ID   RNF24_HUMAN             Reviewed;         148 AA.
AC   Q9Y225; D3DVZ2; D3DVZ3; Q9UMH1;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=RING finger protein 24;
GN   Name=RNF24;
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).
RA   Stavrides G.S., Huckle E.J., Deloukas P.;
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Blood, and Kidney;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-148.
RG   The European IMAGE consortium;
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   FUNCTION, INTERACTION WITH TRPC1; TRPC3; TRPC4; TRPC5; TRPC6 AND TRPC7, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=17850865; DOI=10.1016/j.ceca.2007.07.009;
RA   Lussier M.P., Lepage P.K., Bousquet S.M., Boulay G.;
RT   "RNF24, a new TRPC interacting protein, causes the intracellular retention
RT   of TRPC.";
RL   Cell Calcium 43:432-443(2008).
RN   [8]
RP   STRUCTURE BY NMR OF 68-128 IN COMPLEX WITH ZINC.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RING finger from human RING finger protein 24.";
RL   Submitted (FEB-2009) to the PDB data bank.
CC   -!- FUNCTION: May play a role in TRPCs intracellular trafficking.
CC       {ECO:0000269|PubMed:17850865}.
CC   -!- SUBUNIT: Interacts with TRPC1, TRPC3, TRPC4, TRPC5, TRPC6 and TRPC7.
CC       {ECO:0000269|PubMed:17850865, ECO:0000269|Ref.8}.
CC   -!- INTERACTION:
CC       Q9Y225; P07919: UQCRH; NbExp=3; IntAct=EBI-10195462, EBI-1224427;
CC       Q9Y225-2; Q8WTS1: ABHD5; NbExp=3; IntAct=EBI-13044680, EBI-2813554;
CC       Q9Y225-2; Q9NVT9: ARMC1; NbExp=3; IntAct=EBI-13044680, EBI-3506974;
CC       Q9Y225-2; Q12983: BNIP3; NbExp=3; IntAct=EBI-13044680, EBI-749464;
CC       Q9Y225-2; O95406: CNIH1; NbExp=3; IntAct=EBI-13044680, EBI-12172273;
CC       Q9Y225-2; Q6ZVE7: GOLT1A; NbExp=3; IntAct=EBI-13044680, EBI-17231387;
CC       Q9Y225-2; Q86UP9: LHFPL3; NbExp=3; IntAct=EBI-13044680, EBI-12925734;
CC       Q9Y225-2; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-13044680, EBI-373355;
CC       Q9Y225-2; Q16617: NKG7; NbExp=3; IntAct=EBI-13044680, EBI-3919611;
CC       Q9Y225-2; Q8IZ57: NRSN1; NbExp=3; IntAct=EBI-13044680, EBI-10264528;
CC       Q9Y225-2; P21589: NT5E; NbExp=3; IntAct=EBI-13044680, EBI-6393623;
CC       Q9Y225-2; P60201-2: PLP1; NbExp=3; IntAct=EBI-13044680, EBI-12188331;
CC       Q9Y225-2; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-13044680, EBI-18159983;
CC       Q9Y225-2; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-13044680, EBI-6268651;
CC       Q9Y225-2; Q9Y320: TMX2; NbExp=3; IntAct=EBI-13044680, EBI-6447886;
CC       Q9Y225-2; P23763-3: VAMP1; NbExp=3; IntAct=EBI-13044680, EBI-12097582;
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000269|PubMed:17850865}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:17850865}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y225-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y225-2; Sequence=VSP_041026;
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; AL096778; CAB46627.1; -; mRNA.
DR   EMBL; BT007406; AAP36074.1; -; mRNA.
DR   EMBL; AL031670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471133; EAX10467.1; -; Genomic_DNA.
DR   EMBL; CH471133; EAX10468.1; -; Genomic_DNA.
DR   EMBL; CH471133; EAX10469.1; -; Genomic_DNA.
DR   EMBL; CH471133; EAX10471.1; -; Genomic_DNA.
DR   EMBL; BC000213; AAH00213.1; -; mRNA.
DR   EMBL; BC039584; AAH39584.1; -; mRNA.
DR   EMBL; AL079313; CAB45279.1; -; mRNA.
DR   CCDS; CCDS13074.1; -. [Q9Y225-1]
DR   CCDS; CCDS46577.1; -. [Q9Y225-2]
DR   RefSeq; NP_001127809.1; NM_001134337.2. [Q9Y225-1]
DR   RefSeq; NP_001127810.1; NM_001134338.2. [Q9Y225-2]
DR   RefSeq; NP_001308678.1; NM_001321749.1. [Q9Y225-1]
DR   RefSeq; NP_009150.1; NM_007219.4. [Q9Y225-1]
DR   RefSeq; XP_011527447.1; XM_011529145.2.
DR   RefSeq; XP_016883109.1; XM_017027620.1. [Q9Y225-2]
DR   RefSeq; XP_016883110.1; XM_017027621.1. [Q9Y225-2]
DR   PDB; 2EP4; NMR; -; A=68-128.
DR   PDBsum; 2EP4; -.
DR   AlphaFoldDB; Q9Y225; -.
