Q9BS26 (ERP44_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Endoplasmic reticulum resident protein 44
Short name=ER protein 44
Short name=ERp44

Alternative name(s):
Thioredoxin domain-containing protein 4

Gene names

Name:	ERP44
Synonyms:	KIAA0573, TXNDC4
ORF Names:	UNQ532/PRO1075

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	406 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1L and ERO1LB in the endoplasmic reticulum. Ref.1 Ref.7
Subunit structure	Forms mixed disulfides with both ERO1L and ERO1LB and cargo folding intermediates. Directly interacts with ITPR1 in a pH-, redox state- and calcium-dependent manner, but not with ITPR2 or ITPR3. The strength of this interaction inversely correlates with calcium concentration By similarity. Ref.1 Ref.9
Subcellular location	Endoplasmic reticulum lumen.
Induction	By endoplasmic reticulum stress. Ref.1
Sequence similarities	Contains 1 thioredoxin domain.
Sequence caution	The sequence BAA25499.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Endoplasmic reticulum
Domain	Signal
Molecular function	Chaperone
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Traceable author statement Ref.1. Source: UniProtKB glycoprotein metabolic process Inferred from direct assay Ref.1. Source: UniProtKB response to unfolded protein Inferred from direct assay Ref.1. Source: UniProtKB
Cellular_component	cell surface Inferred from direct assay PubMed 19995400. Source: MGI endoplasmic reticulum lumen Inferred from direct assay Ref.1. Source: UniProtKB endoplasmic reticulum membrane Inferred from direct assay Ref.1. Source: UniProtKB endoplasmic reticulum-Golgi intermediate compartment Inferred from direct assay PubMed 15308636. Source: UniProtKB
Molecular_function	protein disulfide isomerase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Chain

30 – 406

377

Endoplasmic reticulum resident protein 44

PRO_0000034180

Regions

Domain

30 – 138

109

Thioredoxin

Region

236 – 285

50

Interaction with ITPR1 By similarity

Motif

403 – 406

4

Prevents secretion from ER Potential

Amino acid modifications

Disulfide bond

189 ↔ 241

Ref.11

Disulfide bond

301 ↔ 318

Ref.11

Experimental info

Sequence conflict

35

1

D → A in AAQ89407. Ref.3

Secondary structure

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406

Helix Strand Turn

Details...

