SFRP5_HUMAN
ID SFRP5_HUMAN Reviewed; 317 AA.
AC Q5T4F7; O14780; Q86TH7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Secreted frizzled-related protein 5;
DE Short=sFRP-5;
DE AltName: Full=Frizzled-related protein 1b;
DE Short=FRP-1b;
DE AltName: Full=Secreted apoptosis-related protein 3;
DE Short=SARP-3;
DE Flags: Precursor;
GN Name=SFRP5; Synonyms=FRP1B, SARP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-7, AND TISSUE SPECIFICITY.
RC TISSUE=Pancreas;
RX PubMed=9391078; DOI=10.1073/pnas.94.25.13636;
RA Melkonyan H.S., Chang W.C., Shapiro J.P., Mahadevappa M., Fitzpatrick P.A.,
RA Kiefer M.C., Tomei L.D., Umansky S.R.;
RT "SARPs: a family of secreted apoptosis-related proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13636-13641(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-7, AND TISSUE SPECIFICITY.
RX PubMed=9642118; DOI=10.1006/bbrc.1998.8784;
RA Hu E., Zhu Y., Fredrickson T., Barnes M., Kelsell D., Beeley L., Brooks D.;
RT "Tissue restricted expression of two human Frzbs in preadipocytes and
RT pancreas.";
RL Biochem. Biophys. Res. Commun. 247:287-293(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT ALA-7, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=10072424; DOI=10.1093/hmg/8.4.575;
RA Chang J.T., Esumi N., Moore K., Li Y., Zhang S., Chew C., Goodman B.,
RA Rattner A., Moody S., Stetten G., Campochiaro P.A., Zack D.J.;
RT "Cloning and characterization of a secreted frizzled-related protein that
RT is expressed by the retinal pigment epithelium.";
RL Hum. Mol. Genet. 8:575-583(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-7.
RC TISSUE=PNS;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Soluble frizzled-related proteins (sFRPS) function as
CC modulators of Wnt signaling through direct interaction with Wnts. They
CC have a role in regulating cell growth and differentiation in specific
CC cell types. SFRP5 may be involved in determining the polarity of
CC photoreceptor, and perhaps, other cells in the retina.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the retinal pigment epithelium
CC (RPE) and pancreas. Weak expression in heart, liver and muscle.
CC {ECO:0000269|PubMed:10072424, ECO:0000269|PubMed:9391078,
CC ECO:0000269|PubMed:9642118}.
CC -!- DOMAIN: The FZ domain is involved in binding with Wnt ligands.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the secreted frizzled-related protein (sFRP)
CC family. {ECO:0000305}.
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DR EMBL; AF017988; AAB70794.1; -; mRNA.
DR EMBL; AF117758; AAD25052.1; -; mRNA.
DR EMBL; CR596705; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL358938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050435; AAH50435.2; -; mRNA.
DR CCDS; CCDS7472.1; -.
DR PIR; JE0175; JE0175.
DR RefSeq; NP_003006.2; NM_003015.3.
DR AlphaFoldDB; Q5T4F7; -.
DR SMR; Q5T4F7; -.
DR BioGRID; 112323; 4.
DR STRING; 9606.ENSP00000266066; -.
DR MEROPS; I93.002; -.
DR iPTMnet; Q5T4F7; -.
DR PhosphoSitePlus; Q5T4F7; -.
DR BioMuta; SFRP5; -.
DR DMDM; 150421670; -.
DR MassIVE; Q5T4F7; -.
DR PaxDb; Q5T4F7; -.
DR PeptideAtlas; Q5T4F7; -.
DR PRIDE; Q5T4F7; -.
DR ProteomicsDB; 64458; -.
DR Antibodypedia; 17373; 239 antibodies from 26 providers.
DR DNASU; 6425; -.
DR Ensembl; ENST00000266066.4; ENSP00000266066.3; ENSG00000120057.5.
DR GeneID; 6425; -.
DR KEGG; hsa:6425; -.
DR MANE-Select; ENST00000266066.4; ENSP00000266066.3; NM_003015.3; NP_003006.2.
DR UCSC; uc001kor.5; human.
DR CTD; 6425; -.
DR DisGeNET; 6425; -.
DR GeneCards; SFRP5; -.
