位置:首页 > 蛋白库 > FOLR3_HUMAN
FOLR3_HUMAN
ID   FOLR3_HUMAN             Reviewed;         245 AA.
AC   P41439; A0A087WXH3; J3KQ90; Q05C14;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   10-APR-2019, sequence version 2.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=Folate receptor gamma;
DE            Short=FR-gamma;
DE   AltName: Full=Folate receptor 3;
DE   Flags: Precursor;
GN   Name=FOLR3;
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] (ISOFORM 1), AND VARIANT 107-TYR--SER-245 DEL.
RC   TISSUE=Hematopoietic;
RX   PubMed=8110752; DOI=10.1021/bi00171a021;
RA   Shen F., Ross J.F., Wang X., Ratnam M.;
RT   "Identification of a novel folate receptor, a truncated receptor, and
RT   receptor type beta in hematopoietic cells: cDNA cloning, expression,
RT   immunoreactivity, and tissue specificity.";
RL   Biochemistry 33:1209-1215(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Pancreas;
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).
RN   [4]
RP   CHARACTERIZATION.
RX   PubMed=7727426; DOI=10.1021/bi00016a042;
RA   Shen F., Wu M., Ross J.F., Miller D., Ratnam M.;
RT   "Folate receptor type gamma is primarily a secretory protein due to lack of
RT   an efficient signal for glycosylphosphatidylinositol modification: protein
RT   characterization and cell type specificity.";
RL   Biochemistry 34:5660-5665(1995).
RN   [5]
RP   SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX   PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA   Hillman R.T., Green R.E., Brenner S.E.;
RT   "An unappreciated role for RNA surveillance.";
RL   Genome Biol. 5:R8.1-R8.16(2004).
CC   -!- FUNCTION: Binds to folate and reduced folic acid derivatives and
CC       mediates delivery of 5-methyltetrahydrofolate to the interior of cells.
CC       Isoform Short does not bind folate.
CC   -!- INTERACTION:
CC       P41439; X5D778: ANKRD11; NbExp=3; IntAct=EBI-12893875, EBI-17183751;
CC       P41439; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-12893875, EBI-741480;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Long;
CC         IsoId=P41439-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P41439-4; Sequence=VSP_060090, VSP_060091;
CC   -!- TISSUE SPECIFICITY: Spleen, thymus, bone marrow, ovarian carcinoma, and
CC       uterine carcinoma.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. Variant in position:
CC       150:MSAHPTWGPGSGRSTRAGAKSAF->ECSPNLGPWIRQVNQSWRKERILNVPLCKEDCERW
CC       WEDCRTSYTCKSNWHKGWNWTSGINECPAGALCSTFESYFPTPAALCEGLWSHSFKVSNYSRG.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the folate receptor family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA18381.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAA18382.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA83553.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAA83566.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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   EMBL; Z32564; CAA83553.1; ALT_INIT; mRNA.
DR   EMBL; Z32633; CAA83566.1; ALT_INIT; mRNA.
DR   EMBL; U08471; AAA18382.1; ALT_INIT; mRNA.
DR   EMBL; U08470; AAA18381.1; ALT_INIT; mRNA.
DR   EMBL; AP000812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF459676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC030285; AAH30285.1; -; mRNA.
DR   CCDS; CCDS73344.1; -. [P41439-1]
DR   PIR; A53506; A53506.
DR   RefSeq; NP_000795.2; NM_000804.3. [P41439-1]
DR   RefSeq; NP_001304974.1; NM_001318045.1.
DR   AlphaFoldDB; P41439; -.
DR   SMR; P41439; -.
DR   BioGRID; 108635; 6.
DR   IntAct; P41439; 2.
DR   STRING; 9606.ENSP00000481114; -.
DR   DrugBank; DB00158; Folic acid.
DR   DrugBank; DB05168; Vintafolide.
DR   GlyGen; P41439; 3 sites.
DR   iPTMnet; P41439; -.
DR   PhosphoSitePlus; P41439; -.
DR   BioMuta; FOLR3; -.
DR   DMDM; 1169723; -.
DR   jPOST; P41439; -.
DR   MassIVE; P41439; -.
DR   MaxQB; P41439; -.
DR   PeptideAtlas; P41439; -.
DR   PRIDE; P41439; -.
DR   ProteomicsDB; 55460; -. [P41439-1]
DR   Antibodypedia; 30810; 131 antibodies from 22 providers.
DR   DNASU; 2352; -.
DR   Ensembl; ENST00000611028.3; ENSP00000481114.1; ENSG00000110203.10. [P41439-1]
DR   Ensembl; ENST00000612844.4; ENSP00000481027.1; ENSG00000110203.10. [P41439-4]
DR   GeneID; 2352; -.
DR   KEGG; hsa:2352; -.
DR   MANE-Select; ENST00000611028.3; ENSP00000481114.1; NM_000804.4; NP_000795.2.
DR   UCSC; uc058ezu.1; human. [P41439-1]
DR   CTD; 2352; -.
DR   DisGeNET; 2352; -.
DR   GeneCards; FOLR3; -.
DR   HGNC; HGNC:3795; FOLR3.
DR   HPA; ENSG00000110203; Group enriched (bone marrow, lymphoid tissue).
DR   MIM; 602469; gene.
