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Database: UniProt
Entry: A0A261C1W6_9PELO
LinkDB: A0A261C1W6_9PELO
Original site: A0A261C1W6_9PELO 
ID   A0A261C1W6_9PELO        Unreviewed;       534 AA.
AC   A0A261C1W6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=EGF-like domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=FL83_09604 {ECO:0000313|EMBL:OZG15975.1};
OS   Caenorhabditis latens.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG15975.1, ECO:0000313|Proteomes:UP000216463};
RN   [1] {ECO:0000313|EMBL:OZG15975.1, ECO:0000313|Proteomes:UP000216463}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX534 {ECO:0000313|EMBL:OZG15975.1,
RC   ECO:0000313|Proteomes:UP000216463};
RA   Fierst J.L.;
RT   "Caenorhabditis latens genome sequence.";
RL   Submitted (JUL-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OZG15975.1}.
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DR   EMBL; NIPN01000050; OZG15975.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261C1W6; -.
DR   STRING; 1503980.A0A261C1W6; -.
DR   Proteomes; UP000216463; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   CDD; cd00054; EGF_CA; 3.
DR   CDD; cd00109; Kunitz-type; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 2.
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   PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR   PANTHER; PTHR24049:SF22; DROSOPHILA CRUMBS HOMOLOG; 1.
DR   Pfam; PF00008; EGF; 2.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF00014; Kunitz_BPTI; 2.
DR   SMART; SM00181; EGF; 3.
DR   SMART; SM00179; EGF_CA; 3.
DR   SMART; SM00131; KU; 2.
DR   SUPFAM; SSF57362; BPTI-like; 2.
DR   SUPFAM; SSF57196; EGF/Laminin; 3.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 2.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS01187; EGF_CA; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000216463}.
FT   DOMAIN          8..48
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          70..126
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   DOMAIN          165..227
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   DOMAIN          305..344
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          348..392
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          423..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..443
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..496
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        315..332
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        334..343
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        382..391
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:OZG15975.1"
SQ   SEQUENCE   534 AA;  61265 MW;  84CDDE4494F02B33 CRC64;
     MRRTNMENID ECRGYKAVCD KNAWCVNEIG SYKCECMASY RGDGKHCTYV GLGRSSIDCK
     DCSIHATYSC LDKFDHDYKD TCSNENWRPH FYFNHQTRMC EQFWYDGCRG RSRNIFSEYD
     TCTAMCEETN VLTRADAMIP RGHHITSHNH VITQRRSRRL DDRRCSLDFR ISLIVFTQLV
     LLIDCRQWQQ RYYFDHASLT CRQFWFDGCR SDSRNIFDDQ LTCQWLCESQ PMYKSRSCLE
     DFDEGLKKEC NGGRWRQQYY FDKGSKLTCL HTCENPAKKD PKKPWHNNDK FKMKEIIGDI
     YKPNVTDTCL AKNPCKHNGT CIFVWKKDTH YCKCQPGYHG NNCEKIVDFD PCAEKPCLNG
     ATCQLKYNDD DVDEKPTYEC FCAAGFGGPK CDERPCETNP CLNNGTCRTT KGYKTGGGIG
     GASGTGLKAP AGNGTTESGG GGSSGEKSGE KKSGKNKKNP ATRKREREER EKKEAEIQAA
     EEEEKQRKDY EEELQRKKAE EMELEAKKAL ETANSGIHLM PLALILALVL LRDI
//
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