ID A0A093JY57_STRCA Unreviewed; 992 AA.
AC A0A093JY57;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Signal peptide, CUB and EGF-like domain-containing protein 1 {ECO:0000313|EMBL:KFV83344.1};
DE Flags: Fragment;
GN ORFNames=N308_04062 {ECO:0000313|EMBL:KFV83344.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV83344.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV83344.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV83344.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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; KL206553; KFV83344.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093JY57; -.
DR STRING; 441894.ENSSCUP00000015186; -.
DR Proteomes; UP000053584; 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:SF4; SIGNAL PEPTIDE, CUB AND EGF-LIKE DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 2.
DR Pfam; PF07699; Ephrin_rec_like; 3.
DR Pfam; PF14670; FXa_inhibition; 3.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 7.
DR SMART; SM01411; Ephrin_rec_like; 3.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 5.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS01186; EGF_2; 4.
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:UP000053584};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..41
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 85..121
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 280..320
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 321..359
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 802..914
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 325..335
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV83344.1"
FT NON_TER 992
FT /evidence="ECO:0000313|EMBL:KFV83344.1"
SQ SEQUENCE 992 AA; 109829 MW; 947F45DBDCD39FC8 CRC64;
DVDECAEATD DCHIDAICQN TPKSYKCICK PGYKGEGKQC EDIDECENDF YNGGCVHECI
NIPGNYRCTC YDGFMLAHDG HNCLDVDECQ DNNGGCQQIC VNTMGSYECQ CKEGFFLSDN
QHTCIHRSIE GMNCMNKDHG CAHICRETPK GGVACECRPG FELAKNQKDC KLTCNYGNGG
CQHTCDDTDT GPVCGCHQKY ALHSDGRTCI EKDEAAIESS EYNATSVADV DKRVKRRLLM
ETCAVNNGGC DRTCKDTATG VRCSCPVGFT LQPDGKTCKD IDECLVNNGG CDHFCRNTVG
SFECSCQKGY KLLTDERTCQ DIDECSFERT CDHTCINYPG SFECLCHKGY TLYGLTHCGD
IDECSISNGS CDYGCLNTMG SYECVCPPGK KLHWNKKDCV EMVKCLPNGK PAAKAQLVCS
KTGGIESCFL SCPSNTLFVP DSENSYTLSC GVPGPQGKAP PKRNATLPSC ADSLAPPIKQ
KARFKIKDAK CHLRPRSKEK AKESGKQAVL DNCQVTFVNL KCDSSKKKRR GRKSPSKEVS
HITAEFEVEM KSEEVSDTCN IDCVRKRMEQ KLQTAIKTLR KSINKQQFYI QFSGTDYEVA
QKPAKATEGH EACSTGQVLQ EGKCVTCSTG TFYSGEHNQC VPCSPGTYQD TEGQLTCEPC
PSNDGQGVAG ARNVSECGGK LNSIIRRVGQ CSPGHYSSDG FKPCRVCPLG TYQPEPGRTL
CFPCGGGLVT KYEGAVSFQD CETKVHCSPG HYYNSTTHRC IRCPVGTYQP EFGQNYCITC
PGNTSTDFDG STNVTHCKNQ HCGGELGDYT GYIESPNYPG DYPANVECIW NINPPPKRRI
LIVVPEIFLP IEDECGDVLV MRKSASPTSI TTYETCQTYE RPIAFTSRSR KLWIQFKSNE
GNSGKGFQVP YVTYDEDYQQ LIEDIVRDGR LYASENHQEI LKDKKLIKAL FDVLAHPQNY
FKYTAQESKE MFPRSFIKLL RSKVSRFLRP YK
//
