ID A0A2K6R0N6_RHIRO Unreviewed; 976 AA.
AC A0A2K6R0N6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Signal peptide, CUB domain and EGF like domain containing 1 {ECO:0000313|Ensembl:ENSRROP00000034569.1};
GN Name=SCUBE1 {ECO:0000313|Ensembl:ENSRROP00000034569.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000034569.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000034569.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A2K6R0N6; -.
DR STRING; 61622.ENSRROP00000034569; -.
DR Ensembl; ENSRROT00000059015.1; ENSRROP00000034569.1; ENSRROG00000040822.1.
DR GeneTree; ENSGT00940000153185; -.
DR OMA; YQDVEGQ; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
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 CDD; cd00041; CUB; 1.
DR CDD; cd00054; EGF_CA; 3.
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; 3.
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:UP000233200};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 21..61
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 105..141
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 311..349
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 786..898
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 315..325
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 976 AA; 107187 MW; 331ADC866C4D824B CRC64;
TWGLGQRRRS LGGHGSHRSV DVDECSEGTD DCHIDAICQN TPKSYKCLCK PGYKGEGRQC
EDIDECENDY YNGGCVHECI NIPGNYRCTC FDGFMLAHDG HNCLDVDECQ DNNGGCQQIC
VNTMGSYECQ CHSGFFLSDN QHTCIHRSNE GMNCMNKDHG CAHICRETPK GGVACDCRPG
FDLAQNQKDC TLTCNYGNGG CQHSCEDTDT GPMCGCHQKY ALHSDGRTCI ETCAVNNGGC
DRTCKDTATG VRCSCPVGFT LQPDGKTCKD INECLVNNGG CDHFCRNTVG SFECGCRKGY
KLLTDERTCQ DIDECSFERT CDHICINSPG SFQCLCHRGY ILYGTTHCGD VDECSMNNGS
CDQGCVNTKG SYECVCPPGR RLHWNRKDCM ETGKCISRAK TSPRAQLSCS KVGGVESCFL
SCPAHTLFVP DSENSYVLSC GVPGPQGKAL QKRNGTSSGL GPSCSDAPAT PIKQKARFKI
RDAKCHLRPH SQARAKETAR QPLLDHCHVT FVTLKCDSSK KKRRGRKSPS KEVSHITAEF
EIETKMEEAS DTCEADCLRK RAEQSLQAAI KTLRKSIGRQ QFYVQVSGAE YEVAQRPAKV
LEGQGACGAG QVLQDSKCVA CGPGTHFGGE LSQCVPCMPG TYQDTEGQLS CTPCPSSDGV
GLAGARNVSE CGGQCSPGFF SADGFKPCQA CLVGTYQPEP GRTSCFPCGG GLLTKHEGTT
SFQDCEAKVH CSPGHHYNTT THRCIRCPIG TYQPEFGQNH CITCPGNTST DFDGSTNVTH
CKNQHCGGEL GDYTGYIESP NYPGDYPANA ECVWLIAPPP KRRILIVVPE IFLPIEDECG
DVLVMRKSAS PTSITTYETC QTYERPIAFT SRSRKLWIQF KSNEGNSGKG FQVPYVTYDE
DYQQLIEDIV RDGRLYASEN HQEILKDKKL IKALFDVLAH PQNYFKYTAQ ESKEMFPRSF
IKLLRSKVSR FLRPYK
//
