Full text data of ERP44
ERP44
(KIAA0573, TXNDC4)
[Confidence: high (present in two of the MS resources)]
Endoplasmic reticulum resident protein 44; ER protein 44; ERp44 (Thioredoxin domain-containing protein 4; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Endoplasmic reticulum resident protein 44; ER protein 44; ERp44 (Thioredoxin domain-containing protein 4; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BS26
ID ERP44_HUMAN Reviewed; 406 AA.
AC Q9BS26; O60319; Q4VXC1; Q5VWZ7; Q6UW14; Q8WX67;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Endoplasmic reticulum resident protein 44;
DE Short=ER protein 44;
DE Short=ERp44;
DE AltName: Full=Thioredoxin domain-containing protein 4;
DE Flags: Precursor;
GN Name=ERP44; Synonyms=KIAA0573, TXNDC4; ORFNames=UNQ532/PRO1075;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP INTERACTION WITH ERO1L AND ERO1LB, AND INDUCTION.
RC TISSUE=Cervix;
RX PubMed=11847130; DOI=10.1093/emboj/21.4.835;
RA Anelli T., Alessio M., Mezghrani A., Simmen T., Talamo F., Bachi A.,
RA Sitia R.;
RT "ERp44, a novel endoplasmic reticulum folding assistant of the
RT thioredoxin family.";
RL EMBO J. 21:835-844(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION.
RX PubMed=14517240; DOI=10.1093/emboj/cdg491;
RA Anelli T., Alessio M., Bachi A., Bergamelli L., Bertoli G.,
RA Camerini S., Mezghrani A., Ruffato E., Simmen T., Sitia R.;
RT "Thiol-mediated protein retention in the endoplasmic reticulum: the
RT role of ERp44.";
RL EMBO J. 22:5015-5022(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=11921445;
RX DOI=10.1002/1615-9861(200203)2:3<288::AID-PROT288>3.0.CO;2-0;
RA O'Neill E.E., Brock C.J., von Kriegsheim A.F., Pearce A.C., Dwek R.A.,
RA Watson S.P., Hebestreit H.F.;
RT "Towards complete analysis of the platelet proteome.";
RL Proteomics 2:288-305(2002).
RN [9]
RP INTERACTION WITH ITPR1.
RX PubMed=15652484; DOI=10.1016/j.cell.2004.11.048;
RA Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T.,
RA Mikoshiba K.;
RT "Subtype-specific and ER lumenal environment-dependent regulation of
RT inositol 1,4,5-trisphosphate receptor type 1 by ERp44.";
RL Cell 120:85-98(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 25-406, AND DISULFIDE BONDS.
RX PubMed=18552768; DOI=10.1038/embor.2008.88;
RA Wang L., Wang L., Vavassori S., Li S., Ke H., Anelli T., Degano M.,
RA Ronzoni R., Sitia R., Sun F., Wang C.-C.;
RT "Crystal structure of human ERp44 shows a dynamic functional
RT modulation by its carboxy-terminal tail.";
RL EMBO Rep. 9:642-647(2008).
CC -!- FUNCTION: Mediates thiol-dependent retention in the early
CC secretory pathway, forming mixed disulfides with substrate
CC proteins through its conserved CRFS motif. Inhibits the calcium
CC channel activity of ITPR1. May have a role in the control of
CC oxidative protein folding in the endoplasmic reticulum. Required
CC to retain ERO1L and ERO1LB in the endoplasmic reticulum.
CC -!- SUBUNIT: Forms mixed disulfides with both ERO1L and ERO1LB and
CC cargo folding intermediates. Directly interacts with ITPR1 in a
CC pH-, redox state- and calcium-dependent manner, but not with ITPR2
CC or ITPR3. The strength of this interaction inversely correlates
CC with calcium concentration (By similarity).
CC -!- INTERACTION:
CC P49257:LMAN1; NbExp=3; IntAct=EBI-541644, EBI-1057738;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC -!- INDUCTION: By endoplasmic reticulum stress.
CC -!- SIMILARITY: Contains 1 thioredoxin domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25499.1; Type=Erroneous initiation;
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DR EMBL; AJ344330; CAC87611.1; -; mRNA.
