ID A0A3B4YJN5_SERLL Unreviewed; 1157 AA.
AC A0A3B4YJN5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=PDZ domain containing 8 {ECO:0000313|Ensembl:ENSSLDP00000023124.1};
GN Name=PDZD8 {ECO:0000313|Ensembl:ENSSLDP00000023124.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000023124.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000023124.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A3B4YJN5; -.
DR Ensembl; ENSSLDT00000023864.1; ENSSLDP00000023124.1; ENSSLDG00000018047.1.
DR GeneTree; ENSGT00390000017746; -.
DR Proteomes; UP000261360; Unplaced.
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; cd00987; PDZ_serine_protease; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00023055};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..272
FT /note="SMP-LTD"
FT /evidence="ECO:0000259|PROSITE:PS51847"
FT DOMAIN 345..428
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 849..900
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 56..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 814..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1030..1057
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 494..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..595
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..660
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..680
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 962..995
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1157 AA; 128392 MW; D59459C5D4D2DE4C CRC64;
MIYLMLISAL SGAVVTLILQ FLLIYRRSPE PVSRTVQYVK VVPDNALKDY FNTQHAEPGQ
QQQDSTTSPP PPSQSEPIDA TKPETCNFLN AIFLFLFREL RDTPVVRHWL TKKIKVEFEE
LLQTKTAGRL LEGLSLRDIS LGNSLPVFKT ATLMKPAHLN EDGMPEELNF EVDLEYNGGF
HLAIDVELVF GKSAYLFVKM RRVVGRLRLQ FTRMPFSHWS FSFLEDPLVD FEVKSQFEGR
PLPQLTSIIV NQLKRVIKKK HTLPNYKIRY KPFFPFQVQP LLGSACDLDL SVQDSRLVEG
RLKVTLIECS RLFILGSYDR ETHVHCTLEL SSNQWKEKTR SSIKRTEVIK GPCGSVGMTF
RHVPATEGDA VHVSIETVTP NSPAHLADLQ KGDRLIAIGG VKVTSSVQVP KLLKQAGDRV
LVLYERPVRH QTSSLGTLGT LQEGFGQLEE TGFIPQPGGY EEDPAPITTL SDMSDSKDMD
SEFEELIVDK PGHTGGPNNS TTNTSDTKEE FLLTVNQSPK RTVATLASKP LGTISPILNR
KLNLVGLQSP LKPQPKESPK PSPHKTSSDA GEGLQRPTIP PPPPPSRPPV PPRPQIRLTS
ASSETSLLEG VDSVTTATAA VAGTEKICVK QAEAKQSTRP AESTDELPVP PTVTSSSKAD
QAKDKASESS CSTRDSLEDH SILESPETMF RNQTARWPKA SMVFEVESNH KYLNVALWCK
DPFKLGSLLC LGHVSLQLEH VALECMATSS AEYQSTFRLG PPEPRANVSR TALRSLSSHK
GFNEKLCYGD ITLNFCYLAE GDFEYPGGLV EREREGSLHD EDLKEREREH VPSAPRDDLA
YSTMQVEVRH NFQDTQFQNP TWCEYCKKKV WTKAASQCMV CAYVCHKKCQ DKCLSENPFC
VAATERRGAD PEAKSTINRA TTGLTRHIIN TSSRLLNLRQ VPKTRLVEQV ADVVPGAVEP
SPKHTPNTSD NESSDTETYT SGASPSKQPA SSGGSSKLVR KEGGLDDSVF IAVKEIGRDL
YRGLPTDERS QKLELMLDKL QQEIDQELEH NNALLLEERE ATDARRKALI STALAKSGER
LQALTLLMIH YRAGIEDLES VESTSPSEQQ GFKGKGEGLE EEALIGTEVY DSDICSPVEV
QLLDDITEEQ ICVEALH
//
