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Database: UniProt
Entry: A0A131MBU3
LinkDB: A0A131MBU3
Original site: A0A131MBU3 
ID   IRG7_CAEEL              Reviewed;        2217 AA.
AC   A0A131MBU3; Q20219;
DT   10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT   11-MAY-2016, sequence version 1.
DT   10-APR-2019, entry version 24.
DE   RecName: Full=Protein irg-7 {ECO:0000305};
DE   AltName: Full=Infection response protein 7 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=irg-7 {ECO:0000303|PubMed:28196094,
GN   ECO:0000312|WormBase:F40F4.6b};
GN   Synonyms=drd-2 {ECO:0000312|WormBase:F40F4.6b},
GN   upr-1 {ECO:0000312|WormBase:F40F4.6b};
GN   ORFNames=F40F4.6 {ECO:0000312|WormBase:F40F4.6b};
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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, DEVELOPMENTAL STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28196094; DOI=10.1371/journal.pgen.1006577;
RA   Yunger E., Safra M., Levi-Ferber M., Haviv-Chesner A.,
RA   Henis-Korenblit S.;
RT   "Innate immunity mediated longevity and longevity induced by germ cell
RT   removal converge on the C-type lectin domain protein IRG-7.";
RL   PLoS Genet. 13:E1006577-E1006577(2017).
CC   -!- FUNCTION: Plays a role in innate immunity, probably via the atf-7
CC       pathway, to confer resistance to pathogenic bacteria. May also
CC       play a role in the regulation of longevity.
CC       {ECO:0000269|PubMed:28196094}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=b {ECO:0000312|WormBase:F40F4.6b};
CC         IsoId=A0A131MBU3-1; Sequence=Displayed;
CC       Name=a {ECO:0000312|WormBase:F40F4.6a};
CC         IsoId=A0A131MBU3-2; Sequence=VSP_058914;
CC   -!- DEVELOPMENTAL STAGE: Expressed in the posterior cells of the
CC       intestine in L4 larva. {ECO:0000269|PubMed:28196094}.
CC   -!- INDUCTION: Up-regulated following infection with P.luminescens
CC       subsp Hb and E.faecalis bacteria. {ECO:0000269|PubMed:28196094}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in larvae results in
CC       reduced survival following infection with the pathogenic bacterium
CC       P.luminescens. RNAi-mediated knockdown in a glp-1 e2141 mutant
CC       background (in which germ cells are deleted) rescues the increased
CC       lifespan phenotype of the glp-1 mutant.
CC       {ECO:0000269|PubMed:28196094}.
DR   EMBL; BX284606; CCD70146.2; -; Genomic_DNA.
DR   EMBL; BX284606; CZR14621.1; -; Genomic_DNA.
DR   PIR; T16305; T16305.
DR   RefSeq; NP_001309693.1; NM_001322616.1. [A0A131MBU3-1]
DR   RefSeq; NP_508552.2; NM_076151.4. [A0A131MBU3-2]
DR   SMR; A0A131MBU3; -.
DR   STRING; 6239.F40F4.6; -.
DR   EnsemblMetazoa; F40F4.6a; F40F4.6a; WBGene00018237. [A0A131MBU3-2]
DR   EnsemblMetazoa; F40F4.6b; F40F4.6b; WBGene00018237. [A0A131MBU3-1]
DR   GeneID; 180613; -.
DR   KEGG; cel:CELE_F40F4.6; -.
DR   CTD; 180613; -.
DR   WormBase; F40F4.6a; CE47861; WBGene00018237; irg-7. [A0A131MBU3-2]
DR   WormBase; F40F4.6b; CE51544; WBGene00018237; irg-7. [A0A131MBU3-1]
DR   eggNOG; ENOG410J64V; Eukaryota.
DR   eggNOG; ENOG410ZTVM; LUCA.
DR   GeneTree; ENSGT00950000182725; -.
DR   HOGENOM; HOG000020190; -.
DR   OMA; WGGPIAE; -.
DR   OrthoDB; 1016037at2759; -.
DR   PRO; PR:A0A131MBU3; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00018237; Expressed in 4 organ(s), highest expression level in material anatomical entity.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR006582; MD_domain.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF00059; Lectin_C; 1.
DR   Pfam; PF00092; VWA; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00604; MD; 2.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS00022; EGF_1; 6.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS50234; VWFA; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Complete proteome; Disulfide bond;
KW   EGF-like domain; Immunity; Innate immunity; Lectin;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   CHAIN        17   2217       Protein irg-7. {ECO:0000305}.
FT                                /FTId=PRO_5007283654.
FT   DOMAIN      370    405       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      864    896       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1188   1313       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN     1499   1533       EGF-like 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     2016   2202       VWFA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00219}.
FT   DISULFID    379    393       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    395    404       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    868    873       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    886    895       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1212   1312       {ECO:0000255|PROSITE-ProRule:PRU00040}.
FT   DISULFID   1285   1304       {ECO:0000255|PROSITE-ProRule:PRU00040}.
FT   DISULFID   1508   1521       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1523   1532       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ      58     60       Missing (in isoform a). {ECO:0000305}.
FT                                /FTId=VSP_058914.