DR EMBL; AB011145; BAA25499.1; ALT_INIT; mRNA.
DR EMBL; AY359048; AAQ89407.1; -; mRNA.
DR EMBL; AK075024; BAG52054.1; -; mRNA.
DR EMBL; AL360084; CAH70308.1; -; Genomic_DNA.
DR EMBL; AL137072; CAH70308.1; JOINED; Genomic_DNA.
DR EMBL; AL358937; CAH70308.1; JOINED; Genomic_DNA.
DR EMBL; AL137072; CAH72172.1; -; Genomic_DNA.
DR EMBL; AL358937; CAH72172.1; JOINED; Genomic_DNA.
DR EMBL; AL360084; CAH72172.1; JOINED; Genomic_DNA.
DR EMBL; AL358937; CAI95319.1; -; Genomic_DNA.
DR EMBL; AL137072; CAI95319.1; JOINED; Genomic_DNA.
DR EMBL; AL360084; CAI95319.1; JOINED; Genomic_DNA.
DR EMBL; BC005374; AAH05374.1; -; mRNA.
DR RefSeq; NP_055866.1; NM_015051.1.
DR UniGene; Hs.154023; -.
DR PDB; 2R2J; X-ray; 2.60 A; A=30-406.
DR PDBsum; 2R2J; -.
DR ProteinModelPortal; Q9BS26; -.
DR SMR; Q9BS26; 32-401.
DR IntAct; Q9BS26; 13.
DR MINT; MINT-2816102; -.
DR STRING; 9606.ENSP00000262455; -.
DR DMDM; 31077035; -.
DR REPRODUCTION-2DPAGE; IPI00401264; -.
DR PaxDb; Q9BS26; -.
DR PeptideAtlas; Q9BS26; -.
DR PRIDE; Q9BS26; -.
DR Ensembl; ENST00000262455; ENSP00000262455; ENSG00000023318.
DR GeneID; 23071; -.
DR KEGG; hsa:23071; -.
DR UCSC; uc004bam.3; human.
DR CTD; 23071; -.
DR GeneCards; GC09M102742; -.
DR HGNC; HGNC:18311; ERP44.
DR HPA; HPA001318; -.
DR MIM; 609170; gene.
DR neXtProt; NX_Q9BS26; -.
DR PharmGKB; PA164719295; -.
DR eggNOG; COG0526; -.
DR HOGENOM; HOG000007707; -.
DR InParanoid; Q9BS26; -.
DR KO; K17264; -.
DR OMA; RHMYLFP; -.
DR OrthoDB; EOG718KCX; -.
DR PhylomeDB; Q9BS26; -.
DR ChiTaRS; ERP44; human.
DR EvolutionaryTrace; Q9BS26; -.
DR GeneWiki; ERP44; -.
DR GenomeRNAi; 23071; -.
DR NextBio; 44171; -.
DR PRO; PR:Q9BS26; -.
DR Bgee; Q9BS26; -.
DR CleanEx; HS_TXNDC4; -.
DR Genevestigator; Q9BS26; -.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; TAS:UniProtKB.
DR GO; GO:0009100; P:glycoprotein metabolic process; IDA:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IDA:UniProtKB.
DR Gene3D; 3.40.30.10; -; 2.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 3.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Reference proteome; Signal;
KW Stress response.
FT SIGNAL 1 29
FT CHAIN 30 406 Endoplasmic reticulum resident protein
FT 44.
FT /FTId=PRO_0000034180.
FT DOMAIN 30 138 Thioredoxin.
FT REGION 236 285 Interaction with ITPR1 (By similarity).
FT MOTIF 403 406 Prevents secretion from ER (Potential).
FT DISULFID 189 241
FT DISULFID 301 318
FT CONFLICT 35 35 D -> A (in Ref. 3; AAQ89407).
