ID A0A1S3HMD7_LINUN Unreviewed; 1099 AA.
AC A0A1S3HMD7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=PDZ domain-containing protein 8 {ECO:0000313|RefSeq:XP_013386204.1};
GN Name=LOC106155760 {ECO:0000313|RefSeq:XP_013386204.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013386204.1};
RN [1] {ECO:0000313|RefSeq:XP_013386204.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013386204.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_013386204.1; XM_013530750.2.
DR AlphaFoldDB; A0A1S3HMD7; -.
DR STRING; 7574.A0A1S3HMD7; -.
DR EnsemblMetazoa; XM_013530750.2; XP_013386204.1; LOC106155760.
DR GeneID; 106155760; -.
DR KEGG; lak:106155760; -.
DR InParanoid; A0A1S3HMD7; -.
DR OrthoDB; 3681901at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd00030; C2; 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 Gene3D; 2.60.40.150; C2 domain; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001478; PDZ.
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; PF00168; C2; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 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; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000085678};
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 7..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..254
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 778..828
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 418..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1074..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..851
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..935
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1099 AA; 124974 MW; E888B35639D5818E CRC64;
MLPTLALILI SFLCGIILTL VVQIYIIARY VQRQPVSEIP YGAQTSKAAL PQELQNLVLN
LDPTKEDSCD SLNLFVQFLF RELKDTKRIR EWVTKKMNVE FEELLQTTTG RLVDEISVRH
YTLGNTFPVV KSSKVAAVKL HDDRQSMEEL DLKLDIEYSG GFKLAIDVDL IFGKSAFLSV
ELSKLKGRLR LQLSRLPFTH WSLTFYEEPI MEFEVDSRFE GRPIPQLTSL IVNQLRRTIR
KKHTLPFYKI RYGPLFPKQE PESSFPDVRH DERSICTGRL QVGQLTCSRL ADYGGDAHLY
CTLAIDSAPW VDLAMKKRRV YKTYEVPINR PVGQNLGLLF REEFNVDKYE NVLVIEAVFD
NSPAKEGNIK KGDIMSAVNG VKINSEKQAA KLIKQAGEKF NLRMERVSVV KPKKKNVQQL
SGDELEEDRL SLKEPGPDTQ SIYTEPYEDF INITEAAVNG VDGDKLESSY SGATSGEGSP
LQRRRFPFLP KQPMFLRKRM TKQGNESKGT NSSSSKATPL PSVSAPAVVK EDPAVEVVKL
KDKVKDSVSS GDSLASCRTH SDPSLNTKEE PSIPSDNMSL PDIDLPPLHI RTTRDRADTE
TDMDLRKTSL VTYAVEPKWN ENFTFEVQDH HKYFNICVWC KTSAKVDKQF RVIKPEMDFV
IGHVSIPLME IADQCLATTQ GDRQLTYTLL PSMTRGGASR SKTKLSLQRG FDESLTFGDI
TLTFRHDPGP LTPQQRKKIR EEIKKQMEDE KERKTLQIDS VRPLTVGNEE IRKSLEGGHD
FVETNFHSVT YCNFCGKKIW LKAAYQCLMC TMICHKKCIQ RCQSTITCPR NGKPPDVPKP
VQEEKTESNF HRKKEHVKEA ILTRLRKKTG SSPLITGSEE LLRASGEVKM DLPESSVGTG
VKDDNFVQTK AKKSQRRRLS NSESAETKEF DSSETNSSDS EEELNLIQFL QKHQKTHQHE
EQVVSKAKEM GRDLHADLTP IDRRDKLDAM ITKFQQEIDL ESEFRADLLK EEKEAVHPDQ
KVQLKAKVKH SEEKIQALGY LMLHYCAGLQ HCLDQMEEEK QKRKMTSDAA KVISDAAKMT
SDPANATEEK QRKEQGEEL
//
