RSPRY_MOUSE
ID RSPRY_MOUSE Reviewed; 576 AA.
AC Q8BVR6; Q3T9F1; Q3TM35; Q3U802; Q3UKF9; Q3UYN5; Q8BMH0; Q8C039; Q9CZ54;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=RING finger and SPRY domain-containing protein 1;
DE Flags: Precursor;
GN Name=Rspry1; Synonyms=Kiaa1972;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Amnion, Embryo, Mammary gland, Medulla oblongata, Olfactory bulb,
RC Spinal cord, Spleen, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Embryo, 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY.
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).
RN [6]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION DURING MUSCLE ATROPHY,
RP AND INDUCTION BY MYOD1.
RX PubMed=26497270; DOI=10.1016/j.gene.2015.10.046;
RA Waddell D.S., Duffin P.J., Haddock A.N., Triplett V.E., Saredy J.J.,
RA Kakareka K.M., Eldredge J.T.;
RT "Isolation, expression analysis and characterization of NEFA-interacting
RT nuclear protein 30 and RING finger and SPRY domain containing 1 in skeletal
RT muscle.";
RL Gene 576:319-332(2016).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BVR6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BVR6-2; Sequence=VSP_023385, VSP_023386;
CC Name=3;
CC IsoId=Q8BVR6-3; Sequence=VSP_023384;
CC -!- TISSUE SPECIFICITY: Expressed in embryonic bone during primary
CC endochondral ossification. Strong localization is observed in the
CC perichondrium and periostium (at protein level). Also expressed in
CC embryonic and postnatal brain and craniofacial tissues. Expressed in
CC skeletal muscles (PubMed:26497270). {ECO:0000269|PubMed:26365341,
CC ECO:0000269|PubMed:26497270}.
CC -!- DEVELOPMENTAL STAGE: Shows relatively low expression levels in
CC proliferating myoblasts. Expression peaks at around day 1 of
CC differentiation into myotubes and decreases again by day 10, when
CC assayed in C2C12 cell line (at protein level).
CC {ECO:0000269|PubMed:26497270}.
CC -!- INDUCTION: Up-regulated in response to denervation-induced skeletal
CC muscle atrophy. Induced by MYOD1. {ECO:0000269|PubMed:26497270}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE22177.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK173313; BAD32591.1; -; mRNA.
DR EMBL; AK013003; BAB28589.1; -; mRNA.
DR EMBL; AK031153; BAC27283.1; -; mRNA.
DR EMBL; AK032416; BAC27858.1; -; mRNA.
DR EMBL; AK076799; BAC36485.1; -; mRNA.
DR EMBL; AK134544; BAE22177.1; ALT_FRAME; mRNA.
DR EMBL; AK141443; BAE24686.1; -; mRNA.
DR EMBL; AK146028; BAE26842.1; -; mRNA.
DR EMBL; AK150941; BAE29976.1; -; mRNA.
DR EMBL; AK152435; BAE31217.1; -; mRNA.
DR EMBL; AK166167; BAE38607.1; -; mRNA.
DR EMBL; AK172567; BAE43070.1; -; mRNA.
DR EMBL; BC010833; AAH10833.2; -; mRNA.
DR EMBL; BC054121; AAH54121.1; -; mRNA.
DR CCDS; CCDS22544.1; -. [Q8BVR6-1]
DR RefSeq; NP_080550.3; NM_026274.4. [Q8BVR6-1]
DR RefSeq; XP_006531376.1; XM_006531313.3.
DR AlphaFoldDB; Q8BVR6; -.
DR IntAct; Q8BVR6; 1.
DR STRING; 10090.ENSMUSP00000057275; -.
DR GlyGen; Q8BVR6; 1 site.
DR iPTMnet; Q8BVR6; -.
DR PhosphoSitePlus; Q8BVR6; -.
DR SwissPalm; Q8BVR6; -.
DR EPD; Q8BVR6; -.
DR jPOST; Q8BVR6; -.
DR MaxQB; Q8BVR6; -.
DR PaxDb; Q8BVR6; -.
