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Database: UniProt
Entry: A0A091D7E4_FUKDA
LinkDB: A0A091D7E4_FUKDA
Original site: A0A091D7E4_FUKDA 
ID   A0A091D7E4_FUKDA        Unreviewed;      1008 AA.
AC   A0A091D7E4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Signal peptide, CUB and EGF-like domain-containing protein 2 {ECO:0000313|EMBL:KFO18726.1};
GN   ORFNames=H920_19937 {ECO:0000313|EMBL:KFO18726.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO18726.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO18726.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO18726.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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; KN125342; KFO18726.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091D7E4; -.
DR   STRING; 885580.ENSFDAP00000015167; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00054; EGF_CA; 2.
DR   Gene3D; 2.10.25.10; Laminin; 9.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR   Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 3.
DR   InterPro; IPR026823; cEGF.
DR   InterPro; IPR000859; CUB_dom.
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; IPR024731; EGF_dom.
DR   InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR   PANTHER; PTHR24046; SIGNAL PEPTIDE, CUB AND EGF-LIKE DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR24046:SF3; SIGNAL PEPTIDE, CUB AND EGF-LIKE DOMAIN-CONTAINING PROTEIN 2; 1.
DR   Pfam; PF12662; cEGF; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF07699; Ephrin_rec_like; 3.
DR   Pfam; PF14670; FXa_inhibition; 5.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00181; EGF; 10.
DR   SMART; SM00179; EGF_CA; 8.
DR   SMART; SM01411; Ephrin_rec_like; 3.
DR   SUPFAM; SSF57196; EGF/Laminin; 3.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 3.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 5.
DR   PROSITE; PS01180; CUB; 1.
DR   PROSITE; PS01186; EGF_2; 5.
DR   PROSITE; PS50026; EGF_3; 4.
DR   PROSITE; PS01187; EGF_CA; 3.
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:UP000028990};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          26..66
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          109..145
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          345..383
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          384..424
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          818..930
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DISULFID        349..359
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1008 AA;  111102 MW;  ABE165B4EA7018D9 CRC64;
     MVLGRAKAIA HTIGLHARCL LYSFAEIDEC AQRLDDCHAE ALCQNTPTSY KCSCKPGYQG
     EGRQCEDIDE CENELNGGCV HDCLNIPGNY RCTCFDGFML AHDGHNCLDV DECLQNNGGC
     QHTCVNVLGS YGCLCREGFL LSDNQHTCIH LSEEGLSCMN KDHGCSHICK EAPRGSVACE
     CRPGFELAKN QRDCILTCNH GNGGCQHSCE DTAEGPECSC HPQYKLHPDG RSCLEQEDTA
     LEVTESNATS VADGDKRVKR RLLMETCAVN NGGCDRTCKD TSTGVHCSCP VGFTLQLDGK
     TCKDIDECQT RNGGCDHFCK NTVGSFDCSC KKGFKLLTDE KSCQDVDECS LDRTCDHSCL
     NHPGTFACAC DAGYTLYGFT HCGDTNECSD NNGGCQQVCV NTVGSYECQC HPGYKLHWNK
     KDCVEVKGFP PTRVLSYASL LCSKSGGGDR CLLRCHAGVR LSSGLQEAYS VTCGSSSLRS
     KQHKSNDSAF GDVATIRTSV TFKLNEGKCS LKKSEPFPEG LRSALPEKHS SVKESFLYAN
     LTCSSGKQVP GAPGRPSAHK EMFLTVEFER ETYQKEVTAS CDLSCISKRT EKRLRKALRT
     LRKAAHREQF HLQLSGMDLD VAKKSPRASE QRAEACGVGQ GHVENQCVSC KAGTYYDGAQ
     ERCILCPNGT FQNEEGQVAC DPCPRPENLG TLKTSDTWNV SLCGGLCQPG EYSADGFAPC
     QLCALGTFQP EAGRTSCFPC GGGLPTRHLG ATSFQDCETR VQCSPGHFYN TTTHRCIRCP
     AGTYQPEFGK NNCVSCPGNT TTDFDGSTNI TQCKSRRCGG ELGDFTGYIE SPNYPGNYPA
     NTECTWTINP PPKRRILIVV PEIFLPIEDD CGDYLVMRKT SSSNSVTTYE TCQTYERPIA
     FTSRSKKLWI QFKSNEGNSA RGFQVPYVTY DEDYQELIED IVRDGRLYAS ENHQEILKDK
     KLIKALFDVL AHPQNYFKYT AQESREMFPR SFIRLLRSKV SRFLRPYK
//
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