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Database: UniProt
Entry: G5EFD5
LinkDB: G5EFD5
Original site: G5EFD5 
ID   UNC71_CAEEL             Reviewed;        1042 AA.
AC   G5EFD5;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   16-JAN-2019, entry version 71.
DE   RecName: Full=Disintegrin and metalloproteinase domain-containing protein unc-71 {ECO:0000305};
DE   AltName: Full=Uncoordinated protein 71 {ECO:0000312|WormBase:Y37D8A.13};
DE   Flags: Precursor;
GN   Name=unc-71 {ECO:0000312|WormBase:Y37D8A.13};
GN   Synonyms=adm-1 {ECO:0000312|WormBase:Y37D8A.13};
GN   ORFNames=Y37D8A.13 {ECO:0000312|WormBase:Y37D8A.13};
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:AAC47444.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP   STAGE.
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC47444.1};
RX   PubMed=8970152;
RA   Podbilewicz B.;
RT   "ADM-1, a protein with metalloprotease- and disintegrin-like domains,
RT   is expressed in syncytial organs, sperm, and sheath cells of sensory
RT   organs in Caenorhabditis elegans.";
RL   Mol. Biol. Cell 7:1877-1893(1996).
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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [3] {ECO:0000305}
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=9073451; DOI=10.1006/dbio.1996.8473;
RA   Chen E.B., Branda C.S., Stern M.J.;
RT   "Genetic enhancers of sem-5 define components of the gonad-independent
RT   guidance mechanism controlling sex myoblast migration in
RT   Caenorhabditis elegans hermaphrodites.";
RL   Dev. Biol. 182:88-100(1997).
RN   [4] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF GLY-149; ASP-461; LEU-471; CYS-477;
RP   ASP-504; CYS-509; ALA-557; GLY-594; SER-628; CYS-687; PRO-902 AND
RP   ARG-990.
RX   PubMed=12783787;
RA   Huang X., Huang P., Robinson M.K., Stern M.J., Jin Y.;
RT   "UNC-71, a disintegrin and metalloprotease (ADAM) protein, regulates
RT   motor axon guidance and sex myoblast migration in C. elegans.";
RL   Development 130:3147-3161(2003).
RN   [5] {ECO:0000305}
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=22293500; DOI=10.1016/j.febslet.2012.01.031;
RA   Masuda H., Nakamura K., Takata N., Itoh B., Hirose T., Moribe H.,
RA   Mekada E., Okada M.;
RT   "MIG-13 controls anteroposterior cell migration by interacting with
RT   UNC-71/ADM-1 and SRC-1 in Caenorhabditis elegans.";
RL   FEBS Lett. 586:740-746(2012).
CC   -!- FUNCTION: Involved in the migration of sex myoblasts (progenitors
CC       of egg-laying muscles), Q neuroblasts and BDU interneurons during
CC       development (PubMed:9073451, PubMed:12783787, PubMed:22293500).
CC       Involved in axon branching and guidance of neurons including
CC       GABAergic type D motor neurons (PubMed:12783787). Promotes sex
CC       myoblast migration and positioning independently of gonad
CC       attraction cues (PubMed:9073451, PubMed:12783787). May act
CC       downstream of mig-13 in order to promote the guidance, migration
CC       and positioning of Q neuroblasts and their descendants along the
CC       anteroposterior body axis (PubMed:22293500). Required for
CC       coordinated movements (PubMed:12783787).
CC       {ECO:0000269|PubMed:12783787, ECO:0000269|PubMed:22293500,
CC       ECO:0000269|PubMed:9073451}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12783787,
CC       ECO:0000305|PubMed:8970152}; Single-pass type I membrane protein
CC       {ECO:0000255}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout development
CC       (PubMed:8970152, PubMed:12783787, PubMed:22293500). First
CC       expressed in several posterior cells of comma stage embryos
CC       (PubMed:12783787). Expressed in the excretory cell and in some
CC       head neurons in threefold stage embryos (PubMed:12783787). At the
CC       L1 stage of larval development expressed in the syncytial
CC       hypodermis (PubMed:8970152). From the L1 stage of larval
CC       development to adulthood, expressed in head neurons, the excretory
CC       cell, excretory gland cells and in the sphincter muscle
CC       (PubMed:12783787, PubMed:22293500). From the L4 stage of larval
CC       development to adulthood, expressed in hypodermal cells
CC       surrounding the vulva (PubMed:12783787).
