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R-spondin-4 (Roof plate-specific spondin-4) (hRspo4)

 RSPO4_HUMAN             Reviewed;         234 AA.
Q2I0M5; A2A2I6; Q9UGB2;
16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
16-MAY-2006, sequence version 2.
13-FEB-2019, entry version 118.
RecName: Full=R-spondin-4;
AltName: Full=Roof plate-specific spondin-4;
Short=hRspo4;
Flags: Precursor;
Name=RSPO4; Synonyms=C20orf182;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=16357527; DOI=10.4161/cc.5.1.2305;
Kim K.-A., Zhao J., Andarmani S., Kakitani M., Oshima T.,
Binnerts M.E., Abo A., Tomizuka K., Funk W.D.;
"R-spondin proteins: a novel link to beta-catenin activation.";
Cell Cycle 5:23-26(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Glial tumor;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[5]
FUNCTION, AND INTERACTION WITH LGR4 AND LGR5.
PubMed=21909076; DOI=10.1038/embor.2011.175;
Glinka A., Dolde C., Kirsch N., Huang Y.L., Kazanskaya O.,
Ingelfinger D., Boutros M., Cruciat C.M., Niehrs C.;
"LGR4 and LGR5 are R-spondin receptors mediating Wnt/beta-catenin and
Wnt/PCP signalling.";
EMBO Rep. 12:1055-1061(2011).
[6]
FUNCTION, AND INTERACTION WITH LGR4; LGR5 AND LGR6.
PubMed=21727895; DOI=10.1038/nature10337;
de Lau W., Barker N., Low T.Y., Koo B.K., Li V.S., Teunissen H.,
Kujala P., Haegebarth A., Peters P.J., van de Wetering M.,
Stange D.E., van Es J.E., Guardavaccaro D., Schasfoort R.B., Mohri Y.,
Nishimori K., Mohammed S., Heck A.J., Clevers H.;
"Lgr5 homologues associate with Wnt receptors and mediate R-spondin
signalling.";
Nature 476:293-297(2011).
[7]
FUNCTION.
PubMed=29769720; DOI=10.1038/s41586-018-0118-y;
Szenker-Ravi E., Altunoglu U., Leushacke M., Bosso-Lefevre C.,
Khatoo M., Thi Tran H., Naert T., Noelanders R., Hajamohideen A.,
Beneteau C., de Sousa S.B., Karaman B., Latypova X., Basaran S.,
Yuecel E.B., Tan T.T., Vlaminck L., Nayak S.S., Shukla A.,
Girisha K.M., Le Caignec C., Soshnikova N., Uyguner Z.O.,
Vleminckx K., Barker N., Kayserili H., Reversade B.;
"RSPO2 inhibition of RNF43 and ZNRF3 governs limb development
independently of LGR4/5/6.";
Nature 557:564-569(2018).
[8]
VARIANTS NDNC4 ARG-65; PHE-95; ARG-107 AND TYR-118.
PubMed=17041604; DOI=10.1038/ng1883;
Blaydon D.C., Ishii Y., O'Toole E.A., Unsworth H.C., Teh M.-T.,
Rueschendorf F., Sinclair C., Hopsu-Havu V.K., Tidman N., Moss C.,
Watson R., de Berker D., Wajid M., Christiano A.M., Kelsell D.P.;
"The gene encoding R-spondin 4 (RSPO4), a secreted protein implicated
in Wnt signaling, is mutated in inherited anonychia.";
Nat. Genet. 38:1245-1247(2006).
-!- FUNCTION: Activator of the canonical Wnt signaling pathway by
acting as a ligand for LGR4-6 receptors (PubMed:29769720). Upon
binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with
phosphorylated LRP6 and frizzled receptors that are activated by
extracellular Wnt receptors, triggering the canonical Wnt
signaling pathway to increase expression of target genes. Also
regulates the canonical Wnt/beta-catenin-dependent pathway and
non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an
important regulator of the Wnt signaling pathway (PubMed:21727895,
PubMed:21909076). {ECO:0000269|PubMed:21727895,
ECO:0000269|PubMed:21909076, ECO:0000269|PubMed:29769720}.
-!- SUBUNIT: Binds heparin (By similarity). Interacts with LGR4, LGR5
and LGR6. {ECO:0000250, ECO:0000269|PubMed:21727895,
ECO:0000269|PubMed:21909076}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q2I0M5-1; Sequence=Displayed;
Name=2;
IsoId=Q2I0M5-2; Sequence=VSP_018325;
-!- DOMAIN: The FU repeat is required for activation and stabilization
of beta-catenin. {ECO:0000250}.
-!- PTM: Tyr-112 may be phosphorylated; however as this position is
probably extracellular, the vivo relevance is not proven.
-!- DISEASE: Nail disorder, non-syndromic congenital, 4 (NDNC4)
[MIM:206800]: A nail disorder characterized by congenital
anonychia or its milder phenotypic variant hyponychia.