DR PeptideAtlas; Q8BVR6; -.
DR PRIDE; Q8BVR6; -.
DR ProteomicsDB; 256787; -. [Q8BVR6-1]
DR ProteomicsDB; 256788; -. [Q8BVR6-2]
DR ProteomicsDB; 256789; -. [Q8BVR6-3]
DR Antibodypedia; 28826; 88 antibodies from 16 providers.
DR DNASU; 67610; -.
DR Ensembl; ENSMUST00000060389; ENSMUSP00000057275; ENSMUSG00000050079. [Q8BVR6-1]
DR Ensembl; ENSMUST00000121101; ENSMUSP00000112482; ENSMUSG00000050079. [Q8BVR6-2]
DR Ensembl; ENSMUST00000211983; ENSMUSP00000148737; ENSMUSG00000050079. [Q8BVR6-1]
DR Ensembl; ENSMUST00000212729; ENSMUSP00000148724; ENSMUSG00000050079. [Q8BVR6-3]
DR GeneID; 67610; -.
DR KEGG; mmu:67610; -.
DR UCSC; uc009mwq.2; mouse. [Q8BVR6-1]
DR CTD; 89970; -.
DR MGI; MGI:1914860; Rspry1.
DR VEuPathDB; HostDB:ENSMUSG00000050079; -.
DR eggNOG; KOG2242; Eukaryota.
DR GeneTree; ENSGT00940000157894; -.
DR HOGENOM; CLU_026400_0_0_1; -.
DR InParanoid; Q8BVR6; -.
DR OMA; DSGIWYY; -.
DR OrthoDB; 1005747at2759; -.
DR PhylomeDB; Q8BVR6; -.
DR TreeFam; TF313546; -.
DR BioGRID-ORCS; 67610; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Rspry1; mouse.
DR PRO; PR:Q8BVR6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BVR6; protein.
DR Bgee; ENSMUSG00000050079; Expressed in lateral septal nucleus and 245 other tissues.
DR Genevisible; Q8BVR6; MM.
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; Glycoprotein; Metal-binding; Phosphoprotein;
KW Reference proteome; 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_0000278788"
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 53..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..124
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023384"
FT VAR_SEQ 117
FT /note="N -> K (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023385"
FT VAR_SEQ 118..576
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023386"
FT CONFLICT 54
FT /note="D -> N (in Ref. 2; BAE43070)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="T -> A (in Ref. 2; BAE38607)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="L -> M (in Ref. 2; BAC27858)"
FT /evidence="ECO:0000305"
FT CONFLICT 527
FT /note="C -> Y (in Ref. 2; BAE22177)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 576 AA; 64322 MW; 823C3532FCE18387 CRC64;
MIVFGWAVFL ASRSLGQGLL LTLEEHIAHL LGTTGATATM GNSCICRDDS GAEDNVDTHQ
QQAENSTVPT ADSRSQPRDP VRPPRRGRGP HEPRRKKQNV DGLVLDTLAV IRTLVDNDQE
PPYSMITLHE MAETDEGWLD VVQSLIRVIP LEDPLGPAVI TLLLDECPLP TKDALQKLTE
ILNLNGEVAC QDSGHPAKHR NTSAVLGCLA EKLAGPASIG LLSPGILEYL LQCLKLQSHP
TVMLFALIAL EKFAQTSENK LTISESSISD RLVTLELWAD DPDYLKRQVG FCAQWSLDNL
FLKEGRQLTY EKVDLNNIRA MLNSNDVSEY LKISPHGLEA RCDASSFESV RCTFCVDTGV
WYYEVTVVTS GVMQIGWATR DSKFLNHEGY GIGDDEYSCA YDGCRQLIWY NARSKPHVHP
CWKEGDTVGF LLDLNEKQMI FFLNGNQLPP EKQVFSSTVS GFFAAASFMS YQQCEFNFGA
RPFKYPPSMK FSTFNDYAFL TAEEKIILPR HRRLALLKQV SIRENCCSLC CDEVADTQLK
PCGHSDLCMD CALQLETCPL CRKEIVSRIR QISHIS
