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Database: UniProt
Entry: A0A067DD80_CITSI
LinkDB: A0A067DD80_CITSI
Original site: A0A067DD80_CITSI 
ID   A0A067DD80_CITSI        Unreviewed;       377 AA.
AC   A0A067DD80;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS50026};
GN   ORFNames=CISIN_1g017103mg {ECO:0000313|EMBL:KDO36977.1};
OS   Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX   NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO36977.1, ECO:0000313|Proteomes:UP000027120};
RN   [1] {ECO:0000313|EMBL:KDO36977.1, ECO:0000313|Proteomes:UP000027120}
RP   NUCLEOTIDE SEQUENCE.
RG   International Citrus Genome Consortium;
RA   Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA   Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA   Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M8 family.
CC       {ECO:0000256|ARBA:ARBA00005860}.
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; KK792377; KDO36977.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067DD80; -.
DR   STRING; 2711.A0A067DD80; -.
DR   MEROPS; M08.A01; -.
DR   Proteomes; UP000027120; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 2.30.34.10; Leishmanolysin domain 4; 1.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR013111; EGF_extracell.
DR   InterPro; IPR001577; Peptidase_M8.
DR   PANTHER; PTHR10942; LEISHMANOLYSIN-LIKE PEPTIDASE; 1.
DR   PANTHER; PTHR10942:SF0; LEISHMANOLYSIN-LIKE PEPTIDASE; 1.
DR   Pfam; PF07974; EGF_2; 1.
DR   Pfam; PF01457; Peptidase_M8; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027120};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          154..186
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DISULFID        158..168
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        176..185
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   377 AA;  40406 MW;  9A890081645271BA CRC64;
     MLAIAGGQSS LADYCTYFVA YSDGSCTDTN SARAPDRMLG EVRGSNSRCM ASSLVRTGFV
     RGSMTQGNGC YQHRCVNNSL EVAVDGIWKV CPEAGGPVQF PGFNGELICP AYHELCSTGP
     IAVFGQCPNS CTFNGDCVDG KCHCFLGFHG HDCSKRSCPD NCNGHGKCLS NGACECENGY
     TGIDCSTAVC DEQCSLHGGV CDNGVCEFRC SDYAGYTCQN SSKLISSLSV CKYVLEKDAG
     GQHCAPSESS ILQQLEEVVV TPNYHRLFPG GARKLFNIFG TSYCDEAAKR LACWISIQKC
     DKDGDNRLRV CHSACQSYNL ACGASLDCSD QTLFSSKEEG EGQCTGSSDI RLSWLDRLRG
     GLYLKNSSSK GMFVKSS
//
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