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Database: UniProt
Entry: A0A2Y9KSU3_ENHLU
LinkDB: A0A2Y9KSU3_ENHLU
Original site: A0A2Y9KSU3_ENHLU 
ID   A0A2Y9KSU3_ENHLU        Unreviewed;       581 AA.
AC   A0A2Y9KSU3;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Protein disulfide-isomerase-like protein of the testis {ECO:0000313|RefSeq:XP_022372245.1};
GN   Name=LOC111156009 {ECO:0000313|RefSeq:XP_022372245.1};
OS   Enhydra lutris kenyoni (northern sea otter).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Lutrinae; Enhydra.
OX   NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022372245.1};
RN   [1] {ECO:0000313|RefSeq:XP_022372245.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022372245.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the protein disulfide isomerase family.
CC       {ECO:0000256|ARBA:ARBA00006347}.
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DR   RefSeq; XP_022372245.1; XM_022516537.1.
DR   AlphaFoldDB; A0A2Y9KSU3; -.
DR   STRING; 391180.A0A2Y9KSU3; -.
DR   KEGG; elk:111156009; -.
DR   OrthoDB; 5399045at2759; -.
DR   Proteomes; UP000248482; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   CDD; cd02961; PDI_a_family; 1.
DR   CDD; cd02995; PDI_a_PDI_a'_C; 1.
DR   CDD; cd02982; PDI_b'_family; 1.
DR   CDD; cd02981; PDI_b_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 4.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR18929; PROTEIN DISULFIDE ISOMERASE; 1.
DR   PANTHER; PTHR18929:SF58; PROTEIN DISULFIDE-ISOMERASE-LIKE PROTEIN OF THE TESTIS; 1.
DR   Pfam; PF00085; Thioredoxin; 2.
DR   Pfam; PF13848; Thioredoxin_6; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 4.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..581
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016073578"
FT   DOMAIN          371..494
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          538..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..581
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   581 AA;  66930 MW;  82960169204974CB CRC64;
     MKLLWMSLLL VAFCISTVRG LPEEDIKEAS INISQPMHIV EEGNLLVLTP AGLTQMLNQT
     RFLMVLFHNP SSKQSRNLAE ELGQAVEVMG KGKNGIGFGK VDITVEKELQ KEFDVKKAPE
     LKLFFEGNRS EPISCKGVVE STALVVWLRR QISQKAFLFN NTQQVVEFVN SRPLVIIGFF
     QDLEEEVAEL FYDMIKDFPE LTFGVISISN VIGRFHVTLD SVLVFKKGKI VKREELINDI
     TNKHVLNQVI KEHLTNFVIE YNTENKDLIY ELHILNHMLL FASKSWESFG LIMQHYKLAS
     KEFTNKILFI LVNADEPRNG QILKYFRITE ANIPCVQILN LSSDARYKMP SEEITYENLK
     KFGHSFLNRN AKKHQSSEDI PKYWDQGPVK QLVGKNFNVV VFDKERDVFV MFYAPWSEKC
     KALFPVLEEL GRKYQNHSTV TIAKMDITAN DILLMYLDRY PFFRLFPINS QQAVLYTGEH
     TLRGFSDFLE SQIKTRIEDE DEDELLSVEQ SEVTEEEALA EEKKVPFIKE ELPDQKLPEL
     ENVTVPLEPA GLKETAEEEE KVAKPKGPPK QEKKPKVKEE L
//
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