DR   neXtProt; NX_P41439; -.
DR   OpenTargets; ENSG00000110203; -.
DR   PharmGKB; PA28211; -.
DR   VEuPathDB; HostDB:ENSG00000110203; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT00950000183144; -.
DR   HOGENOM; CLU_070826_3_0_1; -.
DR   InParanoid; P41439; -.
DR   OMA; HFIQDGC; -.
DR   OrthoDB; 1224404at2759; -.
DR   PhylomeDB; P41439; -.
DR   PathwayCommons; P41439; -.
DR   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   SignaLink; P41439; -.
DR   BioGRID-ORCS; 2352; 13 hits in 285 CRISPR screens.
DR   ChiTaRS; FOLR3; human.
DR   GenomeRNAi; 2352; -.
DR   Pharos; P41439; Tbio.
DR   PRO; PR:P41439; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; P41439; protein.
DR   Bgee; ENSG00000110203; Expressed in granulocyte and 128 other tissues.
DR   ExpressionAtlas; P41439; baseline and differential.
DR   Genevisible; P41439; HS.
DR   GO; GO:0031362; C:anchored component of external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0019898; C:extrinsic component of membrane; TAS:ProtInc.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR   GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR   GO; GO:0005542; F:folic acid binding; TAS:ProtInc.
DR   GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0015884; P:folic acid transport; TAS:ProtInc.
DR   GO; GO:0007342; P:fusion of sperm to egg plasma membrane involved in single fertilization; IBA:GO_Central.
DR   GO; GO:0035036; P:sperm-egg recognition; IBA:GO_Central.
DR   InterPro; IPR004269; Folate_rcpt.
DR   InterPro; IPR018143; Folate_rcpt-like.
DR   InterPro; IPR032934; FR-gamma.
DR   PANTHER; PTHR10517; PTHR10517; 1.
DR   PANTHER; PTHR10517:SF17; PTHR10517:SF17; 1.
DR   Pfam; PF03024; Folate_rec; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disulfide bond; Folate-binding; Glycoprotein;
KW   Receptor; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..245
FT                   /note="Folate receptor gamma"
FT                   /id="PRO_0000008810"
FT   BINDING         103
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000250|UniProtKB:P15328"
FT   BINDING         107
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000250|UniProtKB:P15328"
FT   BINDING         124..128
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000250|UniProtKB:P15328"
FT   BINDING         157..162
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000250|UniProtKB:P15328"
FT   BINDING         196
FT                   /ligand="folate"
FT                   /ligand_id="ChEBI:CHEBI:62501"
FT                   /evidence="ECO:0000250|UniProtKB:P15328"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        37..65
FT                   /evidence="ECO:0000250|UniProtKB:P15328"
FT   DISULFID        57..105
FT                   /evidence="ECO:0000250|UniProtKB:P15328"
FT   DISULFID        66..109
FT                   /evidence="ECO:0000250|UniProtKB:P15328"
FT   DISULFID        89..175
FT                   /evidence="ECO:0000250|UniProtKB:P15328"
FT   DISULFID        96..146
FT                   /evidence="ECO:0000250|UniProtKB:P15328"
FT   DISULFID        135..209
FT                   /evidence="ECO:0000250|UniProtKB:P15328"
FT   DISULFID        139..189
FT                   /evidence="ECO:0000250|UniProtKB:P15328"
FT   DISULFID        152..169
FT                   /evidence="ECO:0000250|UniProtKB:P15328"
FT   VAR_SEQ         57..172
FT                   /note="CSPWKKNACCTASTSQELHKDTSRLYNFNWDHCGKMEPTCKRHFIQDSCLYE
FT                   CSPNLGPWIRQVNQSWRKERILNVPLCKEDCERWWEDCRTSYTCKSNWHKGWNWTSGIN
FT                   ECPAG -> VGAPQGPSPGSVPLDDLPGAEEPEYGGDGCGGERLSPVSSPPSAVPGRRM
FT                   PAARPAPARSCTRTPPACTTLTGITVVRWNPPASATLSRTAVSMSAHPTWGPGSGRSTR
FT                   AGAKSAF (in isoform 2)"
FT                   /id="VSP_060090"
FT   VAR_SEQ         173..245
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_060091"
FT   VARIANT         107..245
FT                   /note="Missing"
FT                   /evidence="ECO:0000269|PubMed:8110752"
FT                   /id="VAR_081429"
FT   CONFLICT        45
FT                   /note="T -> I (in Ref. 3; AAH30285)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        P41439-4:78
FT                   /note="E -> V (in Ref. 3; AAH30285)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   245 AA;  27885 MW;  478636F757EC40DB CRC64;
     MDMAWQMMQL LLLALVTAAG SAQPRSARAR TDLLNVCMNA KHHKTQPSPE DELYGQCSPW
     KKNACCTAST SQELHKDTSR LYNFNWDHCG KMEPTCKRHF IQDSCLYECS PNLGPWIRQV
     NQSWRKERIL NVPLCKEDCE RWWEDCRTSY TCKSNWHKGW NWTSGINECP AGALCSTFES
     YFPTPAALCE GLWSHSFKVS NYSRGSGRCI QMWFDSAQGN PNEEVAKFYA AAMNAGAPSR
     GIIDS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024