FT TURN 36 38
FT HELIX 39 45
FT STRAND 47 54
FT HELIX 59 75
FT STRAND 85 91
FT TURN 92 94
FT HELIX 96 101
FT STRAND 106 114
FT STRAND 117 122
FT HELIX 129 140
FT STRAND 145 147
FT STRAND 162 168
FT STRAND 170 172
FT HELIX 173 185
FT TURN 186 188
FT STRAND 190 196
FT STRAND 208 212
FT STRAND 214 218
FT HELIX 230 241
FT STRAND 244 247
FT HELIX 250 257
FT STRAND 263 268
FT HELIX 274 286
FT HELIX 288 290
FT TURN 291 293
FT STRAND 294 300
FT TURN 301 304
FT HELIX 305 310
FT HELIX 315 317
FT STRAND 319 324
FT STRAND 329 331
FT HELIX 336 339
FT HELIX 343 353
FT HELIX 387 390
FT TURN 394 396
SQ SEQUENCE 406 AA; 46971 MW; 3865DCF3811BC263 CRC64;
MHPAVFLSLP DLRCSLLLLV TWVFTPVTTE ITSLDTENID EILNNADVAL VNFYADWCRF
SQMLHPIFEE ASDVIKEEFP NENQVVFARV DCDQHSDIAQ RYRISKYPTL KLFRNGMMMK
REYRGQRSVK ALADYIRQQK SDPIQEIRDL AEITTLDRSK RNIIGYFEQK DSDNYRVFER
VANILHDDCA FLSAFGDVSK PERYSGDNII YKPPGHSAPD MVYLGAMTNF DVTYNWIQDK
CVPLVREITF ENGEELTEEG LPFLILFHMK EDTESLEIFQ NEVARQLISE KGTINFLHAD
CDKFRHPLLH IQKTPADCPV IAIDSFRHMY VFGDFKDVLI PGKLKQFVFD LHSGKLHREF
HHGPDPTDTA PGEQAQDVAS SPPESSFQKL APSEYRYTLL RDRDEL
//
ID ERP44_HUMAN Reviewed; 406 AA.
AC Q9BS26; O60319; Q4VXC1; Q5VWZ7; Q6UW14; Q8WX67;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=Endoplasmic reticulum resident protein 44;
DE Short=ER protein 44;
DE Short=ERp44;
DE AltName: Full=Thioredoxin domain-containing protein 4;
DE Flags: Precursor;
GN Name=ERP44; Synonyms=KIAA0573, TXNDC4; ORFNames=UNQ532/PRO1075;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP INTERACTION WITH ERO1L AND ERO1LB, AND INDUCTION.
RC TISSUE=Cervix;
RX PubMed=11847130; DOI=10.1093/emboj/21.4.835;
RA Anelli T., Alessio M., Mezghrani A., Simmen T., Talamo F., Bachi A.,
RA Sitia R.;
RT "ERp44, a novel endoplasmic reticulum folding assistant of the
RT thioredoxin family.";
RL EMBO J. 21:835-844(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
RA Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale
RT effort to identify novel human secreted and transmembrane proteins: a
RT bioinformatics assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION.
RX PubMed=14517240; DOI=10.1093/emboj/cdg491;
RA Anelli T., Alessio M., Bachi A., Bergamelli L., Bertoli G.,
RA Camerini S., Mezghrani A., Ruffato E., Simmen T., Sitia R.;
RT "Thiol-mediated protein retention in the endoplasmic reticulum: the
RT role of ERp44.";
RL EMBO J. 22:5015-5022(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=11921445;
RX DOI=10.1002/1615-9861(200203)2:3<288::AID-PROT288>3.0.CO;2-0;
RA O'Neill E.E., Brock C.J., von Kriegsheim A.F., Pearce A.C., Dwek R.A.,
RA Watson S.P., Hebestreit H.F.;
RT "Towards complete analysis of the platelet proteome.";
RL Proteomics 2:288-305(2002).
RN [9]
RP INTERACTION WITH ITPR1.
RX PubMed=15652484; DOI=10.1016/j.cell.2004.11.048;
RA Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T.,
RA Mikoshiba K.;
RT "Subtype-specific and ER lumenal environment-dependent regulation of
RT inositol 1,4,5-trisphosphate receptor type 1 by ERp44.";
RL Cell 120:85-98(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 25-406, AND DISULFIDE BONDS.
