UNC71_CAEEL
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 03-AUG-2022, entry version 83.
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 STAGE.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAC47444.1};
RX PubMed=8970152; DOI=10.1091/mbc.7.12.1877;
RA Podbilewicz B.;
RT "ADM-1, a protein with metalloprotease- and disintegrin-like domains, is
RT expressed in syncytial organs, sperm, and sheath cells of sensory organs in
RT 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 investigating
RT 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 Caenorhabditis
RT elegans hermaphrodites.";
RL Dev. Biol. 182:88-100(1997).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF GLY-149; ASP-461; LEU-471; CYS-477; ASP-504; CYS-509;
RP ALA-557; GLY-594; SER-628; CYS-687; PRO-902 AND ARG-990.
RX PubMed=12783787; DOI=10.1242/dev.00518;
RA Huang X., Huang P., Robinson M.K., Stern M.J., Jin Y.;
RT "UNC-71, a disintegrin and metalloprotease (ADAM) protein, regulates motor
RT 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 UNC-
RT 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 of
CC 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 GABAergic
CC type D motor neurons (PubMed:12783787). Promotes sex myoblast migration
CC and positioning independently of gonad attraction cues (PubMed:9073451,
CC PubMed:12783787). May act downstream of mig-13 in order to promote the
CC guidance, migration and positioning of Q neuroblasts and their
CC descendants along the anteroposterior body axis (PubMed:22293500).
CC Required for 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 (PubMed:8970152,
CC PubMed:12783787, PubMed:22293500). First expressed in several posterior
CC cells of comma stage embryos (PubMed:12783787). Expressed in the
CC excretory cell and in some head neurons in threefold stage embryos
CC (PubMed:12783787). At the L1 stage of larval development expressed in
CC the syncytial 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 surrounding the
CC vulva (PubMed:12783787). {ECO:0000269|PubMed:12783787,
CC ECO:0000269|PubMed:22293500, ECO:0000269|PubMed:8970152}.
CC -!- DISRUPTION PHENOTYPE: Defective sex myoblast migration
CC (PubMed:9073451). Motor neuron axon guidance defects with aberrant axon
CC 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 is not
CC conserved, so the protein is not expected to have protease activity.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; G5EFD5; -.
DR SMR; G5EFD5; -.
DR STRING; 6239.Y37D8A.13; -.
DR EPD; G5EFD5; -.
DR PaxDb; G5EFD5; -.
DR PeptideAtlas; G5EFD5; -.
DR EnsemblMetazoa; Y37D8A.13.1; Y37D8A.13.1; 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 GeneTree; ENSGT00940000167333; -.
DR HOGENOM; CLU_291906_0_0_1; -.
DR InParanoid; G5EFD5; -.
DR OMA; VNNRMTP; -.
DR OrthoDB; 162519at2759; -.
DR PhylomeDB; G5EFD5; -.
DR Reactome; R-CEL-1474228; Degradation of the extracellular matrix.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:G5EFD5; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006804; Expressed in embryo and 10 other tissues.
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; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; ISS:WormBase.
DR GO; GO:0098609; P:cell-cell adhesion; TAS:WormBase.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; IBA:GO_Central.
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; IPR000742; EGF-like_dom.
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; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1042
FT /note="Disintegrin and metalloproteinase domain-containing
FT protein unc-71"
FT /evidence="ECO:0000305"
FT /id="PRO_5008958430"
FT TOPO_DOM 24..746
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 747..767
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 768..1042
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 227..431
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 437..524
FT /note="Disintegrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DOMAIN 662..699
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 779..809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 980..1028
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..805
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1028
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 103
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 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 338..426
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 378..410
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 380..386
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DISULFID 496..516
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00068"
FT DISULFID 666..681
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 675..687
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 689..698
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT MUTAGEN 149
FT /note="G->R: In ju161; axon guidance defects."
FT /evidence="ECO:0000269|PubMed:12783787"
FT MUTAGEN 461
FT /note="D->N: In ay64; sex myoblast migration defects."
FT /evidence="ECO:0000269|PubMed:12783787"
FT MUTAGEN 471
FT /note="L->P: In ay46; sex myoblast migration defects."
FT /evidence="ECO:0000269|PubMed:12783787"
FT MUTAGEN 477
FT /note="C->Y: In ay17; sex myoblast migration defects."
FT /evidence="ECO:0000269|PubMed:12783787"
FT MUTAGEN 504
FT /note="D->N: In ju160; axon guidance defects."
FT /evidence="ECO:0000269|PubMed:12783787"
FT MUTAGEN 509
FT /note="C->Y: In ju159; axon guidance defects."
FT /evidence="ECO:0000269|PubMed:12783787"
FT MUTAGEN 557
FT /note="A->T: In e541; uncoordinated movement."
FT /evidence="ECO:0000269|PubMed:12783787"
FT MUTAGEN 594
FT /note="G->E: In ju157; axon guidance defects."
FT /evidence="ECO:0000269|PubMed:12783787"
FT MUTAGEN 628
FT /note="S->L: In ay47; sex myoblast migration defects."
FT /evidence="ECO:0000269|PubMed:12783787"
FT MUTAGEN 687
FT /note="C->S: In ay44; sex myoblast migration defects."
FT /evidence="ECO:0000269|PubMed:12783787"
FT MUTAGEN 902
FT /note="P->L: In ay48; sex myoblast migration defects."
FT /evidence="ECO:0000269|PubMed:12783787"
FT MUTAGEN 990
FT /note="R->K: In ju255; axon guidance defects."
FT /evidence="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