Turn

36 – 38

3

Helix

39 – 45

7

Beta strand

47 – 54

8

Helix

59 – 75

17

Beta strand

85 – 91

7

Turn

92 – 94

3

Helix

96 – 101

6

Beta strand

106 – 114

9

Beta strand

117 – 122

6

Helix

129 – 140

12

Beta strand

145 – 147

3

Beta strand

162 – 168

7

Beta strand

170 – 172

3

Helix

173 – 185

13

Turn

186 – 188

3

Beta strand

190 – 196

7

Beta strand

208 – 212

5

Beta strand

214 – 218

5

Helix

230 – 241

12

Beta strand

244 – 247

4

Helix

250 – 257

8

Beta strand

263 – 268

6

Helix

274 – 286

13

Helix

288 – 290

3

Turn

291 – 293

3

Beta strand

294 – 300

7

Turn

301 – 304

4

Helix

305 – 310

6

Helix

315 – 317

3

Beta strand

319 – 324

6

Beta strand

329 – 331

3

Helix

336 – 339

4

Helix

343 – 353

11

Helix

387 – 390

4

Turn

394 – 396

3

Sequences

	Sequence		Length	Mass (Da)
	Q9BS26 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 3865DCF3811BC263	FASTA	406	46,971
	10 20 30 40 50 60 MHPAVFLSLP DLRCSLLLLV TWVFTPVTTE ITSLDTENID EILNNADVAL VNFYADWCRF 70 80 90 100 110 120 SQMLHPIFEE ASDVIKEEFP NENQVVFARV DCDQHSDIAQ RYRISKYPTL KLFRNGMMMK 130 140 150 160 170 180 REYRGQRSVK ALADYIRQQK SDPIQEIRDL AEITTLDRSK RNIIGYFEQK DSDNYRVFER 190 200 210 220 230 240 VANILHDDCA FLSAFGDVSK PERYSGDNII YKPPGHSAPD MVYLGAMTNF DVTYNWIQDK 250 260 270 280 290 300 CVPLVREITF ENGEELTEEG LPFLILFHMK EDTESLEIFQ NEVARQLISE KGTINFLHAD 310 320 330 340 350 360 CDKFRHPLLH IQKTPADCPV IAIDSFRHMY VFGDFKDVLI PGKLKQFVFD LHSGKLHREF 370 380 390 400 HHGPDPTDTA PGEQAQDVAS SPPESSFQKL APSEYRYTLL RDRDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family." Anelli T., Alessio M., Mezghrani A., Simmen T., Talamo F., Bachi A., Sitia R. EMBO J. 21:835-844(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, INTERACTION WITH ERO1L AND ERO1LB, INDUCTION. Tissue: Cervix.
[2]	"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[7]	"Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44." Anelli T., Alessio M., Bachi A., Bergamelli L., Bertoli G., Camerini S., Mezghrani A., Ruffato E., Simmen T., Sitia R. EMBO J. 22:5015-5022(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Towards complete analysis of the platelet proteome." O'Neill E.E., Brock C.J., von Kriegsheim A.F., Pearce A.C., Dwek R.A., Watson S.P., Hebestreit H.F. Proteomics 2:288-305(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. Tissue: Platelet.
[9]	"Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44." Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T., Mikoshiba K. Cell 120:85-98(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ITPR1.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail." Wang L., Wang L., Vavassori S., Li S., Ke H., Anelli T., Degano M., Ronzoni R., Sitia R., Sun F., Wang C.-C. EMBO Rep. 9:642-647(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 25-406, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ344330 mRNA. Translation: CAC87611.1.
AB011145 mRNA. Translation: BAA25499.1. Different initiation.
AY359048 mRNA. Translation: AAQ89407.1.
AK075024 mRNA. Translation: BAG52054.1.
AL360084, AL137072, AL358937 Genomic DNA. Translation: CAH70308.1.
AL137072, AL358937, AL360084 Genomic DNA. Translation: CAH72172.1.
AL358937, AL137072, AL360084 Genomic DNA. Translation: CAI95319.1.
BC005374 mRNA. Translation: AAH05374.1.

IPI

IPI00401264.

RefSeq

NP_055866.1. NM_015051.1.

UniGene

Hs.154023.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2R2J	X-ray	2.60	A	30-406	[»]

ProteinModelPortal

Q9BS26.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BS26. 10 interactions.

MINT

MINT-2816102.

STRING

9606.ENSP00000262455.

Polymorphism databases

DMDM

31077035.

2D gel databases

REPRODUCTION-2DPAGE

IPI00401264.

Proteomic databases

PaxDb

Q9BS26.

PeptideAtlas

Q9BS26.

PRIDE

Q9BS26.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262455; ENSP00000262455; ENSG00000023318.

GeneID

23071.

KEGG

hsa:23071.

UCSC

uc004bam.3. human.

Organism-specific databases

CTD

23071.

GeneCards

GC09M102742.

HGNC

HGNC:18311. ERP44.

HPA

HPA001318.

MIM

609170. gene.

neXtProt

NX_Q9BS26.

PharmGKB

PA164719295.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0526.

HOGENOM

HOG000007707.

InParanoid

Q9BS26.

OMA

LFHMKDD.

OrthoDB

EOG4Z0B5R.

PhylomeDB

Q9BS26.

Gene expression databases

Bgee

Q9BS26.

CleanEx

HS_TXNDC4.

Genevestigator

Q9BS26.

GermOnline

ENSG00000023318. Homo sapiens.

Family and domain databases

Gene3D

3.40.30.10. 2 hits.

InterPro

IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]

Pfam

PF00085. Thioredoxin. 1 hit.
[Graphical view]

SUPFAM

SSF52833. Thiordxn-like_fd. 3 hits.

PROSITE

PS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ERP44. human.

EvolutionaryTrace

Q9BS26.

GenomeRNAi

23071.

NextBio

44171.

SOURCE

Search...

Entry information

Entry name

ERP44_HUMAN

Accession

Primary (citable) accession number: Q9BS26
Secondary accession number(s): O60319 , Q4VXC1, Q5VWZ7, Q6UW14, Q8WX67

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 23, 2003
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 115 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.