RSPRY_HUMAN
ID RSPRY_HUMAN Reviewed; 576 AA.
AC Q96DX4; Q6UX21; Q8ND53;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=RING finger and SPRY domain-containing protein 1;
DE Flags: Precursor;
GN Name=RSPRY1; Synonyms=KIAA1972; ORFNames=UNQ328/PRO444;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 492-576 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [7]
RP INVOLVEMENT IN SEMDFA, AND VARIANT SEMDFA CYS-41.
RX PubMed=26365341; DOI=10.1016/j.ajhg.2015.08.007;
RG Care4Rare Canada Consortium;
RA Faden M., Al-Zahrani F., Mendoza-Londono R., Dupuis L., Hartley T.,
RA Kannu P., Raiman J.A., Howard A., Qin W., Tetreault M., Xi J.Q.,
RA Al-Thamer I., Maas R.L., Boycott K., Alkuraya F.S.;
RT "Identification of a recognizable progressive skeletal dysplasia caused by
RT RSPRY1 mutations.";
RL Am. J. Hum. Genet. 97:608-615(2015).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96DX4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96DX4-2; Sequence=VSP_023382, VSP_023383;
CC -!- DISEASE: Spondyloepimetaphyseal dysplasia, Faden-Alkuraya type (SEMDFA)
CC [MIM:616723]: An autosomal recessive skeletal disorder characterized by
CC spondyloepimetaphyseal dysplasia, short stature, facial dysmorphism,
CC short fourth metatarsals, and intellectual disability.
CC {ECO:0000269|PubMed:26365341}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AB075852; BAB85558.1; -; mRNA.
DR EMBL; AY358548; AAQ88912.1; -; mRNA.
DR EMBL; AK172845; BAD18809.1; -; mRNA.
DR EMBL; BC013173; AAH13173.1; -; mRNA.
DR EMBL; AL834402; CAD39064.1; -; mRNA.
DR CCDS; CCDS10775.1; -. [Q96DX4-1]
DR RefSeq; NP_001292092.1; NM_001305163.1. [Q96DX4-1]
DR RefSeq; NP_001292093.1; NM_001305164.1. [Q96DX4-1]
DR RefSeq; NP_001292111.1; NM_001305182.1. [Q96DX4-2]
DR RefSeq; NP_588609.1; NM_133368.2. [Q96DX4-1]
DR RefSeq; XP_005256277.1; XM_005256220.1. [Q96DX4-1]
DR AlphaFoldDB; Q96DX4; -.
DR SMR; Q96DX4; -.
DR BioGRID; 124650; 72.
DR IntAct; Q96DX4; 41.
DR STRING; 9606.ENSP00000443176; -.
DR GlyGen; Q96DX4; 2 sites, 2 O-linked glycans (1 site).
DR iPTMnet; Q96DX4; -.
DR PhosphoSitePlus; Q96DX4; -.
DR SwissPalm; Q96DX4; -.
DR BioMuta; RSPRY1; -.
DR DMDM; 74731506; -.
DR EPD; Q96DX4; -.
DR jPOST; Q96DX4; -.
DR MassIVE; Q96DX4; -.
DR MaxQB; Q96DX4; -.
DR PaxDb; Q96DX4; -.
DR PeptideAtlas; Q96DX4; -.
DR PRIDE; Q96DX4; -.
DR ProteomicsDB; 76332; -. [Q96DX4-1]
DR ProteomicsDB; 76333; -. [Q96DX4-2]
DR Antibodypedia; 28826; 88 antibodies from 16 providers.
DR DNASU; 89970; -.
DR Ensembl; ENST00000394420.9; ENSP00000377942.4; ENSG00000159579.14. [Q96DX4-1]
DR Ensembl; ENST00000537866.5; ENSP00000443176.1; ENSG00000159579.14. [Q96DX4-1]
DR GeneID; 89970; -.
DR KEGG; hsa:89970; -.
DR MANE-Select; ENST00000394420.9; ENSP00000377942.4; NM_133368.3; NP_588609.1.
DR UCSC; uc002elb.4; human. [Q96DX4-1]
DR CTD; 89970; -.
