ZIG5_CAEEL
ID ZIG5_CAEEL Reviewed; 260 AA.
AC Q9XXD7; Q8WR47;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Zwei Ig domain protein zig-5 {ECO:0000303|PubMed:11809975};
DE AltName: Full=2 Ig domain protein zig-5 {ECO:0000303|PubMed:11809975};
DE Flags: Precursor;
GN Name=zig-5 {ECO:0000312|WormBase:Y48A6A.1};
GN ORFNames=Y48A6A.1 {ECO:0000312|WormBase:Y48A6A.1};
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:AAL59610.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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 [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 [3] {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: Together with zig-8, required postembryonically to maintain
CC the position of ASI and ASH head neuron cell bodies and ventral nerve
CC cord axons of PVQ, PVP and HSN neurons by preventing their displacement
CC that could occur during body growth and movement. May act by reducing
CC L1CAM-like protein sax-7 (long isoform) adhesion.
CC {ECO:0000269|PubMed:22829780}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in PVT, VD1-13, RID, AFD, ASK, RIV, RIB,
CC PVQ, DVA and RIS neurons. {ECO:0000269|PubMed:11809975}.
CC -!- DEVELOPMENTAL STAGE: Expression begins at the 3-fold embryonic stage.
CC {ECO:0000269|PubMed:11809975}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. In a zig-8 mutant
CC background, 74 percent of animals have cell bodies of ASI and ASH head
CC neurons displaced either on the top of or anterior to the nerve ring.
CC In addition, double mutants show defects in the positioning of the
CC ventral nerve cord (VNC) axons characterized by axons of embryonically
CC generated PVQ, PVP and HSN neurons from the left and right VNC drifting
CC into the opposite cord (axon flip-over). Both defects begin at the L3
CC larval stage and become more pronounced at the L4 larval and adult
CC stages. Cell body and axon positioning is normal in embryos and in L1
CC larvae. In a zig-1, zig-2, zig-3 or zig-4 mutant background, cell body
CC positioning of ASI and ASH head neurons is normal. In unc-13 or unc-54
CC mutant background, where locomotion is impaired, cell body positioning
CC of ASI and ASH neurons is normal. In a sax-7 (nj53) mutant background,
CC cell body and axon positioning is normal. Simultaneous RNAi-mediated
CC knockdown of zig-5 and zig-8 at the embryonic, larval or adult stage
CC causes a displacement of ASI and ASH head neurons in 6 to 9 percent of
CC animals. {ECO:0000269|PubMed:22829780}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL59610.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF456252; AAL59610.1; ALT_FRAME; mRNA.
DR EMBL; BX284603; CAA19522.2; -; Genomic_DNA.
DR PIR; T26976; T26976.
DR RefSeq; NP_499405.4; NM_067004.5.
DR AlphaFoldDB; Q9XXD7; -.
DR SMR; Q9XXD7; -.
DR STRING; 6239.Y48A6A.1; -.
DR EPD; Q9XXD7; -.
DR PaxDb; Q9XXD7; -.
DR EnsemblMetazoa; Y48A6A.1.1; Y48A6A.1.1; WBGene00006982.
DR GeneID; 176527; -.
DR KEGG; cel:CELE_Y48A6A.1; -.
DR UCSC; Y48A6A.1; c. elegans.
DR CTD; 176527; -.
DR WormBase; Y48A6A.1; CE31735; WBGene00006982; zig-5.
DR eggNOG; ENOG502TG0Z; Eukaryota.
DR HOGENOM; CLU_1134748_0_0_1; -.
DR InParanoid; Q9XXD7; -.
DR OMA; CLDERTA; -.
DR OrthoDB; 1141111at2759; -.
DR PhylomeDB; Q9XXD7; -.
DR PRO; PR:Q9XXD7; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006982; Expressed in larva and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISS:WormBase.
DR GO; GO:0007389; P:pattern specification process; IMP:WormBase.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF07679; I-set; 2.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 2: Evidence at transcript level;
KW Disulfide bond; Immunoglobulin domain; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..260
FT /note="Zwei Ig domain protein zig-5"
FT /id="PRO_5004336823"
FT DOMAIN 42..143
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 166..256
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 66..126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 187..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 260 AA; 28187 MW; C0F4F68D93C6895F CRC64;
MPSPLNHHLS CFVLSVILLG SHVSTSKIPI APQSVCEGLI EPSVLSIDKP LENIKANRGD
SLVLRCAFYA SPQPTIVWYH RGKRVDSHPA AHFETLLSAT NLGQSVVESA LRIDCLDERT
AGEYFCEATS PCTQPVVTSS TVTINKAPKS ITGTCKSIRQ PLESPPIVSD FTLSRIELPG
GVAQLACRVR GVPTPKTKWF KIEEDESLST IDGQPNYMHL SNGDLLIVGD EETISESFRC
VASNPLGSVH QDASVIYMMA
