ID A0A2K6EI14_PROCO Unreviewed; 965 AA.
AC A0A2K6EI14;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Signal peptide, CUB domain and EGF like domain containing 2 {ECO:0000313|Ensembl:ENSPCOP00000001367.1};
GN Name=SCUBE2 {ECO:0000313|Ensembl:ENSPCOP00000001367.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000001367.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000001367.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A2K6EI14; -.
DR Ensembl; ENSPCOT00000004887.1; ENSPCOP00000001367.1; ENSPCOG00000004199.1.
DR GeneTree; ENSGT00940000153185; -.
DR Proteomes; UP000233160; Unplaced.
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; 2.
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; 2.
DR Pfam; PF14670; FXa_inhibition; 4.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00179; EGF_CA; 6.
DR SMART; SM01411; Ephrin_rec_like; 2.
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:UP000233160};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..965
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014343917"
FT DOMAIN 40..80
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 123..159
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 359..397
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 398..438
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 775..887
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 363..373
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 965 AA; 106156 MW; 2D0765493A0F2148 CRC64;
MGLAGRGCPG AARALLLLLS LLLAAAVPPG RGRAAGPPED VDECAQGLDD CHAEALCQNT
PASYKCSCKP GYQGEGRQCE DIDECENELN GGCVHDCLNI PGNYRCTCFD GFMLAQDGHN
CLDVDECLEN NGGCQHTCVN AMGSYECRCK EGFFLSDNQH TCIHRSEEGL SCMNKDHGCS
HICKEAPRGS VACECRPGFE LAKNQRDCML TCNHGNGGCQ HSCEDTTDGP ECSCHPHYRM
HVDGRSCLER EDTALEMAES NATSVADGDK RVKRRLLMET CAVNNGGCDR TCKDTSTGVH
CSCPIGFTLQ LDGKTCKDID ECQTRNGGCD HFCKNTVGSF DCSCKKGFKL LTDEKSCQDV
DECSLDRTCD HSCINHPGTF ACTCNQGYTL YGFTHCGDTN ECSVNNGGCQ QICVNTVGGY
ECQCHPGYKL HWNKKDCVEV KGLLPASVSP HVSLHCGKSG GGDRCFLRCH SGIHLSSGLQ
EAYSVTCGSS ALRNKQQKSN DSAFGDVATI RTSVTFKLNE GKCSLKKAEL FPEGLRPALP
EKHSSVKESF RYANLTCSSG KQVPGAPGRP SASKEMFITV EFELETNQKE VTASCDLSCI
VKRTEKRLRK AIRTLRKAAH REQFHLHLSG MDLDVAKKPP RTSERRAEPC GVGQGHAENQ
CGLCQPGEYS ADGFAPCQLC ALGTFQPEPG RTSCFPCGGS LPTKHQGATS FQDCETRVQC
SPGHFYNTTT HRCIRCPAGT YQPEFGKNNC VSCPGNTTTD FDGSTNITQC KNRRCGGELG
DFTGYIESPN YPGNYPANTE CTWTINPPPK RRILIVVPEI FLPIEDDCGD YLVMRKTSSS
NSVTTYETCQ TYERPIAFTS RSKKLWIQFK SNEGNSARGF QVPYVTYDED YQELIEDIVR
DGRLYASENH QEILKDKKLI KALFDVLAHP QNYFKYTAQE SREMFPRSFI RLLRSKVSRF
LRPYK
//
