ID F1MJF1_BOVIN Unreviewed; 1018 AA.
AC F1MJF1;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 3.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Signal peptide, CUB domain and EGF like domain containing 1 {ECO:0000313|Ensembl:ENSBTAP00000037465.5};
GN Name=SCUBE1 {ECO:0000313|Ensembl:ENSBTAP00000037465.5,
GN ECO:0000313|VGNC:VGNC:34371};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000037465.5, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000037465.5, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000037465.5,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000037465.5}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000037465.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; F1MJF1; -.
DR STRING; 9913.ENSBTAP00000037465; -.
DR PaxDb; 9913-ENSBTAP00000037465; -.
DR Ensembl; ENSBTAT00000037639.5; ENSBTAP00000037465.5; ENSBTAG00000011275.6.
DR VEuPathDB; HostDB:ENSBTAG00000011275; -.
DR VGNC; VGNC:34371; SCUBE1.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000153185; -.
DR HOGENOM; CLU_013079_0_0_1; -.
DR InParanoid; F1MJF1; -.
DR TreeFam; TF351672; -.
DR Reactome; R-BTA-1474228; Degradation of the extracellular matrix.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000011275; Expressed in trachea and 74 other cell types or tissues.
DR ExpressionAtlas; F1MJF1; baseline.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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; 3.
DR SUPFAM; SSF57184; Growth factor receptor domain; 3.
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; 2.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1018
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018674904"
FT DOMAIN 33..73
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 353..391
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 828..940
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 357..367
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1018 AA; 111158 MW; 143C4559F3CD6969 CRC64;
MGAAAVRWHL CVLLALGARG RLAGGSGLPG AVDVDECSEG TDDCHIDAIC QNTPKSYKCL
CKPGYKGEGR QCEDIDECEN DHYNGGCVHE CINIPGNYRC TCFDGFMLAH DGHNCLDVDE
CQDNNGGCQQ ICVNAMGSYE CQCHSGFFLS DNQHTCIHRS SEGMNCMNKD HGCAHICRET
PKGGVACDCR PGFDLAQNQK DCTLTCNYGN GGCQHSCEDT DTGPTCGCHQ KYALHSDGRT
CIEKDEAAIE RSQFNATSVA DVDKRVKRRL LMETCAVNNG GCDRTCKDTA TGVRCSCPVG
FTLQPDGKTC KDINECLVNN GGCDHFCRNT VGSFECGCRK GYKLLTDERT CQDIDECSFE
RTCDHTCINS PGSFQCLCHR GYTLYGTTHC GDVDECSMNN GSCDQGCVNT KGGYECVCPP
GRRLHWNRKD CVETGRCLSR AKASPPAQLS CGKAGSVESC SLACPGHTLF TPDSDNSYSL
SCGVPSLQGK ALQKRNGTSS STGPSCSGAP ATLIRQKARF KIRDAKCHLR PRSQEPAKEA
PRQLLLENCH MTFVTLKCDS SKKRRRGRKS PSKEVTHITA EFEVETKVEE ASDTCEADCV
RRRAEQSLQA AIKTLRKSLS RQHFSVQVAG TEYELAQRPA KAPEGPGTCG PGHTPQDGKC
VACGPGTYFS GEPGQCVPCP PGTYQDRVGQ LSCTPCPSSD GLGLAGARNV SECGGQCSPG
SFSTDGFRPC QACPMGTYQP EPGRTGCFPC GGGLLTKHEG SASFQDCEAK VHCSPGHHYN
TTTHRCIRCP VGTYQPEFGQ NHCITCPGNT STDFDGSTNV THCKNQHCGG ELGDYTGYIE
SPNYPGDYPA NAECVWHISP PPKRRILVVV PEIFLPIEDE CGDVLVMRKS ASPTSITTYE
TCQTYERPIA FTSRSRKLWI QFKSNEGNSG KGFQVPYVTY DEDYQQLIED IVRDGRLYAS
ENHQEILKDK KLIKALFDVL AHPQNYFKYT AQESKEMFPR SFIKLLRSKV SRFLRPYK
//