RX PubMed=18552768; DOI=10.1038/embor.2008.88;
RA Wang L., Wang L., Vavassori S., Li S., Ke H., Anelli T., Degano M.,
RA Ronzoni R., Sitia R., Sun F., Wang C.-C.;
RT "Crystal structure of human ERp44 shows a dynamic functional
RT modulation by its carboxy-terminal tail.";
RL EMBO Rep. 9:642-647(2008).
CC -!- FUNCTION: Mediates thiol-dependent retention in the early
CC secretory pathway, forming mixed disulfides with substrate
CC proteins through its conserved CRFS motif. Inhibits the calcium
CC channel activity of ITPR1. May have a role in the control of
CC oxidative protein folding in the endoplasmic reticulum. Required
CC to retain ERO1L and ERO1LB in the endoplasmic reticulum.
CC -!- SUBUNIT: Forms mixed disulfides with both ERO1L and ERO1LB and
CC cargo folding intermediates. Directly interacts with ITPR1 in a
CC pH-, redox state- and calcium-dependent manner, but not with ITPR2
CC or ITPR3. The strength of this interaction inversely correlates
CC with calcium concentration (By similarity).
CC -!- INTERACTION:
CC P49257:LMAN1; NbExp=3; IntAct=EBI-541644, EBI-1057738;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
CC -!- INDUCTION: By endoplasmic reticulum stress.
CC -!- SIMILARITY: Contains 1 thioredoxin domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25499.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; AJ344330; CAC87611.1; -; mRNA.
DR EMBL; AB011145; BAA25499.1; ALT_INIT; mRNA.
DR EMBL; AY359048; AAQ89407.1; -; mRNA.
DR EMBL; AK075024; BAG52054.1; -; mRNA.
DR EMBL; AL360084; CAH70308.1; -; Genomic_DNA.
DR EMBL; AL137072; CAH70308.1; JOINED; Genomic_DNA.
DR EMBL; AL358937; CAH70308.1; JOINED; Genomic_DNA.
DR EMBL; AL137072; CAH72172.1; -; Genomic_DNA.
DR EMBL; AL358937; CAH72172.1; JOINED; Genomic_DNA.
DR EMBL; AL360084; CAH72172.1; JOINED; Genomic_DNA.
DR EMBL; AL358937; CAI95319.1; -; Genomic_DNA.
DR EMBL; AL137072; CAI95319.1; JOINED; Genomic_DNA.
DR EMBL; AL360084; CAI95319.1; JOINED; Genomic_DNA.
DR EMBL; BC005374; AAH05374.1; -; mRNA.
DR RefSeq; NP_055866.1; NM_015051.1.
DR UniGene; Hs.154023; -.
DR PDB; 2R2J; X-ray; 2.60 A; A=30-406.
DR PDBsum; 2R2J; -.
DR ProteinModelPortal; Q9BS26; -.
DR SMR; Q9BS26; 32-401.
DR IntAct; Q9BS26; 13.
DR MINT; MINT-2816102; -.
DR STRING; 9606.ENSP00000262455; -.
DR DMDM; 31077035; -.
DR REPRODUCTION-2DPAGE; IPI00401264; -.
DR PaxDb; Q9BS26; -.
DR PeptideAtlas; Q9BS26; -.
DR PRIDE; Q9BS26; -.
DR Ensembl; ENST00000262455; ENSP00000262455; ENSG00000023318.
DR GeneID; 23071; -.
DR KEGG; hsa:23071; -.
DR UCSC; uc004bam.3; human.
DR CTD; 23071; -.
DR GeneCards; GC09M102742; -.
DR HGNC; HGNC:18311; ERP44.
DR HPA; HPA001318; -.
DR MIM; 609170; gene.
DR neXtProt; NX_Q9BS26; -.
DR PharmGKB; PA164719295; -.
DR eggNOG; COG0526; -.
DR HOGENOM; HOG000007707; -.
DR InParanoid; Q9BS26; -.
DR KO; K17264; -.
DR OMA; RHMYLFP; -.
DR OrthoDB; EOG718KCX; -.
DR PhylomeDB; Q9BS26; -.
DR ChiTaRS; ERP44; human.
