ID ZIG2_CAEEL Reviewed; 238 AA.
AC G5EDQ9;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Zwei Ig domain protein zig-2 {ECO:0000303|PubMed:11809975};
DE AltName: Full=2 Ig domain protein zig-2 {ECO:0000303|PubMed:11809975};
DE Flags: Precursor;
GN Name=zig-2 {ECO:0000312|WormBase:F42F12.2};
GN ORFNames=F42F12.2 {ECO:0000312|WormBase:F42F12.2};
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:AAL59607.1}
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: Secreted {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in PVT neurons and weakly in some head
CC neurons. {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-1, 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; AF456249; AAL59607.1; -; mRNA.
DR EMBL; BX284606; CAA92170.1; -; Genomic_DNA.
DR PIR; T22098; T22098.
DR RefSeq; NP_510069.1; NM_077668.3.
DR AlphaFoldDB; G5EDQ9; -.
DR SMR; G5EDQ9; -.
DR STRING; 6239.F42F12.2.1; -.
DR MEROPS; I43.001; -.
DR GlyCosmos; G5EDQ9; 5 sites, No reported glycans.
DR PaxDb; 6239-F42F12-2; -.
DR EnsemblMetazoa; F42F12.2.1; F42F12.2.1; WBGene00006979.
DR GeneID; 192087; -.
DR KEGG; cel:CELE_F42F12.2; -.
DR AGR; WB:WBGene00006979; -.
DR WormBase; F42F12.2; CE03313; WBGene00006979; zig-2.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00970000196086; -.
DR HOGENOM; CLU_072416_1_0_1; -.
DR InParanoid; G5EDQ9; -.
DR OMA; CIAFNGH; -.
DR OrthoDB; 5266637at2759; -.
DR PhylomeDB; G5EDQ9; -.
DR PRO; PR:G5EDQ9; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00006979; Expressed in adult organism and 1 other cell type or tissue.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR PANTHER; PTHR10075; BASIGIN RELATED; 1.
DR PANTHER; PTHR10075:SF101; ZWEI IG DOMAIN PROTEIN ZIG-3; 1.
DR Pfam; PF07679; I-set; 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.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Reference proteome;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..238
FT /note="Zwei Ig domain protein zig-2"
FT /id="PRO_5007661259"
FT DOMAIN 31..130
FT /note="Ig-like C2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DOMAIN 149..230
FT /note="Ig-like C2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 54..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 170..217
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 238 AA; 26330 MW; 6EC6497298B491AE CRC64;
MLKFTAISFV LLNAAESVDH QKPIRALDSQ PLLKFTRTPN DSNVTFGEKF VLSCGANGAP
LPSIYWELNG MRIQGEETSN VYENILNDGK QVSNAAMVSS HYRIPCATAR NSGAYKCIID
NGLTKLEHVA KVFVGGNKTN CALNDNGAPF ISMTVDFRLE ISNNAVALSC RSETATEWSW
HKGEQLLTND GERYQMFPSG DLIIRNISWS DMGEYNCTAR NHFGETTAIT FLYPTLAK
//
