ID A0A3B0JPC9_DROGU Unreviewed; 1374 AA.
AC A0A3B0JPC9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Blast:Protein disulfide-isomerase A5 {ECO:0000313|EMBL:SPP73028.1};
GN ORFNames=DGUA_6G000433 {ECO:0000313|EMBL:SPP73028.1};
OS Drosophila guanche (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP73028.1, ECO:0000313|Proteomes:UP000268350};
RN [1] {ECO:0000313|Proteomes:UP000268350}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Alioto T., Alioto T.;
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; OUUW01000001; SPP73028.1; -; Genomic_DNA.
DR STRING; 7266.A0A3B0JPC9; -.
DR OMA; CTDHENC; -.
DR Proteomes; UP000268350; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd02961; PDI_a_family; 4.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 12.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR19991:SF2; GH08893P; 1.
DR PANTHER; PTHR19991; L 2 01289; 1.
DR Pfam; PF00085; Thioredoxin; 2.
DR Pfam; PF13848; Thioredoxin_6; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 8.
DR PROSITE; PS51352; THIOREDOXIN_2; 5.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:SPP73028.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..1374
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017351795"
FT TRANSMEM 1337..1357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..172
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 329..492
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 543..705
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 896..1009
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 1094..1242
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 1374 AA; 158989 MW; 8FF1CDF80EC0FD0F CRC64;
MTFTRLKTVT LLVTCALLAL SFPGYVNCAN NGKKGSQPAA AAAPLEPEAV IEEVNAKQLE
KLLADKDYVA VFWYARSCVT CDKVLAELEK IDDDTDSFGV DFVKINDKRL AKQYGIKNFP
ALTYFREKEP IIYDGDLMDE EGVLDFLTSL EAMDLPDRIE EVNAKILQKI IEDTDFVAVL
FYDKDQKKSQ KILAELENID DECDQNDIAF VKIDDDKEAK EWGIDEIPSI VLFERGIPHI
YEGDLMKEDE LLGWLVHQKR YSEIPEVTDE MKDKLVENTE HLAVIFYDKD DKQDMRILNE
LENIDDELEK EGIVIVRIDN AAEAKEYGLD HLPALIYFEN KIPALYEGDL MNEDEVLEWL
LVQKKTATIE EVTDEILVNL INEHEYVVVF FTGPCEPGET CDHTLNALET IDDELDEAGI
IFVTTEDTGV AKKYNVKTYP RLVFFRNRDP LHFTGDLDDE DEVLAWITDD ETLEIPGKIE
EVNVKMLDKI LAENDHVVVF FYAEGDKKAQ KILNELENID DECEEKDIDF VKTSDDDIDK
EYDLPGLPAL AFYRHKFRTI YTGDLMKEEE ILEWVIDLHE STADVIESVD RKTLQVLIND
VEHLAVFFYD DECETCSDIL DELENIDDDT DKHGIQFVKS NDVKLAHEIG IFAFPALVYY
ETGVPIMYDG NLDSNQEVFN WILEQKADQS IELIDREQLL EYIGTKDFLA VVFYKEDDPD
SPRVLRHIEL IDDEASEYGI YIVKMHDKLM AKKYGFRNPP GLTYFRKGKY INYDGDIDDE
EEVLDWLTSP ANMEMTDHIE QVNRKMFEKI RKNSDYVAVI FYSDECKQCP RVLAEVEHID
DEADKAGIDF VKIDDKLMAK EYGVFALPAI VFFKPTSKEP VIYAGDLYEE EQILTWLITQ
KDPSGDVIED LEGERLVHLI EESGSIAVYF YADGCEQCTK VLEELENIDD DCDKHGITFV
KTRDFSVADG YGVHEYPALV YFEGGIPNVF EGELSEEEEV LQWLITQKTE DRIELITRQM
LETMVEETQY LAVYFYKINC NICDQILEGL ELIDDECDVF GIHMVKIQDP QLAKRYSIKT
FPALVYFRNG NPLLFEGDLQ NEQSVLEWLI DDDNRELADE IEEVNERMLD RLMAESTLLV
VFFYDDDCAE CEEILEELEE IDGEADMFGI DFVKIASMEA AKKYEIVNIP SLVYYRKQVP
VLYDGDMHQH DKVITWLTSQ DVFEIKNEIE EVNRKMLDKL LEENEFLSVF FYEHNHPDSI
ASLEKLENID SETDNLDITF VKMADSRYAK KWGVTKLPAM VYFRRRFPSI YRGDLLSEDE
VLEWLRKNRF RQPELNIFMY ALIALALAFV VYTAFLLQCF KPAPPPPVQH TKQS
//