ID A8WZP0_CAEBR Unreviewed; 2226 AA.
AC A8WZP0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 2.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=Protein CBR-CLEC-78 {ECO:0000313|EMBL:CAP25850.2};
GN Name=clec-78 {ECO:0000313|WormBase:CBG05359};
GN Synonyms=Cbr-clec-78 {ECO:0000313|EMBL:CAP25850.2};
GN ORFNames=CBG05359 {ECO:0000313|WormBase:CBG05359}, CBG_05359
GN {ECO:0000313|EMBL:CAP25850.2};
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238 {ECO:0000313|EMBL:CAP25850.2, ECO:0000313|Proteomes:UP000008549};
RN [1] {ECO:0000313|EMBL:CAP25850.2, ECO:0000313|Proteomes:UP000008549}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16 {ECO:0000313|EMBL:CAP25850.2,
RC ECO:0000313|Proteomes:UP000008549};
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; HE601337; CAP25850.2; -; Genomic_DNA.
DR STRING; 6238.A8WZP0; -.
DR WormBase; CBG05359; CBP40473; WBGene00027820; Cbr-clec-78.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG4297; Eukaryota.
DR HOGENOM; CLU_238488_0_0_1; -.
DR InParanoid; A8WZP0; -.
DR OMA; LANRNQC; -.
DR OrthoDB; 5474074at2759; -.
DR Proteomes; UP000008549; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProt.
DR CDD; cd00033; CCP; 4.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd00041; CUB; 3.
DR CDD; cd00054; EGF_CA; 4.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 5.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 3.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR003410; HYR_dom.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR PANTHER; PTHR45656:SF15; -; 1.
DR PANTHER; PTHR45656; PROTEIN CBR-CLEC-78; 1.
DR Pfam; PF00431; CUB; 3.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF07699; Ephrin_rec_like; 3.
DR Pfam; PF02494; HYR; 2.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 4.
DR SMART; SM00032; CCP; 8.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00042; CUB; 3.
DR SMART; SM00181; EGF; 5.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM01411; Ephrin_rec_like; 3.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00192; LDLa; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 5.
DR SUPFAM; SSF57196; EGF/Laminin; 5.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 3.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01180; CUB; 3.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50825; HYR; 2.
DR PROSITE; PS01209; LDLRA_1; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50923; SUSHI; 5.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000008549};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..2226
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002729744"
FT DOMAIN 55..180
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 218..337
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 341..451
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 452..567
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 588..650
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 651..711
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 712..772
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1054..1113
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1190..1251
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1308..1453
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 1479..1565
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DOMAIN 1566..1647
FT /note="HYR"
FT /evidence="ECO:0000259|PROSITE:PS50825"
FT DOMAIN 2060..2096
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2098..2134
