ID A0A452EKW8_CAPHI Unreviewed; 1110 AA.
AC A0A452EKW8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=PDZ domain containing 8 {ECO:0000313|Ensembl:ENSCHIP00000012785.1};
GN Name=PDZD8 {ECO:0000313|Ensembl:ENSCHIP00000012785.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000012785.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000012785.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000012785.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR EMBL; LWLT01000025; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A452EKW8; -.
DR Ensembl; ENSCHIT00000020576.1; ENSCHIP00000012785.1; ENSCHIG00000014429.1.
DR GeneTree; ENSGT00390000017746; -.
DR OMA; HIALECM; -.
DR Proteomes; UP000291000; Chromosome 26.
DR Bgee; ENSCHIG00000014429; Expressed in prefrontal cortex and 17 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProt.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IEA:InterPro.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IEA:InterPro.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IEA:InterPro.
DR CDD; cd20825; C1_PDZD8; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd21674; SMP_PDZD8; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR039275; PDZD8.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR031468; SMP_LBD.
DR PANTHER; PTHR21519; PDZ DOMAIN-CONTAINING PROTEIN 8; 1.
DR PANTHER; PTHR21519:SF1; PDZ DOMAIN-CONTAINING PROTEIN 8; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF17820; PDZ_6; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS51847; SMP; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Lipid transport {ECO:0000256|ARBA:ARBA00023055};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW Transport {ECO:0000256|ARBA:ARBA00023055};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 90..294
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 325..408
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 798..849
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 65..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 991..1018
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 479..494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..559
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1078
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1110 AA; 123038 MW; B4E648EF8A3653A4 CRC64;
MGLLLMILAS AVLGSFLTLL TQFLLLYRKQ PEPPPDEAAR AADGFRYIKP VPGLPLREYL
YGGGGGAEEP SGGPPEGGAT PAPETPAPPT RETCYFLNAI ILFLFRELRD TALARRWVTK
KIKVEFEELL QTKTAGRLLE GLSLREVFLG ETVPFIKTIR LLRPVAPSAT GEPDGPEGEA
LPPATTPEEL AFEAEVEYNG GFHLAIDVDL VFGKSAYLFV KLSRVVGRLR FVLTRVPFTH
WFFSFVEDPL IDFEVRSQFE GRPLPQLTSF IVNQLKKIIK RKHTLPSYKI RLLIFGSYDT
EANIHCTLEL STGVWEEKQR SSIKTVELIK GNLQSVGLTL RLVQSADGYA GHVIIETVAP
NSPAAIANLQ RGDRLIAIGG VKITSTLQVL KLIKQAGDRV LVYYERPVGR SNQGTVLQDN
FGQLEENFLT GSCQPNFEEE ATGLAVDAEN RDLDSEFEDL ASDVRAQAEA REEAQSLSHS
PKRTPTTLSV KPLGTISPVL NRKLVAGSYP PPPKLPSKEG NKPLALKSSE VTEPAPVSKP
TQGSTFKPPV PPRPQVKVPL PSTDAPTQAE PDISVEKPEK VLPLPPADKP AEKQVKNVDH
IEEATAAKQF LAKQEVAKDL ISESTCAPKD SSDDHQTWES SEIPYRKKLG KWTRTRASCF
FDIEACHRYL NIALWCRDPF KLGGLICLGH VSLKLEEVAL GCLATSNMEY LSKFRLEAPS
PKAMVTRTAL RNLSMQKGFN DKFCYGDITV HFKYLKEGEP DHAVTNLEKE KELHLVEEVS
ALPKEEHFVG QMGLTENKHS FQDTQFQNPT WCDYCKKKVW TKAASQCMVC AYVCHKKCQE
KCLAETPLCG ATDQRIDRAL KNLRLEGQET LLGLPPRVDA EAGKSVNRTT GLTRHIINTS
SRLLNLRQVS KTRLSEPGTD LVEPSPKQTP NTSDNEGSDT EVCGSNSPSK RGNSAGIKLV
KKEGGLDDSV FIAVKEIGRD LYRGLPTEER IQKLEFMLDK LQNEIDQELE HNNSLVREEK
ETTDTRKKLL LSAALAKSGE RLQALTLLMI HYRAGIEDIE SSESPDQHSK KISKYTDDTE
EDLDSEITQL IDSQPFSSIS DDLFGPSESV
//