CC       {ECO:0000269|PubMed:12783787, ECO:0000269|PubMed:22293500,
CC       ECO:0000269|PubMed:8970152}.
CC   -!- DISRUPTION PHENOTYPE: Defective sex myoblast migration
CC       (PubMed:9073451). Motor neuron axon guidance defects with aberrant
CC       axon branching in type D motor neurons (PubMed:12783787).
CC       {ECO:0000269|PubMed:12783787, ECO:0000269|PubMed:9073451}.
CC   -!- CAUTION: Contains a metallopeptidase domain, but the active site
CC       is not conserved, so the protein is not expected to have protease
CC       activity. {ECO:0000305}.
DR   EMBL; U68185; AAC47444.1; -; mRNA.
DR   EMBL; BX284603; CAA21545.1; -; Genomic_DNA.
DR   PIR; T26644; T26644.
DR   RefSeq; NP_499680.1; NM_067279.6.
DR   UniGene; Cel.7111; -.
DR   ProteinModelPortal; G5EFD5; -.
DR   SMR; G5EFD5; -.
DR   STRING; 6239.Y37D8A.13; -.
DR   EPD; G5EFD5; -.
DR   PaxDb; G5EFD5; -.
DR   PeptideAtlas; G5EFD5; -.
DR   EnsemblMetazoa; Y37D8A.13; Y37D8A.13; WBGene00006804.
DR   GeneID; 176706; -.
DR   KEGG; cel:CELE_Y37D8A.13; -.
DR   CTD; 176706; -.
DR   WormBase; Y37D8A.13; CE20217; WBGene00006804; unc-71.
DR   eggNOG; KOG3607; Eukaryota.
DR   eggNOG; ENOG410XX2M; LUCA.
DR   GeneTree; ENSGT00940000167333; -.
DR   InParanoid; G5EFD5; -.
DR   OMA; EVVHPFQ; -.
DR   OrthoDB; 162519at2759; -.
DR   PhylomeDB; G5EFD5; -.
DR   PRO; PR:G5EFD5; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00006804; Expressed in 8 organ(s), highest expression level in multi-cellular organism.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:WormBase.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; ISS:WormBase.
DR   GO; GO:0098609; P:cell-cell adhesion; TAS:WormBase.
DR   GO; GO:0045026; P:plasma membrane fusion; TAS:WormBase.
DR   GO; GO:0006508; P:proteolysis; ISS:WormBase.
DR   CDD; cd04269; ZnMc_adamalysin_II_like; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   Gene3D; 4.10.70.10; -; 1.
DR   InterPro; IPR006586; ADAM_Cys-rich.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR002870; Peptidase_M12B_N.
DR   InterPro; IPR034027; Reprolysin_adamalysin.
DR   Pfam; PF08516; ADAM_CR; 1.
DR   Pfam; PF00200; Disintegrin; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF01562; Pep_M12B_propep; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   SMART; SM00608; ACR; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; SSF57552; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; Disulfide bond; EGF-like domain;
KW   Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   CHAIN        24   1042       Disintegrin and metalloproteinase domain-
FT                                containing protein unc-71. {ECO:0000305}.
FT                                /FTId=PRO_5008958430.
FT   TOPO_DOM     24    746       Extracellular. {ECO:0000305}.
FT   TRANSMEM    747    767       Helical. {ECO:0000255}.
FT   TOPO_DOM    768   1042       Cytoplasmic. {ECO:0000305}.
FT   DOMAIN      227    431       Peptidase M12B. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00276}.
FT   DOMAIN      437    524       Disintegrin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00068}.
FT   DOMAIN      662    699       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   COMPBIAS    205    216       His-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00009}.
FT   CARBOHYD    103    103       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    155    155       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    538    538       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    703    703       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   DISULFID    338    426       {ECO:0000255|PROSITE-ProRule:PRU00276}.
FT   DISULFID    378    410       {ECO:0000255|PROSITE-ProRule:PRU00276}.
FT   DISULFID    380    386       {ECO:0000255|PROSITE-ProRule:PRU00276}.
FT   DISULFID    496    516       {ECO:0000255|PROSITE-ProRule:PRU00068}.
FT   DISULFID    666    681       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    675    687       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    689    698       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   MUTAGEN     149    149       G->R: In ju161; axon guidance defects.