DR HGNC; HGNC:10779; SFRP5.
DR HPA; ENSG00000120057; Tissue enhanced (choroid plexus, pancreas).
DR MIM; 604158; gene.
DR neXtProt; NX_Q5T4F7; -.
DR OpenTargets; ENSG00000120057; -.
DR PharmGKB; PA35695; -.
DR VEuPathDB; HostDB:ENSG00000120057; -.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000160608; -.
DR HOGENOM; CLU_054647_1_0_1; -.
DR InParanoid; Q5T4F7; -.
DR OMA; PEMLHCG; -.
DR OrthoDB; 1306779at2759; -.
DR PhylomeDB; Q5T4F7; -.
DR TreeFam; TF350133; -.
DR PathwayCommons; Q5T4F7; -.
DR BioGRID-ORCS; 6425; 12 hits in 1066 CRISPR screens.
DR GeneWiki; SFRP5; -.
DR GenomeRNAi; 6425; -.
DR Pharos; Q5T4F7; Tbio.
DR PRO; PR:Q5T4F7; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q5T4F7; protein.
DR Bgee; ENSG00000120057; Expressed in pigmented layer of retina and 152 other tissues.
DR Genevisible; Q5T4F7; HS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:ProtInc.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:BHF-UCL.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:BHF-UCL.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:BHF-UCL.
DR GO; GO:0030178; P:negative regulation of Wnt signaling pathway; NAS:ParkinsonsUK-UCL.
DR GO; GO:2000057; P:negative regulation of Wnt signaling pathway involved in digestive tract morphogenesis; IMP:BHF-UCL.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0007601; P:visual perception; TAS:ProtInc.
DR CDD; cd07444; CRD_SFRP5; 1.
DR Gene3D; 1.10.2000.10; -; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR InterPro; IPR015526; Frizzled/SFRP.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR034860; SFRP-5.
DR InterPro; IPR041761; SFRP5_CRD.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11309; PTHR11309; 1.
DR PANTHER; PTHR11309:SF46; PTHR11309:SF46; 1.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF01759; NTR; 1.
DR SMART; SM00643; C345C; 1.
DR SMART; SM00063; FRI; 1.
DR SUPFAM; SSF50242; SSF50242; 1.
DR SUPFAM; SSF63501; SSF63501; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50189; NTR; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Differentiation; Disulfide bond; Reference proteome;
KW Secreted; Signal; Wnt signaling pathway.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..317
FT /note="Secreted frizzled-related protein 5"
FT /id="PRO_0000032555"
FT DOMAIN 48..165
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DOMAIN 181..303
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 53..116
FT /evidence="ECO:0000250"
FT DISULFID 63..109
FT /evidence="ECO:0000250"
FT DISULFID 100..135
FT /evidence="ECO:0000250"
FT DISULFID 124..162
FT /evidence="ECO:0000250"
FT DISULFID 128..152
FT /evidence="ECO:0000250"
FT DISULFID 181..253
FT /evidence="ECO:0000250"
FT DISULFID 184..255
FT /evidence="ECO:0000250"
FT DISULFID 198..303
FT /evidence="ECO:0000250"
FT VARIANT 7
FT /note="G -> A (in dbSNP:rs11815012)"
FT /evidence="ECO:0000269|PubMed:10072424,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9391078,
FT ECO:0000269|PubMed:9642118"
FT /id="VAR_021412"
FT CONFLICT 33
FT /note="D -> H (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 35563 MW; 4BF060F1161751F9 CRC64;
MRAAAAGGGV RTAALALLLG ALHWAPARCE EYDYYGWQAE PLHGRSYSKP PQCLDIPADL
PLCHTVGYKR MRLPNLLEHE SLAEVKQQAS SWLPLLAKRC HSDTQVFLCS LFAPVCLDRP
IYPCRSLCEA VRAGCAPLME AYGFPWPEML HCHKFPLDND LCIAVQFGHL PATAPPVTKI
CAQCEMEHSA DGLMEQMCSS DFVVKMRIKE IKIENGDRKL IGAQKKKKLL KPGPLKRKDT
KRLVLHMKNG AGCPCPQLDS LAGSFLVMGR KVDGQLLLMA VYRWDKKNKE MKFAVKFMFS
YPCSLYYPFF YGAAEPH
