ID A0A091CMH1_FUKDA Unreviewed; 1079 AA.
AC A0A091CMH1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Low-density lipoprotein receptor-related protein 12 {ECO:0000313|EMBL:KFO20059.1};
GN ORFNames=H920_18565 {ECO:0000313|EMBL:KFO20059.1};
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:KFO20059.1, ECO:0000313|Proteomes:UP000028990};
RN [1] {ECO:0000313|EMBL:KFO20059.1, ECO:0000313|Proteomes:UP000028990}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Liver {ECO:0000313|EMBL:KFO20059.1};
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 -!- PTM: Carbamylation allows a single lysine to coordinate two divalent
CC metal cations. {ECO:0000256|PIRSR:PIRSR611778-50}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Hydantoinase/dihydropyrimidinase family.
CC {ECO:0000256|ARBA:ARBA00008829}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR EMBL; KN124863; KFO20059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091CMH1; -.
DR STRING; 885580.ENSFDAP00000007914; -.
DR eggNOG; KOG2584; Eukaryota.
DR Proteomes; UP000028990; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd00041; CUB; 2.
DR CDD; cd01314; D-HYD; 1.
DR CDD; cd00112; LDLa; 3.
DR Gene3D; 4.10.1220.10; EGF-type module; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR011778; Hydantoinase/dihydroPyrase.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR NCBIfam; TIGR02033; D-hydantoinase; 1.
DR PANTHER; PTHR11647:SF50; DIHYDROPYRIMIDINASE; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF00431; CUB; 2.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00042; CUB; 2.
DR SMART; SM00192; LDLa; 3.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 3.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR PROSITE; PS01180; CUB; 2.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 3.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Lipoprotein {ECO:0000313|EMBL:KFO20059.1};
KW Receptor {ECO:0000313|EMBL:KFO20059.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT DOMAIN 1..100
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 200..313
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 1031..1079
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 644
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR611778-50"
FT DISULFID 107..119
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 114..132
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 126..141
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 180..195
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 345..360
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1079 AA; 119174 MW; 872BBAF37DA11907 CRC64;
MITSPGWPSA YPVRLNCSWL IKANPGEIIT ISFQDFDIQG SRRCSLDWLT IETYKNIESY
RACGSTVPPP YISSQDHLWI RFHSDDSVSR KGFRLAYFSG KSEEPDCACD QFHCGNGKCI
PEAWQCNNMD ECGDSSDEEL CAREASPPTA ASFQPCAYNQ FQCLSRFTKV YTCLPESLKC
DGNIDCLDLG DEIDCDVPTC GQWLKYFYGT FNSPNYPDFY PPGSNCTWLI DTGDRRKVII
RFTDFKLDGT GYGDYVKIYD GLEENPRRLL RVLTAFDSHA PLTVVSSSGQ IRVHFCADKV
NAARGFNATY QVDGFCLPWE IPCGGNWGCY TEQQRCRCVF ESWVCDSQDD CGDGSDEESC
PVIVPTRVIT AAVIGSLICG LLLVIALGCT CKLYSLRMFE RRSFETQLSR VEAELLRREA
PPSYGQLIAQ GLIPPVEDFP VCSPSQASVL ENLRLAVRSQ LGFTSIRLPM AGRSSGLWNR
IFSFARSRHS GSLALVSASG DEAAPQYLSI SPPSPHTPDV PWAHGGPRSS PSCVSSVTPM
GLTLHVTCCA LLVASAPVEM SLCHAGLRRN GGRAALAGGT TTIIDFAIPP KGGSLLDAFH
TWRRWADPKV CCDYSLHVAV TWWSEQVKEE MAILTREKGV NSFKMFMAYK DTFMVRDPEL
YAAFKQCKEI GAIAQVHAEN GDLIAEEAKK MLALGITGPE GHALCRPEVV EAEATLRAIT
LASVVSCPLY VVHVMSRSAA KVIADARREG KVVYGEPIAA SLGTDGTHYW HEEWSHAAHH
VMSPPLRPDP STPGFLMNLL ANDDLTTTAT DHCTFNTCQK ALGKDDFTKI PNGVNGVEDR
MSVIWEKGVH SGKMDENRFV AVTSTNAAKI FNLYPRKGRI AVGSDADIVI WDPNATRTIS
ANTHHQAVNF NIFEGMVCHG VPLVTISRGK VVYEAGELSV SPGHGKFIPR EPFAEYVYKR
VQQRDQVRYA TRCCSQQAGH RSGVWGAMEV LTPHSVHCWC EPVPLSPFKF LLVQVHGPWG
LWAIQLVRDP KKHPDNKDAG SHQGRPLEEG RGPRALESSA KPLKCDPRRE RRKRGAEGP
//