DR DisGeNET; 89970; -.
DR GeneCards; RSPRY1; -.
DR HGNC; HGNC:29420; RSPRY1.
DR HPA; ENSG00000159579; Low tissue specificity.
DR MalaCards; RSPRY1; -.
DR MIM; 616585; gene.
DR MIM; 616723; phenotype.
DR neXtProt; NX_Q96DX4; -.
DR OpenTargets; ENSG00000159579; -.
DR Orphanet; 457395; Progressive spondyloepimetaphyseal dysplasia-short stature-short fourth metatarsals-intellectual disability syndrome.
DR PharmGKB; PA143485602; -.
DR VEuPathDB; HostDB:ENSG00000159579; -.
DR eggNOG; KOG2242; Eukaryota.
DR GeneTree; ENSGT00940000157894; -.
DR HOGENOM; CLU_026400_0_0_1; -.
DR InParanoid; Q96DX4; -.
DR OMA; DSGIWYY; -.
DR OrthoDB; 1005747at2759; -.
DR PhylomeDB; Q96DX4; -.
DR TreeFam; TF313546; -.
DR PathwayCommons; Q96DX4; -.
DR SignaLink; Q96DX4; -.
DR BioGRID-ORCS; 89970; 16 hits in 1062 CRISPR screens.
DR ChiTaRS; RSPRY1; human.
DR GenomeRNAi; 89970; -.
DR Pharos; Q96DX4; Tdark.
DR PRO; PR:Q96DX4; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q96DX4; protein.
DR Bgee; ENSG00000159579; Expressed in kidney epithelium and 196 other tissues.
DR ExpressionAtlas; Q96DX4; baseline and differential.
DR Genevisible; Q96DX4; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR CDD; cd12883; SPRY_RING; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR045129; RNF123/RSPRY1-like.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035774; SPRY_RSPRY1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR13363; PTHR13363; 1.
DR Pfam; PF00622; SPRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Dwarfism; Glycoprotein;
KW Intellectual disability; Metal-binding; Phosphoprotein; Reference proteome;
KW Secreted; Signal; Zinc; Zinc-finger.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..576
FT /note="RING finger and SPRY domain-containing protein 1"
FT /id="PRO_0000278786"
FT DOMAIN 300..483
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 527..562
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 50..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BVR6"
FT CARBOHYD 314
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 117
FT /note="N -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_023382"
FT VAR_SEQ 118..576
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12975309"
FT /id="VSP_023383"
FT VARIANT 41
FT /note="G -> C (in SEMDFA; dbSNP:rs864309652)"
FT /evidence="ECO:0000269|PubMed:26365341"
FT /id="VAR_075873"
SQ SEQUENCE 576 AA; 64180 MW; 8598E43E96691F9B CRC64;
MIVFGWAVFL ASRSLGQGLL LTLEEHIAHF LGTGGAATTM GNSCICRDDS GTDDSVDTQQ
QQAENSAVPT ADTRSQPRDP VRPPRRGRGP HEPRRKKQNV DGLVLDTLAV IRTLVDNDQE
PPYSMITLHE MAETDEGWLD VVQSLIRVIP LEDPLGPAVI TLLLDECPLP TKDALQKLTE
ILNLNGEVAC QDSSHPAKHR NTSAVLGCLA EKLAGPASIG LLSPGILEYL LQCLKLQSHP
TVMLFALIAL EKFAQTSENK LTISESSISD RLVTLESWAN DPDYLKRQVG FCAQWSLDNL
FLKEGRQLTY EKVNLSSIRA MLNSNDVSEY LKISPHGLEA RCDASSFESV RCTFCVDAGV
WYYEVTVVTS GVMQIGWATR DSKFLNHEGY GIGDDEYSCA YDGCRQLIWY NARSKPHIHP
CWKEGDTVGF LLDLNEKQMI FFLNGNQLPP EKQVFSSTVS GFFAAASFMS YQQCEFNFGA
KPFKYPPSMK FSTFNDYAFL TAEEKIILPR HRRLALLKQV SIRENCCSLC CDEVADTQLK
PCGHSDLCMD CALQLETCPL CRKEIVSRIR QISHIS
