ZIG8_CAEEL
ID ZIG8_CAEEL Reviewed; 268 AA.
AC G5ED00;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Zwei Ig domain protein zig-8 {ECO:0000303|PubMed:11809975};
DE AltName: Full=2 Ig domain protein zig-8 {ECO:0000303|PubMed:11809975};
DE Flags: Precursor;
GN Name=zig-8 {ECO:0000312|WormBase:Y39E4B.8};
GN ORFNames=Y39E4B.8 {ECO:0000312|WormBase:Y39E4B.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|EMBL:AAL59611.1}
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 {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 [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-5, 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 neurons and pharyngeal muscles.
CC {ECO:0000269|PubMed:11809975}.
CC -!- DEVELOPMENTAL STAGE: Expression begins at the late L1 larval stage.
CC {ECO:0000269|PubMed:11809975}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. In a zig-5 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}.
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DR EMBL; AF456253; AAL59611.1; -; mRNA.
DR EMBL; BX284603; CAB54429.2; -; Genomic_DNA.
DR RefSeq; NP_499714.1; NM_067313.6.
DR PDB; 6ON9; X-ray; 2.00 A; A=22-137.
DR PDB; 6ONB; X-ray; 1.70 A; A/C=22-137.
DR PDB; 6PLL; X-ray; 2.69 A; A/B/C=22-137.
DR PDBsum; 6ON9; -.
DR PDBsum; 6ONB; -.
DR PDBsum; 6PLL; -.
DR AlphaFoldDB; G5ED00; -.
DR SMR; G5ED00; -.
DR IntAct; G5ED00; 1.
DR STRING; 6239.Y39E4B.8; -.
DR EPD; G5ED00; -.
DR PaxDb; G5ED00; -.
DR PeptideAtlas; G5ED00; -.
DR EnsemblMetazoa; Y39E4B.8.1; Y39E4B.8.1; WBGene00006985.
DR GeneID; 176732; -.
DR KEGG; cel:CELE_Y39E4B.8; -.
DR CTD; 176732; -.
DR WormBase; Y39E4B.8; CE24241; WBGene00006985; zig-8.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000175227; -.
DR HOGENOM; CLU_1039115_0_0_1; -.
DR InParanoid; G5ED00; -.
DR OMA; HCRVKSL; -.
DR OrthoDB; 974511at2759; -.
DR PhylomeDB; G5ED00; -.
DR PRO; PR:G5ED00; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006985; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0032589; C:neuron projection membrane; IBA:GO_Central.
DR GO; GO:0050808; P:synapse organization; IBA:GO_Central.
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; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR037448; Zig-8.
DR PANTHER; PTHR23279; PTHR23279; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..268
FT /note="Zwei Ig domain protein zig-8"
FT /id="PRO_5007661457"
FT DOMAIN 40..128
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 140..251
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 57..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 165..226
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:6ONB"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:6ONB"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:6ONB"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:6ON9"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:6ONB"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:6ONB"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:6ONB"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:6ONB"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:6ONB"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:6ONB"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:6ONB"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:6ONB"
SQ SEQUENCE 268 AA; 30272 MW; 47643AC5F1D9E3A1 CRC64;
MRRFSNICVI LFSFLYATGH GASEEVMACL RQERSRVENP SQTIVNVVAE NPAYLHCSVP
PDAEHEIAWT RVSDGALLTA GNRTFTRDPR WQVSKKSANI WVLNLRRAEQ QDSGCYLCEI
NDKHNTVYAV YLKVLEPPLP SPSSLQKKST KLMANMSGDE VVLNCTVTST DKDEEVLDVV
WTRDGNTINF NDTEKYILKV KRDAGVVIET MRIRKATMED DGNYACEHSQ QKASQIVHIN
KAEAQTSNSA TFPCSIFSIS IFMYFLYL