DR EvolutionaryTrace; Q9BS26; -.
DR GeneWiki; ERP44; -.
DR GenomeRNAi; 23071; -.
DR NextBio; 44171; -.
DR PRO; PR:Q9BS26; -.
DR Bgee; Q9BS26; -.
DR CleanEx; HS_TXNDC4; -.
DR Genevestigator; Q9BS26; -.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA:UniProtKB.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IDA:UniProtKB.
DR GO; GO:0045454; P:cell redox homeostasis; TAS:UniProtKB.
DR GO; GO:0009100; P:glycoprotein metabolic process; IDA:UniProtKB.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IDA:UniProtKB.
DR Gene3D; 3.40.30.10; -; 2.
DR InterPro; IPR012336; Thioredoxin-like_fold.
DR InterPro; IPR013766; Thioredoxin_domain.
DR Pfam; PF00085; Thioredoxin; 1.
DR SUPFAM; SSF52833; SSF52833; 3.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Endoplasmic reticulum; Reference proteome; Signal;
KW Stress response.
FT SIGNAL 1 29
FT CHAIN 30 406 Endoplasmic reticulum resident protein
FT 44.
FT /FTId=PRO_0000034180.
FT DOMAIN 30 138 Thioredoxin.
FT REGION 236 285 Interaction with ITPR1 (By similarity).
FT MOTIF 403 406 Prevents secretion from ER (Potential).
FT DISULFID 189 241
FT DISULFID 301 318
FT CONFLICT 35 35 D -> A (in Ref. 3; AAQ89407).
FT TURN 36 38
FT HELIX 39 45
FT STRAND 47 54
FT HELIX 59 75
FT STRAND 85 91
FT TURN 92 94
FT HELIX 96 101
FT STRAND 106 114
FT STRAND 117 122
FT HELIX 129 140
FT STRAND 145 147
FT STRAND 162 168
FT STRAND 170 172
FT HELIX 173 185
FT TURN 186 188
FT STRAND 190 196
FT STRAND 208 212
FT STRAND 214 218
FT HELIX 230 241
FT STRAND 244 247
FT HELIX 250 257
FT STRAND 263 268
FT HELIX 274 286
FT HELIX 288 290
FT TURN 291 293
FT STRAND 294 300
FT TURN 301 304
FT HELIX 305 310
FT HELIX 315 317
FT STRAND 319 324
FT STRAND 329 331
FT HELIX 336 339
FT HELIX 343 353
FT HELIX 387 390
FT TURN 394 396
SQ SEQUENCE 406 AA; 46971 MW; 3865DCF3811BC263 CRC64;
MHPAVFLSLP DLRCSLLLLV TWVFTPVTTE ITSLDTENID EILNNADVAL VNFYADWCRF
SQMLHPIFEE ASDVIKEEFP NENQVVFARV DCDQHSDIAQ RYRISKYPTL KLFRNGMMMK
REYRGQRSVK ALADYIRQQK SDPIQEIRDL AEITTLDRSK RNIIGYFEQK DSDNYRVFER
VANILHDDCA FLSAFGDVSK PERYSGDNII YKPPGHSAPD MVYLGAMTNF DVTYNWIQDK
CVPLVREITF ENGEELTEEG LPFLILFHMK EDTESLEIFQ NEVARQLISE KGTINFLHAD
CDKFRHPLLH IQKTPADCPV IAIDSFRHMY VFGDFKDVLI PGKLKQFVFD LHSGKLHREF
HHGPDPTDTA PGEQAQDVAS SPPESSFQKL APSEYRYTLL RDRDEL
//
MIM
609170
*RECORD*
*FIELD* NO
609170
*FIELD* TI
*609170 THIOREDOXIN DOMAIN-CONTAINING PROTEIN 4; TXNDC4
;;ENDOPLASMIC RETICULUM RESIDENT PROTEIN, 44-KD; ERp44;;
read moreKIAA0573
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated human brain cDNA
library, Nagase et al. (1998) cloned TXNDC4, which they designated
KIAA0573. The transcript contains a repetitive element in the 3-prime
UTR, and the deduced 451-amino acid protein has an apparent molecular
mass of 50 kD, as estimated by SDS-PAGE. KIAA0573 shares weak homology
with barley protein disulfide isomerase precursor. RT-PCR detected
robust expression in all tissues examined.
