ID A0A1S3BYU3_CUCME Unreviewed; 481 AA.
AC A0A1S3BYU3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Protein disulfide-isomerase 5-4-like {ECO:0000313|RefSeq:XP_008454535.1};
GN Name=LOC103494928 {ECO:0000313|RefSeq:XP_008454535.1};
GN Synonyms=103494928 {ECO:0000313|EnsemblPlants:MELO3C018096.2.1};
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656 {ECO:0000313|Proteomes:UP000089565, ECO:0000313|RefSeq:XP_008454535.1};
RN [1] {ECO:0000313|Proteomes:UP000089565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DHL92 {ECO:0000313|Proteomes:UP000089565};
RX PubMed=22753475; DOI=10.1073/pnas.1205415109;
RA Garcia-Mas J., Benjak A., Sanseverino W., Bourgeois M., Mir G.,
RA Gonzalez V.M., Henaff E., Camara F., Cozzuto L., Lowy E., Alioto T.,
RA Capella-Gutierrez S., Blanca J., Canizares J., Ziarsolo P.,
RA Gonzalez-Ibeas D., Rodriguez-Moreno L., Droege M., Du L.,
RA Alvarez-Tejado M., Lorente-Galdos B., Mele M., Yang L., Weng Y.,
RA Navarro A., Marques-Bonet T., Aranda M.A., Nuez F., Pico B., Gabaldon T.,
RA Roma G., Guigo R., Casacuberta J.M., Arus P., Puigdomenech P.;
RT "The genome of melon (Cucumis melo L.).";
RL Proc. Natl. Acad. Sci. U.S.A. 109:11872-11877(2012).
RN [2] {ECO:0000313|EnsemblPlants:MELO3C018096.2.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2023) to UniProtKB.
RN [3] {ECO:0000313|RefSeq:XP_008454535.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_008454535.1; XM_008456313.2.
DR EnsemblPlants; MELO3C018096.2.1; MELO3C018096.2.1; MELO3C018096.2.
DR GeneID; 103494928; -.
DR Gramene; MELO3C018096.2.1; MELO3C018096.2.1; MELO3C018096.2.
DR KEGG; cmo:103494928; -.
DR eggNOG; KOG2667; Eukaryota.
DR InParanoid; A0A1S3BYU3; -.
DR OrthoDB; 89348at2759; -.
DR Proteomes; UP000089565; Unplaced.
DR Proteomes; UP000596662; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046907; P:intracellular transport; IEA:UniProt.
DR CDD; cd02961; PDI_a_family; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR045888; Erv.
DR InterPro; IPR012936; Erv_C.
DR InterPro; IPR039542; Erv_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10984; ENDOPLASMIC RETICULUM-GOLGI INTERMEDIATE COMPARTMENT PROTEIN; 1.
DR PANTHER; PTHR10984:SF37; PROTEIN DISULFIDE-ISOMERASE 5-3; 1.
DR Pfam; PF07970; COPIIcoated_ERV; 1.
DR Pfam; PF13850; ERGIC_N; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000089565};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 443..465
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 114..263
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 270..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 481 AA; 53624 MW; A154029FBD268763 CRC64;
MISSTKLKSV DFYRKIPRDL TEATLSGAGL SIVAALSMVF LFGMELSNYL SVSTSTSVIV
DNSTDGDFLR MDFNISFPAL SCEFAAVDVH DVLGTNRLNI TKTIRKFSVD SNLRSTGSEF
HSGPLSNLIK HGDEVDEEAN EGSAVLNARN FDRYANQHPI LVVNFYAPWC YWSNRLKPSW
EKAAKTIRER YDPELDGRIL MGKVDCTEEG DLCRKHHIQG YPSIRIFRKG SDVRDDHGHH
DHESYYGDRD TDTLVKTMED LVAPLPAGSQ KLALEDKSNN GTGSVKRPAP SAGGCRIEGY
VRLKKVPGSL VIAARSESHS FDASQMNMSH IISHLSFGRK ISPKAFSDAK QLIPYIGISH
DRLNGRSFIN QRDLGANVTI EHYLQIVKTE VLTRRSGKLL EEYEYTAHSS VSQSLYIPVA
KFHFELSPMQ VVITENQKSF SHFITNVCAI IGGVFTVAGI LDALLHNTIR LMKKVELGKN
F
//