Anonychia/hyponychia is the absence or severe hypoplasia of all
fingernails and toenails without significant bone anomalies.
{ECO:0000269|PubMed:17041604}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the R-spondin family. {ECO:0000305}.
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EMBL; DQ355152; ABC75877.1; -; mRNA.
EMBL; AK122609; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AL050325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS42845.1; -. [Q2I0M5-2]
CCDS; CCDS42846.1; -. [Q2I0M5-1]
RefSeq; NP_001025042.2; NM_001029871.3. [Q2I0M5-1]
RefSeq; NP_001035096.1; NM_001040007.2. [Q2I0M5-2]
UniGene; Hs.444980; -.
ProteinModelPortal; Q2I0M5; -.
SMR; Q2I0M5; -.
BioGrid; 131268; 1.
IntAct; Q2I0M5; 15.
STRING; 9606.ENSP00000217260; -.
iPTMnet; Q2I0M5; -.
PhosphoSitePlus; Q2I0M5; -.
BioMuta; RSPO4; -.
DMDM; 97189858; -.
PaxDb; Q2I0M5; -.
PeptideAtlas; Q2I0M5; -.
PRIDE; Q2I0M5; -.
ProteomicsDB; 61298; -.
ProteomicsDB; 61299; -. [Q2I0M5-2]
DNASU; 343637; -.
Ensembl; ENST00000217260; ENSP00000217260; ENSG00000101282. [Q2I0M5-1]
Ensembl; ENST00000400634; ENSP00000383475; ENSG00000101282. [Q2I0M5-2]
GeneID; 343637; -.
KEGG; hsa:343637; -.
UCSC; uc002wej.4; human. [Q2I0M5-1]
CTD; 343637; -.
DisGeNET; 343637; -.
EuPathDB; HostDB:ENSG00000101282.8; -.
GeneCards; RSPO4; -.
HGNC; HGNC:16175; RSPO4.
HPA; HPA048887; -.
MalaCards; RSPO4; -.
MIM; 206800; phenotype.
MIM; 610573; gene.
neXtProt; NX_Q2I0M5; -.
OpenTargets; ENSG00000101282; -.
Orphanet; 94150; Anonychia congenita totalis.
PharmGKB; PA25726; -.
eggNOG; KOG3525; Eukaryota.
eggNOG; COG1404; LUCA.
GeneTree; ENSGT00940000160937; -.
HOGENOM; HOG000290668; -.
HOVERGEN; HBG082751; -.
InParanoid; Q2I0M5; -.
OMA; FFGIRGQ; -.
OrthoDB; 881262at2759; -.
PhylomeDB; Q2I0M5; -.
TreeFam; TF331799; -.
Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination.
GenomeRNAi; 343637; -.
PRO; PR:Q2I0M5; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101282; Expressed in 77 organ(s), highest expression level in hypothalamus.
Genevisible; Q2I0M5; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0005109; F:frizzled binding; IBA:GO_Central.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0035878; P:nail development; IMP:MGI.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IBA:GO_Central.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
CDD; cd00064; FU; 1.
InterPro; IPR006212; Furin_repeat.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR000884; TSP1_rpt.
Pfam; PF15913; Furin-like_2; 1.
SMART; SM00261; FU; 2.
SMART; SM00209; TSP1; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS50092; TSP1; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disease mutation;
Disulfide bond; Glycoprotein; Heparin-binding; Phosphoprotein;
Polymorphism; Reference proteome; Secreted; Sensory transduction;
Signal; Wnt signaling pathway.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 234 R-spondin-4.
/FTId=PRO_0000234446.
REPEAT 85 128 FU.
DOMAIN 138 197 TSP type-1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
CARBOHYD 34 34 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 35 41 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 38 47 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 50 69 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 73 88 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 91 98 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 95 104 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 107 118 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 122 135 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 139 181 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 150 157 {ECO:0000255|PROSITE-ProRule:PRU00210}.
DISULFID 190 196 {ECO:0000255|PROSITE-ProRule:PRU00210}.
VAR_SEQ 137 198 Missing (in isoform 2).
{ECO:0000303|PubMed:16357527}.
/FTId=VSP_018325.
VARIANT 65 65 Q -> R (in NDNC4; dbSNP:rs74315420).
{ECO:0000269|PubMed:17041604}.
/FTId=VAR_030399.
VARIANT 95 95 C -> F (in NDNC4; dbSNP:rs780506366).
{ECO:0000269|PubMed:17041604}.
/FTId=VAR_030400.
VARIANT 106 106 R -> Q (in dbSNP:rs6140807).
/FTId=VAR_052665.
VARIANT 107 107 C -> R (in NDNC4; dbSNP:rs74315421).
{ECO:0000269|PubMed:17041604}.
/FTId=VAR_030401.