By peptide sequencing of proteins immunoprecipitated with ERO1L-alpha
(ERO1L; 615435) following its overexpression in HeLa cells, followed by
database analysis and screening HeLa and neuroblastoma cell line cDNA
libraries, Anelli et al. (2002) obtained a full-length cDNA encoding
TXNDC4, which they called ERp44. The deduced 436-amino acid protein has
an N-terminal endoplasmic reticulum (ER) targeting signal sequence.
After cleavage, the calculated molecular mass of ERp44 is 43.9 kD. ERp44
also contains a thioredoxin (187700)-like domain, which includes a CRFS
motif; a calsequestrin (114250)-like domain; and a C-terminal ER
retention signal (RDEL). The CRFS motif is present in mouse, fly, and
nematode ERp44 homologs.
GENE FUNCTION
Anelli et al. (2002) found that ERp44 formed mixed disulfides with
proteins involved in oxidative protein folding in the ER, including
ERO1L-alpha and ERO1L-beta (ERO1LB; 615437), and with cargo folding
intermediates. While the interaction with transport-competent IgK chains
(147200) was transient, ERp44 bound more stably with IgJ chains
(147790), which are retained in the ER and are eventually degraded by
proteasomes. ERp44 did not bind a short-lived ribophorin (see 180470)
mutant lacking cysteines. Overexpression of ERp44 altered the
equilibrium of different ERO1L-alpha isoforms, suggesting that ERp44 may
be involved in control of oxidative protein folding.
Higo et al. (2005) found that ERp44 interacted directly with the third
luminal loop of inositol 1,4,5-trisphosphate receptor type 1 (IP3R1;
147265). The interaction was dependent on pH, Ca(2+) concentration, and
redox state, with the presence of free cysteine residues in the loop of
IP3R1 required. Ca(2+)-imaging experiments and single-channel recording
of IP3R1 activity with a planar lipid bilayer system demonstrated that
IP3R1 was directly inhibited by ERp44. Higo et al. (2005) concluded that
ERp44 senses the environment in the ER lumen and modulates IP3R1
activity accordingly, which in turn contributes to regulating both
intraluminal conditions and the complex patterns of cytosolic Ca(2+)
concentrations.
GENE STRUCTURE
Anelli et al. (2002) determined that the TXNDC4 gene contains 12 exons.
MAPPING
By radiation hybrid analysis, Nagase et al. (1998) mapped the TXNDC4
gene to chromosome 9. Anelli et al. (2002) mapped the TXNDC4 gene to
chromosome 9q22-q32 by genomic sequence analysis.
*FIELD* RF
1. Anelli, T.; Alessio, M.; Mezghrani, A.; Simmen, T.; Talamo, F.;
Bachi, A.; Sitia, R.: ERp44, a novel endoplasmic reticulum folding
assistant of the thioredoxin family. EMBO J. 21: 835-844, 2002.
2. Higo, T.; Hattori, M.; Nakamura, T.; Natsume, T.; Michikawa, T.;
Mikoshiba, K.: Subtype-specific and ER lumenal environment-dependent
regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44. Cell 120:
85-98, 2005.
3. Nagase, T.; Ishikawa, K.; Miyajima, N.; Tanaka, A.; Kotani, H.;
Nomura, N.; Ohara, O.: 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. DNA Res. 5: 31-39,
1998.
*FIELD* CN
Patricia A. Hartz - updated: 2/11/2005
*FIELD* CD
Stylianos E. Antonarakis: 1/24/2005
*FIELD* ED
mgross: 09/27/2013
mgross: 9/26/2013
terry: 7/26/2006
mgross: 2/11/2005
mgross: 1/24/2005
*RECORD*
*FIELD* NO
609170
*FIELD* TI
*609170 THIOREDOXIN DOMAIN-CONTAINING PROTEIN 4; TXNDC4
;;ENDOPLASMIC RETICULUM RESIDENT PROTEIN, 44-KD; ERp44;;
read moreKIAA0573
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated human brain cDNA
library, Nagase et al. (1998) cloned TXNDC4, which they designated
KIAA0573. The transcript contains a repetitive element in the 3-prime
UTR, and the deduced 451-amino acid protein has an apparent molecular
mass of 50 kD, as estimated by SDS-PAGE. KIAA0573 shares weak homology
with barley protein disulfide isomerase precursor. RT-PCR detected
robust expression in all tissues examined.
