ID H0VIG6_CAVPO Unreviewed; 959 AA.
AC H0VIG6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Signal peptide, CUB domain and EGF like domain containing 2 {ECO:0000313|Ensembl:ENSCPOP00000009997.3};
GN Name=SCUBE2 {ECO:0000313|Ensembl:ENSCPOP00000009997.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000009997.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000009997.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000009997.3};
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 EMBL; AAKN02053661; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02053662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02053663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0VIG6; -.
DR STRING; 10141.ENSCPOP00000009997; -.
DR Ensembl; ENSCPOT00000011222.3; ENSCPOP00000009997.3; ENSCPOG00000011118.4.
DR VEuPathDB; HostDB:ENSCPOG00000011118; -.
DR GeneTree; ENSGT00940000153185; -.
DR HOGENOM; CLU_013079_0_0_1; -.
DR InParanoid; H0VIG6; -.
DR OMA; CVETKDP; -.
DR TreeFam; TF351672; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000011118; Expressed in ovary and 8 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0097108; F:hedgehog family protein binding; IEA:Ensembl.
DR GO; GO:0003413; P:chondrocyte differentiation involved in endochondral bone morphogenesis; IEA:Ensembl.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; IEA:Ensembl.
DR GO; GO:0045778; P:positive regulation of ossification; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; 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; 1.
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; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 4.
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:UP000005447};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..959
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013379698"
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 769..881
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DISULFID 363..373
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 959 AA; 105611 MW; 8F5164985897D156 CRC64;
MGVAGRGRPG AARALLLSLP LLLAAAGPPG PGRAAGPPED IDECAQGLDD CHADALCQNT
PTSYKCSCKP GYQGEGRQCQ DIDECENELN GGCVHDCLNI PGNYRCTCFD GFMLAHDGHN
CLDVDECLEN NGGCQHTCVN AMGSYECRCK EGFFLSDNQH TCIHRSEEGL SCMNKDHGCS
HICKEAPRGS VACECRPGFE LAKNQRDCIL TCNHGNGGCQ HSCEDTAEGP ECSCHPQYKL
HTDGRSCFER EDTGLEVTES NATSVADGDK RVKRRLLMET CAVNNGGCDR TCKDTSTGVH
CSCPVGFTLQ LDGKTCKDID ECQTRNGGCD HFCKNTVGSF DCSCKKGFKL LTDEKSCQDV
DECSLDRTCD HSCLNYPGTF ACACDPGFTL YGFTHCGDTN ECSDNNGGCQ QVCVNTVGDY
ECQCHPGYKL HWNKKDCVEV KGFLPTSVLP HVSLLCSKSG GGDRCFLRCH SGIRISSEKH
SSVKESFRYV NLTCSSGKQV LGAPGRPSTP KEMFLTVEFE RETYQKEVTA SCDLSCIAKR
TEKRLRKALR TLRKAVHREQ FHLQLSGMDL DVAKKSPRAS EWRAESCGVG QGHVGNQCVS
CRAGTYYDGA QERCILCPNG TFQNEEGQVT CEPCPRPENI GALKTSEAWN VSECGGLCQP
GEYSVDGFAP CQLCALGTFQ PEAGRTSCFS CGGGLPTKHL GATSFQDCET RVQCSPGHFY
NTTTHRCIRC SSGTYQPEFG KNSCVSCPGN TTTDFDGSTN ITQCKNRRCG GELGDFTGYI
ESPNYPGNYP ANTECTWTIN PPPKRRILIV VPEIFLPIED DCGDYLVMRK TSSSNSVTTY
ETCQTYERPI AFTSRSKKLW IQFKSNEGNS ARGFQVPYVT YDEDYQELIE DIVRDGRLYA
SENHQEILKD KKLIKALFDV LAHPQNYFKY TAQESREMFP RSFIRLLRSK VSRFLRPYK
//
