RSPRY_MACFA
ID RSPRY_MACFA Reviewed; 576 AA.
AC Q95LP3;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=RING finger and SPRY domain-containing protein 1;
DE Flags: Precursor;
GN Name=RSPRY1; ORFNames=QtsA-15931;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; AB072745; BAB69714.1; -; mRNA.
DR RefSeq; NP_001306505.1; NM_001319576.1.
DR AlphaFoldDB; Q95LP3; -.
DR SMR; Q95LP3; -.
DR STRING; 9541.XP_005592078.1; -.
DR GeneID; 102121113; -.
DR CTD; 89970; -.
DR eggNOG; KOG2242; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
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; IEA:InterPro.
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 2: Evidence at transcript level;
KW Glycoprotein; Metal-binding; Phosphoprotein; Reference proteome; Secreted;
KW 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_0000278787"
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"
SQ SEQUENCE 576 AA; 64259 MW; 68D230AD1C4F5F8D CRC64;
MIVLGWAVFL ASRSLGQGLL LTLEEHIAHF LGTRGATTTM GNSCICRDDS GTDDSVDTQQ
QQAENSAVPT ADTRSQPRDP VRPPRRGRGP HEPRRKKQNV DGLVLDTLAV IRTLVDNDQE
PPYSMITLHE MAETDEGWLD VVQSLIRVIP LEDPLGPAVI TLLLDECPLP TKDALQKLTE
ILNLNGEVAC QDSGHPAKHR 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 EKQVFSSTIS GFFAAASFMS YQQCEFNFGA
KPFKYPPSMK FSTFNDYAFL TAEEKIILPR HRRLALLKQV SIRENCCSLC CDEVADTQLK
PCGHSDLCMD CALQLETCPL CRKEIVSRIR QISHIS