ID A0A091CTQ0_FUKDA Unreviewed; 1006 AA.
AC A0A091CTQ0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Sortilin {ECO:0000313|EMBL:KFO22819.1};
GN ORFNames=H920_15766 {ECO:0000313|EMBL:KFO22819.1};
OS Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Fukomys.
OX NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO22819.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO22819.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO22819.1};
RA Gladyshev V.N., Fang X.;
RT "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT African mole rats.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase T1A family. {ECO:0000256|PROSITE-
CC ProRule:PRU00808}.
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DR EMBL; KN123939; KFO22819.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091CTQ0; -.
DR STRING; 885580.ENSFDAP00000004917; -.
DR eggNOG; KOG3511; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IEA:UniProtKB-UniRule.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd03753; proteasome_alpha_type_5; 1.
DR CDD; cd15482; Sialidase_non-viral; 1.
DR Gene3D; 2.10.70.80; -; 1.
DR Gene3D; 3.30.60.270; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR023332; Proteasome_alpha-type.
DR InterPro; IPR033812; Proteasome_alpha_type_5.
DR InterPro; IPR001353; Proteasome_sua/b.
DR InterPro; IPR031777; Sortilin_C.
DR InterPro; IPR031778; Sortilin_N.
DR InterPro; IPR006581; VPS10.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR12106:SF23; SORTILIN; 1.
DR PANTHER; PTHR12106; SORTILIN RELATED; 1.
DR Pfam; PF00227; Proteasome; 1.
DR Pfam; PF15902; Sortilin-Vps10; 1.
DR Pfam; PF15901; Sortilin_C; 1.
DR SMART; SM00602; VPS10; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942, ECO:0000256|PROSITE-
KW ProRule:PRU00808}; Reference proteome {ECO:0000313|Proteomes:UP000028990};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 935..956
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 278..890
FT /note="VPS10"
FT /evidence="ECO:0000259|SMART:SM00602"
FT REGION 889..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1006 AA; 111463 MW; FEE3BFE1D9C79A09 CRC64;
MRSREQRVLG VSAVWLELGA GGPLLVLESP PWPLPPFPVF AMFLTRSEYD RSVRRAESGT
GFWLGSTAIG IQTSEGVCLA VEKRITSPLM EPSSIEKIVE IDAHIGCAMS GLIADAKTLI
DKARVETQNH WFTYNETMTV ESVTQAVSNL ALQFGEEDAD PGAMSRPFGV ALLFGGVDEK
GPQLFHMDPS GTFVQCDARA IGSASEGAQS SLQEVYHKSM TLKEAIKSSL IILKQVMEEK
LNATNIEHVF DDLSGSVSLS WVGDRTGVIL VLTTFHVPLV IMTFGQSKLY RSEDYGKNFK
DITNLINNTF IRTEFGMAIG PENSGKVILT AEVSGGSHGG RIFRSSDFAK NFIQTDLPFH
PLTQMMYSPQ NSDYLLALST ENGLWVSKNF GGKWEEIHKA VCLAKWGSEN IIFFTTYVNG
SCKADLGALE LWRTSDLGKT FKTIGVKIYS FGLGGRFLFA SVMADKDTTR RIHVSTDQGD
TWSMAQLPSV GQEQFYSILA ANDDMVFMHV DEPGDTGFGT IFTSDDRGIV YSKSLDRHLY
TTPGGETDFT NVTSLRGVYI TSMLSEDNSI QTMITFDQGG RWKHLRKPEN SECDATAKNK
NECSLHIHAS YSISQKLNVP MAPLSEPNAV GIVIAHGSVG DAISVMVPDV YISDDGGYSW
MKMLEGPHYY TILDSGGIIV AIEHSSHPIN VIKFSTDEGQ CWQTYTFTRE PIYFTGLASE
PGARSMNISI WGFTESFLTR QWVSYTIDFK DILERNCEER DYTIWLAHST DPGDYEDGCI
LGYREQYLRL RKSSVCQNGR DYVVTKQPSI CPCSLEDFLC DFGYFRPENE SKCVEQPELK
GHDLEFCLYG REEHLTTTGY RKIPGDRCQG GVNPAREVKD LKKKCTSNFL SPKTQDSRPQ
GHSLSQNPAP PPLGYTENTH FLSPTQKQNS KSNSVPIILA IVGLMLVTVV AGVLIVKKYV
CGGRFLVHRY SVLQQHAEAD GVDALDTASR ANKSGYHDDS DEDLLE
//