FT                                {ECO:0000269|PubMed:12783787}.
FT   MUTAGEN     461    461       D->N: In ay64; sex myoblast migration
FT                                defects. {ECO:0000269|PubMed:12783787}.
FT   MUTAGEN     471    471       L->P: In ay46; sex myoblast migration
FT                                defects. {ECO:0000269|PubMed:12783787}.
FT   MUTAGEN     477    477       C->Y: In ay17; sex myoblast migration
FT                                defects. {ECO:0000269|PubMed:12783787}.
FT   MUTAGEN     504    504       D->N: In ju160; axon guidance defects.
FT                                {ECO:0000269|PubMed:12783787}.
FT   MUTAGEN     509    509       C->Y: In ju159; axon guidance defects.
FT                                {ECO:0000269|PubMed:12783787}.
FT   MUTAGEN     557    557       A->T: In e541; uncoordinated movement.
FT                                {ECO:0000269|PubMed:12783787}.
FT   MUTAGEN     594    594       G->E: In ju157; axon guidance defects.
FT                                {ECO:0000269|PubMed:12783787}.
FT   MUTAGEN     628    628       S->L: In ay47; sex myoblast migration
FT                                defects. {ECO:0000269|PubMed:12783787}.
FT   MUTAGEN     687    687       C->S: In ay44; sex myoblast migration
FT                                defects. {ECO:0000269|PubMed:12783787}.
FT   MUTAGEN     902    902       P->L: In ay48; sex myoblast migration
FT                                defects. {ECO:0000269|PubMed:12783787}.
FT   MUTAGEN     990    990       R->K: In ju255; axon guidance defects.
FT                                {ECO:0000269|PubMed:12783787}.
SQ   SEQUENCE   1042 AA;  114196 MW;  BA6A33593927D4C4 CRC64;
     MICASKITML GLLVMCTLGG VLGKVDIRQT TANKAFMETM RADGYEVVHP FQIRDKNERI
     GIDTRNYFLK AQEHYSHVTI VIRSNQLGRL KLVLERNNFI FLNQTAFHKL DADGERVIQN
     RVENCYYQGT VGGEESSFVA LSSCNGLRGV ISFANGTTFG IWPLDGGDRN SRRHPHILYK
     SEWSQEAKCG SSMAHAVGQR RMKKHVHKHR SHHHEHNKKR DVSKRTKYVE VALIADYEFM
     KARGLHDLDA ISYMLESLNI ADSMLSRDLN IRLSAVYVEL WTDVQRIDLW EDIERTLSGV
     VDYASGHIYH IQKDASILFT AGSFANQEVS NAAIRSICTA RSAVIVKGVE QFATHWNGEL
     LAQSIGHLLG LEHDTTACSC EPSPECVMRQ QPGRVGGGGG SPFSWQFSKC SVARMHGIWQ
     DGNIQCLLNK PFQVSELREC GNGVVDGSEE CDCGSRENCQ DPCCDPLTCT LRPHAQCAAH
     HKCCHRCELR KAGDTCRSSK SPCDVAEQCD GKSGDCPPDG HLIDGTVCGT DGQCWRGNCS
     DSHQQCQKLW GREARVAEPV CFEQNTKGAE YANCGQRQAD GTYHPCQIED TRCGTLHCHS
     GSITPIDSSL KAFTFHFTEN SHQIQCKSIA SAAVGLTSDG TNCASGRVCV AGSCVEMSSV
     SSATACPTNN LALLCSGHGH CTTTARCVCF NGWSGVACDI RSNSSTYQGS MGFGEEGSGG
     SSQKSSERKT IMIPHLNIGT TLETATLFAI LLGFGVFLLL CLVCLMLCYR RRSVVEIPKP
     SDEKDEESPD RQIKFGNMPS YREEKRKRKS NKKIYGALNR ITEADERDST SLRSRDSAGG
     SQQLVDRRNG APVVVGGIRD PYAGEHIYAE SSSNHLTRQF RGINSDGSYP LRSFGSWRSS
     APISPASSSG QLTDVSTATT PLRLNKIGKF LKTLQSDDES PSPFSDHQSF TTGIGIGARL
     EQMQFGGGGD EELSAVEADH DVGSNTESSR GCEEPMDPGS WDSPTLVNGA SSSSTSNNYN
     FRQSPSLFSD PFKLEMTNSM HN
//
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