SQ   SEQUENCE   2217 AA;  243736 MW;  137AB95B7D8F880D CRC64;
     MRNWVLIAAL AVICLATEQE LSHKDRIRAV LRSWSPASQK QFFEPVREQK YRTMEERVIF
     LDTHHISKRS IAEPHVLAGM ATRGCNKPGY TGETCQYPLC SARNPYIPNN DGFDDIAIDA
     YNLANCSESY IVVVDETMRN IKIEVETASA LNPTFYLQAE NGDLIFPDES IQLPTMFTAN
     YLHLPPGQYM LGPRADTSEQ FCTMMMSSRS SIHVSGGFTS GDQAERSDYP NLKFTYFDTE
     SVVAIHAQGL DFPGQIQAIG FTGAENHISR YIPMTTRFNC TYPYILERYT CRKTSNNDAG
     HNLIQVEGVT NSGYKFRRIV PYQCVLPPVT TTTPAVPTTP AAPITSCQNG GQLLTDSNGV
     AYCYCFGLYS GSTCSQMLCA NGGFLPTPTS DRCQCPEGFS GFHCQNILCT DMSGFDFNAE
     NPTLTLVIRS RSQLSAVIEQ ATESVQSIVD LLASEPGYLS KFIVVLFDNG KLLVNRQYDS
     WDAAMVDLTK AIHSAPSEGG CDDVVMSAVA SALSLYPTNK SPIYVITDAT PNDSAEKETV
     FHLESYWRAP IYFIYVQPSP ADGCNSSPDN SAYRDMVDMA ARSSGNTFYF SDRSTISTFF
     YRHMLNTLFR SQLVLSGDYS HCSSQNLYKS AAFDLSVDYV TIVATGTNLT LVVTSPTGQY
     PTFNTAFSDG VNYVWTYNSP VAGQWFFSIR SLEPEAACTF KVYQKKFNFG GQTQYSPDYD
     IFWSFASTLT SAAGVLRQPV LGFDSSPVFH VTNYPQFLSM DRVHANLQIY AIRDGVQTEV
     YGSSGMYRDA CEFNFYFPPF TCRVPEEVLY FNFFARDNND MALQRAGTMF CAAVHPTPPP
     DHQCQNGGVM NPSNTTCFCT PEFTGTYCQN IICYNGGTAS GDHCVCPPGY AGESCEMARC
     IETGPNPEFI RYGVDMVFAV EITQNSIASL SMLNINFQEI LRDVLMQNRG WIRNFVLVGF
     NSTWGGPIAE SPADNLTAIT TALRTLASSV PADTGCTVKL WDALNYAIFS RQMAPGSFVE
     IFQTTPEDDT DTRSLGLFYD MSRTMELVLY GFLTSNPRLQ PEGFVCNATV ENYYTLLGIV
     SGSTGTTYSL QANEISNAVR LIPLQFSNGQ VTFNALDDCR HDDGLITYFP VDAYTQTIQI
     QTFGYGTTIQ VYTGAGVMAE ALELFYDDFT GQSVYEIRKA CDEGWEPIGQ YCIKFMATVE
     NILPMPQAKA FCASAGGFLV DDLTDDKNGF LKSVAANTQF WTGLFKNNDG QFYWDRGTGI
     NPDLLNQPIT YWADGEPSDD PTRQCVYFNG RSGDANKVWT TDTCAEPRAF ACQKHRYDAD
     HRPNVIGDDD LPAGWWYAKV KSNPPSGYPN MCTMSVRVQS SLQIVTGFST KIGNDFPLPD
     PIQDSTENRL ISYVHSVDNE NRVPILTDAI LWDAYNGTFY NGLKYQVRFG CQFAWVTQDF
     PCPNGDSQAN EFGVLHVGED EFGNTFQRLT FGHCSRAQIT CGNGGIRQNG QCVCTDYWTG
     SRCTVPICVN GGTRNPDEAT CSCPDGYEGP NCQFEVCQPN VPQLFSNDRK SLLMVVETTR
     QNSDTVNQLI ANLKNIVSAV TNNMPLWFTN FGLVTFDTTG RTFEKFDYTS IDDLITDLTT
     QSNAISTDGV CSMPYLGVLA HLLEHDDVIA MPNSEIFLVT PAGPSDLGNY VETMEVLFNT
     QAHLHYVVSK TANCATFDGV NNVRDMTWLG YGSSGNILFT DPANIVNLFN SYLPTLYGAS
     VLQDPTGITN YTCSDGSLPW FVPVDINTTF IYVTTSAEFG SLSVKDPLGA AHSATPVYNV
     NDQKIYAIEV DRLGGIWTLQ LVQPPGLCLA HVYSTGGAKV YTKFSMPNPI GGKPDPLGSH
     QDGRFVQPTA GFDNVAVFHL AGNPFHRGQL QYVEIFDIGA NSITNILRSE LYVRAGCSYE
     YYSDLFTCNG DMIAVYVHGV DEANQKFRRQ EIVICNGRSP TTNQPATGTI GPITMPTQQT
     ALTQGPVTQQ TQVPGTQPTQ GPVATTQNPY TSAQFDVVFM IDGSQSAQSS FDSLTKFVQT
     FMVSFNVGQS GARVGLIVVG GDITNPIPPA ANLNSLSSQA MLNSNLAQLS GGYTDFEDAG
     QILNYTLQIV SSPDFMAANN GYRSGISNHV LIYLTTTTAF DTDPTPAAQT ILAQKQYGII
     TIGYGGATDN NKLQTISGGS ACSFTAPDFA SLNNQIKTIQ QLILNANANG GVYCINN
//
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