ID Q5ZR36_CAEEL Unreviewed; 1818 AA.
AC Q5ZR36;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 159.
DE SubName: Full=Papilin {ECO:0000313|EMBL:CCD66557.1};
GN Name=mec-1 {ECO:0000313|EMBL:CCD66557.1,
GN ECO:0000313|WormBase:T07H8.4f};
GN ORFNames=CELE_T07H8.4 {ECO:0000313|EMBL:CCD66557.1}, T07H8.4
GN {ECO:0000313|WormBase:T07H8.4f};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD66557.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD66557.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD66557.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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; BX284605; CCD66557.1; -; Genomic_DNA.
DR RefSeq; NP_001024119.1; NM_001028948.3.
DR SMR; Q5ZR36; -.
DR EnsemblMetazoa; T07H8.4f.1; T07H8.4f.1; WBGene00003165.
DR UCSC; T07H8.4a; c. elegans.
DR AGR; WB:WBGene00003165; -.
DR WormBase; T07H8.4f; CE37673; WBGene00003165; mec-1.
DR HOGENOM; CLU_234018_0_0_1; -.
DR OrthoDB; 2879873at2759; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00003165; Expressed in larva and 2 other cell types or tissues.
DR ExpressionAtlas; Q5ZR36; baseline and differential.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0043062; P:extracellular structure organization; IMP:WormBase.
DR GO; GO:0007638; P:mechanosensory behavior; IMP:WormBase.
DR GO; GO:0009612; P:response to mechanical stimulus; IMP:WormBase.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00109; Kunitz-type; 7.
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; 14.
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; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR PANTHER; PTHR10083:SF217; PROTEIN CBG23496; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00014; Kunitz_BPTI; 12.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00181; EGF; 1.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00131; KU; 14.
DR SUPFAM; SSF57362; BPTI-like; 14.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 3.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 14.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
PE 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|EPD:Q5ZR36,
KW ECO:0007829|PeptideAtlas:Q5ZR36};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT DOMAIN 13..51
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 57..114
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 222..282
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 426..486
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 670..726
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 915..971
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1065..1122
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1134..1190
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1201..1257
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1269..1325
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1345..1395
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1408..1465
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1485..1539
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1551..1601
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1609..1660
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 498..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1818 AA; 207464 MW; A567060663701234 CRC64;
MKGFRSLGKV CIDLNECDNG AVCGPNARCV NEIGSFQCVC DAGFSTDGDC KIGQEACMDE
FDVNLTEEDC NNGKQEIKYY YDADSVQCKQ FFYGGCKTTS RNFFADLQTC DVICVSNQRD
YLKSKGQSLS HHPVLEISSD LNNGNDLKSN HYKIDLFSSP SSPVTPNRPL SADDWPLKPI
TLKPALNLDF SQGKTKSTAE KHKEADDAEI LVHQLTPEHN SCDLKFEPVL REECISADWA
EKFFWNSEFK DCEPFWYDSS CDPRDRAGKN FFETFEDCKN KCDGVQSQYV VPITTVPDEQ
SKIEEVETSE TPGIVDETTT TAAPEEESEE NGFFFKVKPQ NYLEDVLSSE TEETQHYGFN
PNEFLKQNSQ NQKPTEITEI LRILPAQTEH DEASELKKED KIEHDILEHL KNKEPTEKVL
STPSTCDLEY DDALRNECTS ADWTELYYWN AQFKECEAFW YDSSCGDQDF SKKNLFKNFD
DCNNQCVKKI GEALKKMDPE TTTTTSTTTT TTTAPTTTKM EEPKRSNYKQ SDPLNLILNK
ALNPDESSEL PEKFPPAHEQ GFVNFAIKSE VTATTKFDRL KYMAEFRKKL LALPDNFSTT
PKQSSPTSSP TTTRMRSPST HKSTVSQATK TASSTPQSPS TTTSFDDFVE KEKKTVLETI
KILDRPEDLC DEPLHPKLEE DCKNDQWEIQ WFFNSDRGAC KSFWYGGCEI ESRNFFPDHA
NCRHSCAHKY ATPASFSSKV YIPPGELSTP VPPRKDRLTT SLKLTYPHSE DLFPSEEHST
VVELDGNFQR TEKQERIRLF PTKTFRPRAP TPTASNIVNV SEGEKTETAP AFYSHIDRVV
HDMKTGEHPG YTKPEEFVRR IESASNDYIK YDLQKPDVVT IIDKSPPTVP SRKERTERTE
VTTKLPSTRS INDPCDDEYD PKWDEDCLGD TWVVRSYYDS KAEKCKAFWY GGCHTSSRNI
WFDKETCRTS CAHKFPTDMP MYGGAQSSEV SAEILPSPQE ENSSKETSSS SSSSSSSNTA
HISPEHRFKV DLDQKFADVK REHEGREDLA YSQMVQHPVT VSADCLEVYN ASLSKPCGDG
KSWSNRYFYD KDTRSCRMFW SNGCFSSSKN NFDDLETCQW KCEGRHPQPA GKSCLDKFDE
RYLEDCRHGE FTNRFYFDHD RKKCVAFHWG GCQSKSQNFF ADMTVCQDLC ESPPRELTQA
CLQPFDTTYE TSCSAEKPQQ YYYFDMSSGI CKMFWFGNCK GENQNIFSTL EACQWICERK
RDERKPAICA DKFDTKYTES CGDSQWTEKW YFDQSSGDCS SFWWDECTSS SQNIFPDEKS
CTSNCKHPGF EISSKLATEE SKFRCLEPVE IGSCQETYPA FYYDRASRTC RPFAYSGCGG
NSNRFMTVSQ CENLCFAFNS MNEAEVDCHL PMHIGYGKNE DSCLPQAGFR FYYDRNYGKC
SQMWYLGCGG NANNFYSYEI CQRTCSQSDV PRELERKTRA SSEVCFEPPG DRGICGKNSS
TNPLKRWTYG NQKCTSFTYS GCGGNRNRFA TQDICENTCN GLMNSNDPRI CSFSPDWGSC
NQLRYVWFYN LTRGTCDQFL YGGCGGNPNR FDTFEICQKA CEVTGTDPCM ESLDRGSWCE
AMSNRYYFNK RARQCKGFHY TGCGKSGNNF LTKEECQTKC EKRFPRAAPS KKKAKVKLPV
GYSGAKPKDK TPMLRHINLN GNNQTYFKSE PQWMDYSSCY GYRYNVTGRD TILNVHYCAI
RGSADCISES YRSTEGEEYC NILRPFLRGQ NLYSFYFGLD SVNPMYRPKD GLSGRIQRKN
ETIAAVLVLK ANQCHEIC
//
