ID A0A2U9CEG9_SCOMX Unreviewed; 1221 AA.
AC A0A2U9CEG9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 08-NOV-2023, entry version 25.
DE SubName: Full=Putative PDZ domain-containing protein 8 {ECO:0000313|EMBL:AWP14460.1};
GN ORFNames=SMAX5B_008488 {ECO:0000313|EMBL:AWP14460.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP14460.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP14460.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP026257; AWP14460.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9CEG9; -.
DR STRING; 52904.ENSSMAP00000027464; -.
DR Proteomes; UP000246464; Chromosome 15.
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:0048468; P:cell development; IEA:UniProt.
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; cd00136; PDZ; 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:UP000246464};
KW Transport {ECO:0000256|ARBA:ARBA00023055};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 118..308
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 381..464
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 913..964
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 74..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1094..1121
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 74..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..632
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 694..731
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1059
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1221 AA; 134965 MW; 00754D38FBBF3827 CRC64;
MIYLILVSAL SGAVVTLILQ FLLIYRRSPE PVGRTVQYVK VVPGNALKDY FNTQHAEAGQ
QQQQQQDAAA AQRQQEAAAA SSARHQEAAV TGGSPKQQPS PPPPMPQPQS EGTDGATKPE
TCNFLNAIFL FLFRELRDTP LLRHWLTKKI KVEFEELLQT KTAGRLLEAL SLRDISLGDS
LPVFKTARLM RPAQLNDDGM PEELNFEVDL EYNGGFHLAI DVELVFGKCA YLFVKMRRVV
GRLRLQFTRV PFSHWSFSFL EDPLVDFEVR SQFEGRPLPQ LTSIIVNQLK RVIKKKHTLP
NYKIRYKPFF PFQVQPPLGS VCDLDLSVQD SRLVEGRLKV TLIECSRLFI LGSYDRETHV
HCTLELSSHQ WKEKSRSSIK RTEVIKGPCG SVGMTFRHVP ATEGDAVHVS IETVTPNSPA
ALADLQRGDR LIAIGGVKVT SSVQVPKLLK QAGDRVVVLY ERPVRHQAPS LGSLGTLQEG
FGQLEETGFI PQPGGYEEEP APITTLSDIS DSKDMDSEFE ELIVDSKLNQ TGGPNSSTTN
TSESKEDFLL TVNQSPKRTV ANLASKPLGS ISPILNRKLN LVGLQSPLKP QPKESPKPSP
HKTSGDPGEG LQRPTVPPPP PPSRPLLPPR PQIRLTPASS ETSLLEGVDS VTTTNATVAP
TATATVCASE KSPEKAPLTA ANEERAGTEK TCVKQAEAKQ TAKPNESSDE VPGPSTATNS
SKAYQTKDKA SDGSCSTRDS LEDHAIWESP ETMFRNQTAR WPKASMVCDV ESNHKYLNVA
LWCKDPFKLG SLLCLGHVSL QLEHVALECM ATSSAEYQST FRLGPTEPRA NVSRTALRSL
GTHKGFNEKL CYGDVTLNFC YLAEGDFEYQ GGLVEREEGS LHDEDLRERE REHIPSAPRD
DLAYGAMQLV EVRHNFQDTQ FQNPTWCEYC KKKVWTKAAS QCMICAYVCH KKCQDKCLSE
NPFCVAATER RGADPEAKST INRATTGLTR HIINTSSRLL NLRQVQKTRL VEQVVDVVPG
TVEPSPKHTP NTSDNESSDT ETYTSGASPS KQPVSSGGSS KLVRREGGLD DSVFIAVKEI
GRDLYRGLPT DERSQKLELM LDKLQQEIDQ ELEHNTALLL EEREATDSRR KALINTALTK
SGERLQALTL LMIHYRAGIE DLESVESTSP SEQQGFKGKG EGLEEEALMG TEVYDSDICS
PVEVQLLDDI TEEQICVEAL H
//