ID G0MY36_CAEBE Unreviewed; 2046 AA.
AC G0MY36;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=CBN-MEC-1 protein {ECO:0000313|EMBL:EGT47151.1};
GN Name=Cbn-mec-1 {ECO:0000313|EMBL:EGT47151.1};
GN ORFNames=CAEBREN_24767 {ECO:0000313|EMBL:EGT47151.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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; GL379819; EGT47151.1; -; Genomic_DNA.
DR STRING; 135651.G0MY36; -.
DR EnsemblMetazoa; CBN24767.1; CBN24767.1; WBGene00163492.
DR eggNOG; KOG4295; Eukaryota.
DR HOGENOM; CLU_234018_0_0_1; -.
DR InParanoid; G0MY36; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0050976; P:detection of mechanical stimulus involved in sensory perception of touch; IEA:EnsemblMetazoa.
DR GO; GO:0043062; P:extracellular structure organization; IEA:EnsemblMetazoa.
DR GO; GO:0007638; P:mechanosensory behavior; IEA:EnsemblMetazoa.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00109; Kunitz-type; 8.
DR CDD; cd21630; Kunitz_TAP-like; 3.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 15.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR PANTHER; PTHR10083:SF377; BPTI_KUNITZ INHIBITOR DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00014; Kunitz_BPTI; 13.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00131; KU; 15.
DR SUPFAM; SSF57362; BPTI-like; 15.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 4.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 15.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..2046
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012294007"
FT DOMAIN 50..100
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 195..233
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 239..296
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 401..461
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 617..677
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 882..938
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1129..1185
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1277..1334
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1346..1402
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1413..1469
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1495..1551
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1571..1621
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1634..1691
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1711..1765
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1777..1827
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1835..1886
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 817..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2046 AA; 234079 MW; B1E35732A9E8762F CRC64;
MIHFLLLLYL PFSHAAKDLA WYSTSNGVGG LSSRSVINPP LQAATAIDFC QLPVDTGKCS
QQLVRYYYDA VVDECKRFTF SGCGGNSNRF MRRAHCRNRC VKQPNKLEFQ ELKHRRTVTT
STPIPLKKVE EVTEETTTAT EKRQPVTVPV RKVDIVQSGH ENGLCQDCDP LYGTCIDGKC
GCMKGFRSLG KVCIDLNECD NGAVCGPNAR CVNEIGSFQC VCDAGFSTDG DCKIGQEACM
DEFDVNLTEE DCNNGKQEIK YYYDSESVQC KQFFYGGCKT KSRNFFADLQ TCDVICVSNQ
RDYLESKGQS LHHPTHQLSS EVTNELKSNH YKIDLFSSPS SPVRPNRPLS ADDWPLKPVT
LKPALNLDFT EGHTKSTDEK IREAKDAEKL VKELTPDHNI CDLKFEPVLR EECISADWAE
KFFWNSEFRD CEPFWYDSSC DPRDRAGKNY FETFEECKKR CDGAHESTYI TPTDIAKEVD
HEVEERKENE EERKIVEEEE KFEATTKAPE KEDDENGFFF KVKPQNYLED VLSTEKDDAL
NKPNGFNPNE FLKMNIEKVS DDGLKKIVPK VVPAEENKEE DNMKREDKIE HDILDNLKKK
EEKETEGEVI LSKPSTCELE YDADLRNECT SADWTELFYW NEQFKECEAF WYDSSCGEPD
YEKKNLFKNW DDCNNKCVKK IGKTATSEIH SNILIFVNNY TETIPFITTT TSTTTTTATT
TATLTTSSIM LEETRRPSYN QNDPLNLILN KALKPDESSE LPEKFPPNHE KTFVNFALKS
EVTATTKFDR LKYMAEFRKK LLALPDNFST TVKLISPTSV PSTTSKKSTS TAQETTVTQT
PKTTTSMDSI ETTTTSFDDF VEAEKKRVLE TIKILDRPDD LCDEPLHPKL EEDCKNDQWE
IKWFFNSDRS ACKSFWYGGC EVESRNFFPD HANCRHTCAH KYGTPASFSP KVFIPLGDLS
TPVPPRKDRL TTSLKLTYPH SEDLFPNQNH VSVVELDGNF QRLEEQDRLR LSPTKAYKQR
DQVPTEPNIV NISEGDKMEI APAFYSHIDR VVHDMKSGGH PGYTKPEEFV RRIEAASNDY
IKYDFQKPEV VTVIDKSPPT VPTRPAKETT VKSDPTTRMP STRSINDPCD DEYDPKWDED
CLGDSWVVRS YYDPKAEKCK AFWYGGCHTS SRNIWFDKET CRTSCAHKFP TELPMFGGSQ
SGESPESTAE FVIASEAPSA SSSSVSSSSN TAHISPEHRF KVDLNQKLAD IKKEHEGRED
LDYSKMVQHP VTVAADCLEV FNQSLSKPCG DGKSWSNRYY YDKDTRSCRM FWSNGCFDSS
KNNFDDLETC QWKCEGRHPQ PAGKSCLDKF DERYLEDCRH GEFTNRFYFD HDRKKCVAFH
WGGCQAKSQN FFADMNVCQD LCESPPREIT QACIQPFDKT YENSCSAEKP QQYYYFDSSS
GICKMFWFGN CKGENENIFS TLESCQWICE RKREERKPGK YFLEKLHQRS FSAICADKFD
QKYTESCGNS QWTEKWYFDQ SSGDCTSFWW DGCTSSSQNI FPDEKSCTSN CKHPGFEISS
KLESEDSKFR CLEPVEIGNC QETYPAFYYD RTSRSCRPFA YSGCGGNSNR FMTVSQCENL
CFAFNSMNEA EVDCHLPMHI GYGKNEDSCL PQAGFRFYYD RNYGKCSQMW YLGCGGNANN
FYSYEICQRT CSQSDQPREL ERKTRASSEV CFEAAGDRGI CGKNSSTYPL QRWTYGAQKC
TSFTYSGCGG NRNRFASQDL CEKTCKGLLN SNDPRICSFP PDWGSCNQLR YVWFYNLTRG
TCDQFLYGGC GGNPNRFETF EICQKACEVT GTDPCMESLD RGSWCEAMSN RYYFNKRARQ
CKGFHYTGCG KSGNNFLTKE ECQTKCEKRF PRAAPAASKK KTKVKLPVGY SGSKPKDKTP
MLRHINLNGF NQTYFKSEPQ WMDYTSCYGY RYNVSGRDTV LNVHYCSLRG SSDCISESYR
TTEGEEYCNI LRPFLRGQNL YSFYFGLDSV NPLYRPRDGL SGRIQRKNET IAAVLVLKAN
HCHEIC
//
