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Database: UniProt
Entry: A0A1S3GB00_DIPOR
LinkDB: A0A1S3GB00_DIPOR
Original site: A0A1S3GB00_DIPOR 
ID   A0A1S3GB00_DIPOR        Unreviewed;       622 AA.
AC   A0A1S3GB00;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Ran-binding protein 9 {ECO:0000256|ARBA:ARBA00039980};
GN   Name=Ranbp9 {ECO:0000313|RefSeq:XP_012885875.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012885875.1};
RN   [1] {ECO:0000313|RefSeq:XP_012885875.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012885875.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the RANBP9/10 family.
CC       {ECO:0000256|ARBA:ARBA00006535}.
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DR   RefSeq; XP_012885875.1; XM_013030421.1.
DR   AlphaFoldDB; A0A1S3GB00; -.
DR   STRING; 10020.ENSDORP00000004941; -.
DR   GeneID; 105996365; -.
DR   KEGG; dord:105996365; -.
DR   CTD; 10048; -.
DR   InParanoid; A0A1S3GB00; -.
DR   OrthoDB; 38145at2759; -.
DR   Proteomes; UP000081671; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   CDD; cd12909; SPRY_RanBP9_10; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013144; CRA_dom.
DR   InterPro; IPR024964; CTLH/CRA.
DR   InterPro; IPR006594; LisH.
DR   InterPro; IPR003877; SPRY_dom.
DR   InterPro; IPR035782; SPRY_RanBP9/10.
DR   PANTHER; PTHR12864; RAN BINDING PROTEIN 9-RELATED; 1.
DR   PANTHER; PTHR12864:SF56; RAN-BINDING PROTEIN 9; 1.
DR   Pfam; PF10607; CTLH; 1.
DR   Pfam; PF08513; LisH; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM00757; CRA; 1.
DR   SMART; SM00667; LisH; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50896; LISH; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671}.
FT   DOMAIN          72..259
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..383
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  68400 MW;  B611BF920C69D7C7 CRC64;
     MEEGNKKKKA GRGQRERRSG PGAGGGARAH SPPTPGGTAR SGPAGIDYSR LGDPRRPGPE
     QPRALNEQEK ELQRRLKRLY PAVDEQETPL PRSWSPKDKF SYIGLSQNNL RVHYKGHGKT
     PKDAASVRAT HPIPAACGIY YFEVKIVSKG RDGYMGIGLS AQGVNMNRLP GWDKHSYGYH
     GDDGHSFCSS GTGQPYGPTF TTGDVIGCCV NLINNTCFYT KNGHSLGIAF TDLPPNLYPT
     VGLQTPGEVV DANFGQHPFV FDIEDYMREW RTKIQAQIDR FPIGDREGEW QTMIQKMVSS
     YLVHHGYCAT AEAFARSTDQ TVLEELASIK NRQILFSFRV RQFIEMVNGT DSEVRCLGGR
     SPKSQDSYPV SPRPFSSPSM SPSHGMNIHT LASGKGSTAH FSGFESCSNG VISNKAHQSY
     CHSKHQSPNL NVPELNSINM SRSQQVNNFT SNDVDMETDH YSNGVGETSS NGFLNGSSKH
     DHEMEDCDTE MEVDSSQLRR QLCGGSQAAI ERMIHFGREL QAMSEQLRRE CGKNTANKKM
     LKDAFSLLAY SDPWNSPVGN QLDPIQREPV CSALNSAILE THNLPKQPPL ALAMGQATQC
     LGLMARSGIG SCAFATVEDY LH
//
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