ASH neuron
CC cell bodies (PubMed:22829780). No defect in the positioning of PQV,
CC PVP, RMEV, HSN adn AVK axons in the ventral nerve cord
CC (PubMed:19737747). {ECO:0000269|PubMed:19737747,
CC ECO:0000269|PubMed:22829780}.
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DR EMBL; BX284606; CCD68815.1; -; Genomic_DNA.
DR PIR; T29925; T29925.
DR RefSeq; NP_508882.3; NM_076481.5.
DR AlphaFoldDB; Q22125; -.
DR SMR; Q22125; -.
DR STRING; 6239.T03G11.8.1; -.
DR GlyCosmos; Q22125; 2 sites, No reported glycans.
DR EPD; Q22125; -.
DR PaxDb; 6239-T03G11-8; -.
DR PeptideAtlas; Q22125; -.
DR EnsemblMetazoa; T03G11.8.1; T03G11.8.1; WBGene00006983.
DR GeneID; 192089; -.
DR KEGG; cel:CELE_T03G11.8; -.
DR UCSC; T03G11.8; c. elegans.
DR AGR; WB:WBGene00006983; -.
DR WormBase; T03G11.8; CE40660; WBGene00006983; zig-6.
DR eggNOG; ENOG502T0ZU; Eukaryota.
DR HOGENOM; CLU_101115_0_0_1; -.
DR InParanoid; Q22125; -.
DR OMA; VITYWTR; -.
DR OrthoDB; 2875049at2759; -.
DR PhylomeDB; Q22125; -.
DR PRO; PR:Q22125; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006983; Expressed in larva and 4 other cell types or tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISS:WormBase.
DR GO; GO:0032589; C:neuron projection membrane; IBA:GO_Central.
DR GO; GO:0042592; P:homeostatic process; IMP:WormBase.
DR GO; GO:0050808; P:synapse organization; IBA:GO_Central.
DR CDD; cd00096; Ig; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003006; Ig/MHC_CS.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR PANTHER; PTHR12080:SF48; IG DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR12080; SIGNALING LYMPHOCYTIC ACTIVATION MOLECULE; 1.
DR Pfam; PF00047; ig; 1.
DR Pfam; PF13927; Ig_3; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; Immunoglobulin; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
DR PROSITE; PS00290; IG_MHC; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..243
FT /note="Zwei Ig domain protein zig-6"
FT /id="PRO_5004200546"
FT DOMAIN 30..118
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 133..212
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 47..102
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 145..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 243 AA; 27066 MW; FC736DA09F478E77 CRC64;
MTKLCLLLLP LVFLVSYSFA EEEITISISP NANPVQKPIG HQISLVCSIK KTDSNGEKPG
MIWKKHGGLD RTGNVEVKKL DDYTLGLIIR NSSVEDSGVY YCQAQVGSKV YMNKMDVIVF
EDIVFRDKQL HFGQVLATAS VNISCEVSAK KDSVITYWTR HGKQILEGGK HKFYSRGSIL
EIQNYQPEQD AGQYTCEVFH VSSGSSNTKT VTLGTTGEKN YVACQQMCNS FCTDVHNKVF
TNN
//
