ID A0A2K5MP70_CERAT Unreviewed; 1154 AA.
AC A0A2K5MP70;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=PDZ domain containing 8 {ECO:0000313|Ensembl:ENSCATP00000027032.1};
GN Name=PDZD8 {ECO:0000313|Ensembl:ENSCATP00000027032.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000027032.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000027032.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR RefSeq; XP_011898450.1; XM_012043060.1.
DR AlphaFoldDB; A0A2K5MP70; -.
DR STRING; 9531.ENSCATP00000027032; -.
DR Ensembl; ENSCATT00000051274.1; ENSCATP00000027032.1; ENSCATG00000036913.1.
DR GeneID; 105577950; -.
DR KEGG; caty:105577950; -.
DR CTD; 118987; -.
DR GeneTree; ENSGT00390000017746; -.
DR OMA; HIALECM; -.
DR OrthoDB; 3681901at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000036913; Expressed in liver and 12 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IEA:Ensembl.
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:0007010; P:cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IEA:Ensembl.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IEA:Ensembl.
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 Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
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:UP000233060};
KW Transport {ECO:0000256|ARBA:ARBA00023055};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 91..294
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 366..449
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 840..891
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 66..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1132..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1033..1060
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 586..600
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 967..996
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1154 AA; 128650 MW; D4168E34E44BD093 CRC64;
MGLLLMILAS AVLGSFLTLL AQFLLLYRRQ PEPPADEAAR AGEGFRYIKP VPGLLLREYL
YGGGRDEEPS GAAPEGGATP TAAPETPAPP TRETCYFLNA TILFLFRELR DTALTRRWVT
KKIKVEFEEL LQTKTAGRLL EGLSLRDVFL GETVPFIKTI RLIRPVVPSA TGEPDGPEGE
ALPAACPEEL AFEAEVEYNG GFHLAIDVDL VFGKSAYLFV KLSRVVGRLR LVFTRVPFTH
WFFSFVEDPL IDFEVRSQFE GRPMPQLTSI IVNQLKKIIK RKHTLPSYKI RFKPFFPYQT
LQGFEEDEEH IHIQQWALTE GRLKVTLLEC SRLLIFGSYD REANVHCTLE LSSSVWEEKQ
RSSIKTVELI KGNLQSVGLT LRLVQSTDGY AGHVIIETVA PNSPAAIADL QRGDRLIAIG
GVKITSTLQV LKLIKQAGDR VLVYYERPVG QSNQGAVLQD NFGQLEENFL SSSCQSGYEE
EAAGLTVDTE SRELDSEFED LASDVRAQNE FKDEAQSLSH SPKRTPTTLS IKPLGAISPV
LNRKLAVGSH PLPPKIQSKD GNKPPPLKTS EITDPAQVSK PTQGSTFKPP VPPRPQVKVP
LPSTDAPNQA EPDVLVEKPE KVPPPPLVDK SAEKQAKNVD PIDDAAASKQ FLAKQEVAKD
VTSETSCPTK DSSDDRQTWE SSEILYRNKL GKWTRTRASC LFDIEACHRY LNIALWCRDP
FKLGGLICLG HVSLKLEDVA LGCLATSNME YLSKLRLEAP SPKAIVTRTA LRNLSMQKGF
NDKFCYGDIT IHFKYLKEGE SDHHVVTNVE KEKEPHLVEE VSVLPKEEQF VGQMGLTENK
HSFQDTQFQN PTWCDYCKKK VWTKAASQCM FCAYVCHKKC QEKCLAETSV CGATDRRIDR
TLKNLRLEGQ ETLLGLPPRV DAEASKSVNK TTGLTRHIIN TSSRLLNLRQ VSKTRLSEPG
TDLVEPSPKH TPNTSDNEGS DTEVCGPNSP SKRGNSTGIK LVRKEGGLDD SVFIAVKEIG
RDLYRGLPTE ERIQKLEFML DKLQNEIDQE LEHNNSLVRE EKETTDTRKK SLLSAALAKS
GERLQALTLL MIHYRAGIED IETLESLSLD QHSKKISKYT DDTEEDLDNE ISQLIDSQPF
SSISDDLFGP SESV
//