ZIG1_CAEEL
ID ZIG1_CAEEL Reviewed; 265 AA.
AC G5EGI7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Zwei Ig domain protein zig-1 {ECO:0000303|PubMed:11809975};
DE AltName: Full=2 Ig domain protein zig-1 {ECO:0000303|PubMed:11809975};
DE Flags: Precursor;
GN Name=zig-1 {ECO:0000312|WormBase:K10C3.3};
GN ORFNames=K10C3.3 {ECO:0000312|WormBase:K10C3.3};
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:AAL59606.1}
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=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: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in neurons and body wall 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 (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). In a zig-2, zig-3, zig-4 or zig-5 or zig-8 mutant
CC background, cell body positioning of ASI and ASH head neurons is normal
CC (PubMed:22829780). {ECO:0000269|PubMed:19737747,
CC ECO:0000269|PubMed:22829780}.
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DR EMBL; AF456248; AAL59606.1; -; mRNA.
DR EMBL; BX284601; CAB05773.2; -; Genomic_DNA.
DR PIR; T23555; T23555.
DR RefSeq; NP_492608.2; NM_060207.5.
DR AlphaFoldDB; G5EGI7; -.
DR STRING; 6239.K10C3.3; -.
DR EPD; G5EGI7; -.
DR PaxDb; G5EGI7; -.
DR PeptideAtlas; G5EGI7; -.
DR EnsemblMetazoa; K10C3.3.1; K10C3.3.1; WBGene00006978.
DR GeneID; 192086; -.
DR KEGG; cel:CELE_K10C3.3; -.
DR CTD; 192086; -.
DR WormBase; K10C3.3; CE30349; WBGene00006978; zig-1.
DR eggNOG; ENOG502S3Y2; Eukaryota.
DR HOGENOM; CLU_963851_0_0_1; -.
DR InParanoid; G5EGI7; -.
DR OMA; TLWCQAE; -.
DR OrthoDB; 1242813at2759; -.
DR PhylomeDB; G5EGI7; -.
DR PRO; PR:G5EGI7; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00006978; Expressed in larva and 3 other tissues.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR043204; Basigin-like.
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 PANTHER; PTHR10075; PTHR10075; 1.
DR Pfam; PF07679; I-set; 1.
DR SMART; SM00409; IG; 2.
DR SMART; SM00408; IGc2; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..265
FT /note="Zwei Ig domain protein zig-1"
FT /id="PRO_5007661293"
FT TOPO_DOM 18..232
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 41..108
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255"
FT DOMAIN 120..220
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 155..202
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 265 AA; 29170 MW; EF8FB32786A604D8 CRC64;
MKNLLLITFF VVSTVTALGG RGSKSALVLV AARSSENHPL HATDPITIWC APDNPQVVIK
TAHFIRSSDN EKLEAALNPT KKNATYTFGS PSVKDAGEYK CELDTPHGKI SHKVFIYSRP
VVHSHEHFTE HEGHEFHLES TGTTVEKGES VTLTCPVTGY PKPVVKWTKD SAPLALSQSV
SMEGSTVIVT NANYTDAGTY SCEAVNEYTV NGKTSKMLLV VDKMVDVRSE FQWVYPLAVI
LITIFLLVVI IVFCEWRNKK STSKA
