ID   ZIG7_CAEEL              Reviewed;         239 AA.
AC   O44730;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 3.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Zwei Ig domain protein zig-7 {ECO:0000303|PubMed:11809975};
DE   AltName: Full=2 Ig domain protein zig-7 {ECO:0000303|PubMed:11809975};
DE   Flags: Precursor;
GN   Name=zig-7 {ECO:0000312|WormBase:F54D7.4};
GN   ORFNames=F54D7.4 {ECO:0000312|WormBase:F54D7.4};
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 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; BX284601; CCD68970.1; -; Genomic_DNA.
DR   RefSeq; NP_491451.2; NM_059050.5.
DR   AlphaFoldDB; O44730; -.
DR   SMR; O44730; -.
DR   STRING; 6239.F54D7.4; -.
DR   EPD; O44730; -.
DR   PaxDb; O44730; -.
DR   PeptideAtlas; O44730; -.
DR   EnsemblMetazoa; F54D7.4.1; F54D7.4.1; WBGene00006984.
DR   GeneID; 172096; -.
DR   KEGG; cel:CELE_F54D7.4; -.
DR   UCSC; F54D7.4; c. elegans.
DR   CTD; 172096; -.
DR   WormBase; F54D7.4; CE33929; WBGene00006984; zig-7.
DR   eggNOG; ENOG502S990; Eukaryota.
DR   HOGENOM; CLU_1162045_0_0_1; -.
DR   InParanoid; O44730; -.
DR   OMA; ANPEPMV; -.
DR   OrthoDB; 1242813at2759; -.
DR   PhylomeDB; O44730; -.
DR   PRO; PR:O44730; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00006984; Expressed in larva and 4 other tissues.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; -; 1.
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; IPR003598; Ig_sub2.
DR   PANTHER; PTHR10075; PTHR10075; 1.
DR   SMART; SM00408; IGc2; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..239
FT                   /note="Zwei Ig domain protein zig-7"
FT                   /id="PRO_5004158391"
FT   DOMAIN          145..211
FT                   /note="Ig-like C2-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   CARBOHYD        43
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        164..211
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   239 AA;  26386 MW;  C4911A4327907FFC CRC64;
     MKLINCISIA LLCTLVDFSS AEITVISNLA VVGSPESHVG TPNKTLYANI QNLWCGAQNL
     GEHIDVEYGE FTRLSDGKVF KGTVNQGKVY LEIGKASVKV AGRYRCEVRT LDKEIHSGNL
     IIYMPPVLDF PAAVRVSEVL NARPPHVIGA ERRGLHGERM VLECPVLANP EPMVRWEKNG
     EPLGNSDSIE YDGNNLILNS LTEDHIGKYR CIGDNSFPLF VDGPAIPHQI YFDQDIKVL