DR   SMR; Q9Y225; -.
DR   BioGRID; 116402; 18.
DR   IntAct; Q9Y225; 16.
DR   STRING; 9606.ENSP00000388550; -.
DR   iPTMnet; Q9Y225; -.
DR   PhosphoSitePlus; Q9Y225; -.
DR   BioMuta; RNF24; -.
DR   DMDM; 20139860; -.
DR   jPOST; Q9Y225; -.
DR   MassIVE; Q9Y225; -.
DR   MaxQB; Q9Y225; -.
DR   PaxDb; 9606-ENSP00000388550; -.
DR   PeptideAtlas; Q9Y225; -.
DR   ProteomicsDB; 85610; -. [Q9Y225-1]
DR   ProteomicsDB; 85611; -. [Q9Y225-2]
DR   Pumba; Q9Y225; -.
DR   Antibodypedia; 23773; 134 antibodies from 19 providers.
DR   DNASU; 11237; -.
DR   Ensembl; ENST00000336095.10; ENSP00000336753.5; ENSG00000101236.17. [Q9Y225-1]
DR   Ensembl; ENST00000358395.11; ENSP00000351166.6; ENSG00000101236.17. [Q9Y225-1]
DR   Ensembl; ENST00000432261.6; ENSP00000388550.2; ENSG00000101236.17. [Q9Y225-2]
DR   Ensembl; ENST00000545616.2; ENSP00000444711.1; ENSG00000101236.17. [Q9Y225-2]
DR   GeneID; 11237; -.
DR   KEGG; hsa:11237; -.
DR   MANE-Select; ENST00000358395.11; ENSP00000351166.6; NM_001134337.3; NP_001127809.1.
DR   UCSC; uc002wkh.4; human. [Q9Y225-1]
DR   AGR; HGNC:13779; -.
DR   CTD; 11237; -.
DR   DisGeNET; 11237; -.
DR   GeneCards; RNF24; -.
DR   HGNC; HGNC:13779; RNF24.
DR   HPA; ENSG00000101236; Tissue enhanced (bone).
DR   MIM; 612489; gene.
DR   neXtProt; NX_Q9Y225; -.
DR   OpenTargets; ENSG00000101236; -.
DR   PharmGKB; PA34428; -.
DR   VEuPathDB; HostDB:ENSG00000101236; -.
DR   eggNOG; KOG0800; Eukaryota.
DR   GeneTree; ENSGT00940000159443; -.
DR   HOGENOM; CLU_142341_0_0_1; -.
DR   InParanoid; Q9Y225; -.
DR   OMA; HNKQDHG; -.
DR   OrthoDB; 5474929at2759; -.
DR   PhylomeDB; Q9Y225; -.
DR   PathwayCommons; Q9Y225; -.
DR   SignaLink; Q9Y225; -.
DR   SIGNOR; Q9Y225; -.
DR   BioGRID-ORCS; 11237; 31 hits in 1195 CRISPR screens.
DR   ChiTaRS; RNF24; human.
DR   EvolutionaryTrace; Q9Y225; -.
DR   GeneWiki; RNF24; -.
DR   GenomeRNAi; 11237; -.
DR   Pharos; Q9Y225; Tbio.
DR   PRO; PR:Q9Y225; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q9Y225; Protein.
DR   Bgee; ENSG00000101236; Expressed in secondary oocyte and 182 other cell types or tissues.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd16675; RING-H2_RNF24; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR048025; RNF24_RING-H2.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR22763:SF196; RING FINGER PROTEIN 24 ISOFORM X1; 1.
DR   PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00744; RINGv; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   Genevisible; Q9Y225; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Golgi apparatus; Membrane;
KW   Metal-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..148
FT                   /note="RING finger protein 24"
FT                   /id="PRO_0000056063"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         78..119
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   VAR_SEQ         1
FT                   /note="M -> MLNKSGESRYPALFPVLGGSSM (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_041026"
FT   CONFLICT        45
FT                   /note="Y -> S (in Ref. 6; CAB45279)"
FT                   /evidence="ECO:0000305"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:2EP4"
FT   STRAND          87..89
FT                   /evidence="ECO:0007829|PDB:2EP4"
FT   STRAND          91..94
FT                   /evidence="ECO:0007829|PDB:2EP4"
FT   TURN            95..97
FT                   /evidence="ECO:0007829|PDB:2EP4"
FT   STRAND          98..101
FT                   /evidence="ECO:0007829|PDB:2EP4"
FT   HELIX           102..111
FT                   /evidence="ECO:0007829|PDB:2EP4"
FT   TURN            116..118
FT                   /evidence="ECO:0007829|PDB:2EP4"
SQ   SEQUENCE   148 AA;  17210 MW;  66C240C3A5991EA5 CRC64;
     MSSDFPHYNF RMPNIGFQNL PLNIYIVVFG TAIFVFILSL LFCCYLIRLR HQAHKEFYAY
     KQVILKEKVK ELNLHELCAV CLEDFKPRDE LGICPCKHAF HRKCLIKWLE VRKVCPLCNM
     PVLQLAQLHS KQDRGPPQGP LPGAENIV
//