RSPRY_PONAB
ID RSPRY_PONAB Reviewed; 576 AA.
AC Q5R881;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=RING finger and SPRY domain-containing protein 1;
DE Flags: Precursor;
GN Name=RSPRY1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
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DR EMBL; CR859873; CAH92029.1; -; mRNA.
DR RefSeq; NP_001126179.1; NM_001132707.1.
DR RefSeq; XP_009249028.1; XM_009250753.1.
DR RefSeq; XP_009249029.1; XM_009250754.1.
DR AlphaFoldDB; Q5R881; -.
DR SMR; Q5R881; -.
DR STRING; 9601.ENSPPYP00000008340; -.
DR Ensembl; ENSPPYT00000008681; ENSPPYP00000008340; ENSPPYG00000007383.
DR GeneID; 100173142; -.
DR KEGG; pon:100173142; -.
DR CTD; 89970; -.
DR eggNOG; KOG2242; Eukaryota.
DR GeneTree; ENSGT00940000157894; -.
DR HOGENOM; CLU_026400_0_0_1; -.
DR InParanoid; Q5R881; -.
DR OMA; DSGIWYY; -.
DR OrthoDB; 1005747at2759; -.
DR TreeFam; TF313546; -.
DR Proteomes; UP000001595; Chromosome 16.
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_0000278789"
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; 64210 MW; 8598E438D4F7603E CRC64;
MIVFGWAVFL ASRSLGQGLL LTLEEHIAHF LGTGGATTTM 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