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2136..2174
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2176..2214
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 184..196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 191..209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 203..218
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 452..479
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
FT DISULFID 714..757
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 743..770
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 1084..1111
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 2086..2095
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2124..2133
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2145..2162
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2164..2173
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2204..2213
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2226 AA; 243410 MW; 88191D6568101920 CRC64;
MHENCRKRRL LTEVVFVVLL LLIEPTQSSS SSSKFTPPSQ VTDVELKCPD EWIRLGTKCY
LPFNIHQSWP FALTTCQRYG STLAKIQTGS ENQFIANLLS KPGGKMGEIK EYWIGLTVEV
LDDDELYIWS DGTPTSRYVG FWRQDQPNFL NGTCAMGRVE RKDLEWRLET CNLLRRFVCE
RPACVQGSYF CSSGSCISES KKCNGFNDCD DGSDEQNCPS AFQPACRTYE KGESGQLSSP
NYPNSYDPNL NCRYVLEGPV NSRIELTIEH FETEPVFDVL TVLDGGPAEN STTVIKRLSG
SFETAQTITS STNMMIVQFR SDAQSNARGF QLKWRAIPFS CGGHYIAQAY IQPFVSPGYP
KTFANGAECV WTVETTPGQV ISLILDDFSL GAEDNLIIYN GPTPSATVLA SFSGNLTTKK
YVTSSTSHIY IYMMTRQNSN SRGFSISYKR GCDLSMSDVL GEIISPGYLS SEYPNDVQCT
YTIETEDQKA DRSISLIAQR FDLADGDTVR VFENSVSKGK ALHENDGFGL KTKPEKQIDS
NSNRIQMVFK SGSSRQAMGF NFSYSIVTAQ QTKSLKLSII PIPNLLFPDC PAFPSVPMVT
LSTKQRSVST RVTVSCPIGF EFASGEGISK TVVCLMGGKW SQSHISTCQP IYCGAVPQIA
NGYVDSATNV SFGGQVKYSC HKGFFFSSGK DIETVYCGEL GKWNTPPPCK AATCQPLTQF
TNGERRLEFG DGTGYGSVFR YDCHSGYRRE GVESLLCKSD GTWSSKQPSC TSELKILFIP
VFGLVFFVKS LAHISQKSRM PESRFPIDSY LVTSLVSSAT LASQLTDLKR YCSFSDFQNF
QKTMSSDPLP GQSDCLLNPQ LMCLESQPIE TGSSNFCPDP KSTDKKIKVL KFAIPMIVEQ
IRFTNQRNGK IQKISVKYSE SNKSRTKKLQ IDNQSIFGVD DDDVATLPMA LEVQVLEIEA
VGMEGTPCVE VEALGCQRTS CADINECLKN NGHCDHLCIN TQGSYKVRGI FWCACRNGYD
LFMENGQSGV NVSAGETGNN VNDLIRFEKS CVPRQCEHIG SPENGQLLST AKNFEFPMIV
QFQCDFGYQM MGPDYIQCLA DGTWNGTEPF CLPATCQGIE QLPSKSDGLH VTPNNSTITF
GQNVSISCTL PNRPGRPNSA LFSYRQCIFD PKDDGRDYWL SGPPPECSFI ECPAPPTMPG
AVYVGDVTDR KMGSTLEFTC RQPYTVAGRS DRTIKCSSDA TWDLGDLRCE GPVCVDPGYP
YDGQVSLFVG IVELESVEEG AIARFSCKRP GFVPFPSDTL QCALGASCVL SEDVGIVSGF
VPDGAFSDNS DSTNLGYEPH HARMGSSGWC GAKEDFIFLS VDLQRVYTLT TLRIAGVAGS
GHLKGHVTKF QLFYKTQNQN KYEPYPVEFE SPAGNHNAMH HFDLKFSLRA RYILFGVTEY
EGNPCMKFDL MGCVAPVFAA HEVDSHLQIG WNGSVPQCVD MDPPKFENCP ESEIFAKVDE
NGQLKAVEFE EPVASDNSGK IAYTQIEPLG MRSGLMITSD MDITYTAYDS AGNTAVCTLK
IRIPDTQPPV MKCPDSYTIP VGNSTKHVIF DMTTVDLVLH DTSNVSEVTF SPTEATLKIG
EFVEVTAQAE DENGNRNSCK FQVAYAPEAC SPASLASSNH IVKNCVHEDG AVVCSVYCAQ
GYRFIDPDQI TQNFVCKDGR WSPRNNAPAC VPIPKDPAGF HVNVGMTYPV LSPVPDHCLK
GYAELAAKEF DNLDKVLSAR CSSSVEVFVR LLKLDFSNLN GQLIGNYTIQ VLPTEQQSVF
YDLCGLTLRT IFDLNIPGAN QPIQSLLSLS GESIASQTAG CPSITAKGSS IVQGFACGTG
EVLRQEAKDR LPECSKYFVG NFCRKFQGLS NHMPFFLVAC PSGSVNINNT CILCPRGSYQ
DDSGQTSCKP CPDGTYTLDE GSQSVASCLS TCGYGMYSTT GLIPCQLCPR HTFSGPAPVG
GFRDCEACPS GAYTAKLGAS SATECRLACK TGSYSNTGLE PCSPCPINFY QPALGQQSCL
ECSNATATQG SGESLESACF PIDCSAKMCE NNADCSVFMH RAQCHCKPGY VGDRCEIVED
VCATQPCYNG GKCEQVGTTY KCTCPKMFSG ARCQFESDEC VGKTCPNGGV CHDLPGLKST
TCLCRTGFAG PNCEEITDIC STNNPCRNGA RCIGEKLGRF KCQCVPGWEG PTCDNNIGEG
KKFGRS
//