VARIANT 118 118 C -> Y (in NDNC4; dbSNP:rs74315422).
{ECO:0000269|PubMed:17041604}.
/FTId=VAR_030402.
SEQUENCE 234 AA; 26171 MW; 853E4494533B73F7 CRC64;
MRAPLCLLLL VAHAVDMLAL NRRKKQVGTG LGGNCTGCII CSEENGCSTC QQRLFLFIRR
EGIRQYGKCL HDCPPGYFGI RGQEVNRCKK CGATCESCFS QDFCIRCKRQ FYLYKGKCLP
TCPPGTLAHQ NTRECQGECE LGPWGGWSPC THNGKTCGSA WGLESRVREA GRAGHEEAAT
CQVLSESRKC PIQRPCPGER SPGQKKGRKD RRPRKDRKLD RRLDVRPRQP GLQP


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Related Genes :
[RSPO4 C20orf182] R-spondin-4 (Roof plate-specific spondin-4) (hRspo4)
[Rspo1] R-spondin-1 (Cysteine-rich and single thrombospondin domain-containing protein 3) (Cristin-3) (mCristin-3) (Roof plate-specific spondin-1)
[RSPO1] R-spondin-1 (Roof plate-specific spondin-1) (hRspo1)
[RSPO2 UNQ9384/PRO34209] R-spondin-2 (Roof plate-specific spondin-2) (hRspo2)
[Rspo2] R-spondin-2 (Cysteine-rich and single thrombospondin domain-containing protein 2) (Cristin-2) (mCristin-2) (Roof plate-specific spondin-2)
[RSPO3 PWTSR THSD2] R-spondin-3 (Protein with TSP type-1 repeat) (hPWTSR) (Roof plate-specific spondin-3) (hRspo3) (Thrombospondin type-1 domain-containing protein 2)
[Rspo3] R-spondin-3 (Cabriolet) (Cysteine-rich and single thrombospondin domain-containing protein 1) (Cristin-1) (Nucleopondin) (Roof plate-specific spondin-3)
[Rspo4] R-spondin-4 (Cysteine-rich and single thrombospondin domain-containing protein 4) (Cristin-4) (mCristin-4) (Roof plate-specific spondin-4)
[rspo2] R-spondin-2 (Roof plate-specific spondin-2)
[rspo3 sb:cb387 zgc:162040] R-spondin-3 (Cabriolet) (Roof plate-specific spondin-3)
[rspo1 zgc:92153] R-spondin-1 (Roof plate-specific spondin-1)
[rspo2] R-spondin-2 (Roof plate-specific spondin-2) (XRspo2)
[RSPO3] R-spondin-3 (Roof plate-specific spondin-3)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[] Endonuclease V (EC 3.2.2.17) (DNA-(apurinic or apyrimidinic site) lyase) (AP lyase) (EC 4.2.99.18) (T4 pyrimidine dimer glycosylase) (T4-Pdg)
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[Cyb5r4 Ncb5or] Cytochrome b5 reductase 4 (EC 1.6.2.2) (Flavohemoprotein b5/b5R) (b5+b5R) (N-terminal cytochrome b5 and cytochrome b5 oxidoreductase domain-containing protein) (cb5/cb5R)
[ppoA AN1967] Psi-producing oxygenase A (Fatty acid oxygenase ppoA) [Includes: Linoleate 8R-lipoxygenase (EC 1.13.11.60); 9,12-octadecadienoate 8-hydroperoxide 8R-isomerase (EC 5.4.4.5)]
[] Genome polyprotein [Cleaved into: Core protein p21 (Capsid protein C) (p21); Core protein p19; Envelope glycoprotein E1 (gp32) (gp35); Envelope glycoprotein E2 (NS1) (gp68) (gp70); p7; Protease NS2-3 (p23) (EC 3.4.22.-); Serine protease NS3 (EC 3.4.21.98) (EC 3.6.1.15) (EC 3.6.4.13) (Hepacivirin) (NS3P) (p70); Non-structural protein 4A (NS4A) (p8); Non-structural protein 4B (NS4B) (p27); Non-structural protein 5A (NS5A) (p56); RNA-directed RNA polymerase (EC 2.7.7.48) (NS5B) (p68)]
[LGR4 GPR48] Leucine-rich repeat-containing G-protein coupled receptor 4 (G-protein coupled receptor 48)
[ddh serA5 HFX_2024] D-2-hydroxyacid dehydrogenase (D2-HDH) (EC 1.1.1.-) (D-specific 2-hydroxyacid dehydrogenase)
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[CYB5R4 NCB5OR] Cytochrome b5 reductase 4 (EC 1.6.2.2) (Flavohemoprotein b5/b5R) (b5+b5R) (N-terminal cytochrome b5 and cytochrome b5 oxidoreductase domain-containing protein) (cb5/cb5R)

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