By peptide sequencing of proteins immunoprecipitated with ERO1L-alpha
(ERO1L; 615435) following its overexpression in HeLa cells, followed by
database analysis and screening HeLa and neuroblastoma cell line cDNA
libraries, Anelli et al. (2002) obtained a full-length cDNA encoding
TXNDC4, which they called ERp44. The deduced 436-amino acid protein has
an N-terminal endoplasmic reticulum (ER) targeting signal sequence.
After cleavage, the calculated molecular mass of ERp44 is 43.9 kD. ERp44
also contains a thioredoxin (187700)-like domain, which includes a CRFS
motif; a calsequestrin (114250)-like domain; and a C-terminal ER
retention signal (RDEL). The CRFS motif is present in mouse, fly, and
nematode ERp44 homologs.
GENE FUNCTION
Anelli et al. (2002) found that ERp44 formed mixed disulfides with
proteins involved in oxidative protein folding in the ER, including
ERO1L-alpha and ERO1L-beta (ERO1LB; 615437), and with cargo folding
intermediates. While the interaction with transport-competent IgK chains
(147200) was transient, ERp44 bound more stably with IgJ chains
(147790), which are retained in the ER and are eventually degraded by
proteasomes. ERp44 did not bind a short-lived ribophorin (see 180470)
mutant lacking cysteines. Overexpression of ERp44 altered the
equilibrium of different ERO1L-alpha isoforms, suggesting that ERp44 may
be involved in control of oxidative protein folding.
Higo et al. (2005) found that ERp44 interacted directly with the third
luminal loop of inositol 1,4,5-trisphosphate receptor type 1 (IP3R1;
147265). The interaction was dependent on pH, Ca(2+) concentration, and
redox state, with the presence of free cysteine residues in the loop of
IP3R1 required. Ca(2+)-imaging experiments and single-channel recording
of IP3R1 activity with a planar lipid bilayer system demonstrated that
IP3R1 was directly inhibited by ERp44. Higo et al. (2005) concluded that
ERp44 senses the environment in the ER lumen and modulates IP3R1
activity accordingly, which in turn contributes to regulating both
intraluminal conditions and the complex patterns of cytosolic Ca(2+)
concentrations.
GENE STRUCTURE
Anelli et al. (2002) determined that the TXNDC4 gene contains 12 exons.
MAPPING
By radiation hybrid analysis, Nagase et al. (1998) mapped the TXNDC4
gene to chromosome 9. Anelli et al. (2002) mapped the TXNDC4 gene to
chromosome 9q22-q32 by genomic sequence analysis.
*FIELD* RF
1. Anelli, T.; Alessio, M.; Mezghrani, A.; Simmen, T.; Talamo, F.;
Bachi, A.; Sitia, R.: ERp44, a novel endoplasmic reticulum folding
assistant of the thioredoxin family. EMBO J. 21: 835-844, 2002.
2. Higo, T.; Hattori, M.; Nakamura, T.; Natsume, T.; Michikawa, T.;
Mikoshiba, K.: Subtype-specific and ER lumenal environment-dependent
regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44. Cell 120:
85-98, 2005.
3. Nagase, T.; Ishikawa, K.; Miyajima, N.; Tanaka, A.; Kotani, H.;
Nomura, N.; Ohara, O.: 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. DNA Res. 5: 31-39,
1998.
*FIELD* CN
Patricia A. Hartz - updated: 2/11/2005
*FIELD* CD
Stylianos E. Antonarakis: 1/24/2005
*FIELD* ED
mgross: 09/27/2013
mgross: 9/26/2013
terry: 7/26/2006
mgross: 2/11/2005
mgross: 1/24/2005