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8.A.88.2.3 Protein disulfide-isomerase, TMX3, of 454 aas and 2 TMSs, N- and C-terminal. It probably participates in the folding of proteins containing disulfide bonds as a dithiol oxidoreductase because it catalyzes the rearrangement of -S-S- bonds in proteins. (Haugstetter et al. 2005).
Accession Number:	Q96JJ7
Protein Name:	Protein disulfide-isomerase TMX3
Length:	454
Molecular Weight:	51872.00
Species:	Homo sapiens (Human) [9606]
Number of TMSs:	1
Location¹ / Topology² / Orientation³:	Endoplasmic reticulum membrane¹ / Single-pass membrane protein²
Substrate	electron

UniProt (Universal Protein Resource)
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FASTA formatted sequence

1:	MAAWKSWTAL RLCATVVVLD MVVCKGFVED LDESFKENRN DDIWLVDFYA PWCGHCKKLE 
61:	PIWNEVGLEM KSIGSPVKVG KMDATSYSSI ASEFGVRGYP TIKLLKGDLA YNYRGPRTKD 
121:	DIIEFAHRVS GALIRPLPSQ QMFEHMQKRH RVFFVYVGGE SPLKEKYIDA ASELIVYTYF 
181:	FSASEEVVPE YVTLKEMPAV LVFKDETYFV YDEYEDGDLS SWINRERFQN YLAMDGFLLY 
241:	ELGDTGKLVA LAVIDEKNTS VEHTRLKSII QEVARDYRDL FHRDFQFGHM DGNDYINTLL 
301:	MDELTVPTVV VLNTSNQQYF LLDRQIKNVE DMVQFINNIL DGTVEAQGGD SILQRLKRIV 
361:	FDAKSTIVSI FKSSPLMGCF LFGLPLGVIS IMCYGIYTAD TDGGYIEERY EVSKSENENQ 
421:	EQIEESKEQQ EPSSGGSVVP TVQEPKDVLE KKKD

8.A.88.2.3
Protein disulfide-isomerase, TMX3, of 454 aas and 2 TMSs, N- and C-terminal. It probably participates in the folding of proteins containing disulfide bonds as a dithiol oxidoreductase because it catalyzes the rearrangement of -S-S- bonds in proteins. (Haugstetter et al. 2005).

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8.A.88.2.3Protein disulfide-isomerase, TMX3, of 454 aas and 2 TMSs, N- and C-terminal. It probably participates in the folding of proteins containing disulfide bonds as a dithiol oxidoreductase because it catalyzes the rearrangement of -S-S- bonds in proteins. (Haugstetter et al. 2005).

Cross database links:

External Searches:

Analyze:

8.A.88.2.3
Protein disulfide-isomerase, TMX3, of 454 aas and 2 TMSs, N- and C-terminal. It probably participates in the folding of proteins containing disulfide bonds as a dithiol oxidoreductase because it catalyzes the rearrangement of -S-S- bonds in proteins. (Haugstetter et al. 2005).