Full text data of SSR4
SSR4
(TRAPD)
[Confidence: high (present in two of the MS resources)]
Translocon-associated protein subunit delta; TRAP-delta (Signal sequence receptor subunit delta; SSR-delta; Flags: Precursor)
Translocon-associated protein subunit delta; TRAP-delta (Signal sequence receptor subunit delta; SSR-delta; Flags: Precursor)
hRBCD
IPI00019385
IPI00019385 Translocon-associated protein, delta subunit precursor Translocon-associated protein, delta subunit precursor membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a ER membrane n/a found at its expected molecular weight found at molecular weight
IPI00019385 Translocon-associated protein, delta subunit precursor Translocon-associated protein, delta subunit precursor membrane n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a ER membrane n/a found at its expected molecular weight found at molecular weight
UniProt
P51571
ID SSRD_HUMAN Reviewed; 173 AA.
AC P51571; A8K378; Q53XY1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Translocon-associated protein subunit delta;
DE Short=TRAP-delta;
DE AltName: Full=Signal sequence receptor subunit delta;
DE Short=SSR-delta;
DE Flags: Precursor;
GN Name=SSR4; Synonyms=TRAPD;
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].
RC TISSUE=Brain;
RX PubMed=7492314;
RA Holthuis J.C.M., van Riel M.C.H.M., Martens G.J.M.;
RT "Translocon-associated protein TRAP delta and a novel TRAP-like
RT protein are coordinately expressed with pro-opiomelanocortin in
RT Xenopus intermediate pituitary.";
RL Biochem. J. 312:205-213(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Liver, Placenta, and Spleen;
RX PubMed=9286695; DOI=10.1006/geno.1997.4822;
RA Brenner V., Nyakatura G., Rosenthal A., Platzer M.;
RT "Genomic organization of two novel genes on human Xq28: compact head
RT to head arrangement of IDH gamma and TRAP delta is conserved in rat
RT and mouse.";
RL Genomics 44:8-14(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Leukocyte, and Placenta;
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 [8]
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 [9]
RP VARIANT ARG-144.
RX PubMed=20598277; DOI=10.1016/j.ajhg.2010.06.008;
RA Sun Y., Almomani R., Aten E., Celli J., van der Heijden J.,
RA Venselaar H., Robertson S.P., Baroncini A., Franco B.,
RA Basel-Vanagaite L., Horii E., Drut R., Ariyurek Y., den Dunnen J.T.,
RA Breuning M.H.;
RT "Terminal osseous dysplasia is caused by a single recurrent mutation
RT in the FLNA gene.";
RL Am. J. Hum. Genet. 87:146-153(2010).
CC -!- FUNCTION: TRAP proteins are part of a complex whose function is to
CC bind calcium to the ER membrane and thereby regulate the retention
CC of ER resident proteins.
CC -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and
CC TRAP-gamma.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type I membrane protein.
CC -!- SIMILARITY: Belongs to the TRAP-delta family.
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DR EMBL; X90583; CAA62211.1; -; mRNA.
DR EMBL; Z68129; CAA92215.1; -; Genomic_DNA.
DR EMBL; Z69043; CAA93157.1; -; mRNA.
DR EMBL; BT007192; AAP35856.1; -; mRNA.
DR EMBL; AK290493; BAF83182.1; -; mRNA.
DR EMBL; U52111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72811.1; -; Genomic_DNA.
DR EMBL; BC003371; AAH03371.1; -; mRNA.
DR EMBL; BC032351; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S59865; S59865.
DR RefSeq; NP_001191455.1; NM_001204526.1.
DR RefSeq; NP_006271.1; NM_006280.2.
DR UniGene; Hs.409223; -.
DR ProteinModelPortal; P51571; -.
DR IntAct; P51571; 14.
DR MINT; MINT-1160772; -.
DR STRING; 9606.ENSP00000317331; -.
DR PhosphoSite; P51571; -.
DR DMDM; 1711550; -.
DR PaxDb; P51571; -.
DR PRIDE; P51571; -.
DR DNASU; 6748; -.
DR Ensembl; ENST00000320857; ENSP00000317331; ENSG00000180879.
DR Ensembl; ENST00000370086; ENSP00000359103; ENSG00000180879.
DR Ensembl; ENST00000370087; ENSP00000359104; ENSG00000180879.
DR Ensembl; ENST00000594475; ENSP00000471489; ENSG00000269520.
DR Ensembl; ENST00000599490; ENSP00000470405; ENSG00000269520.
DR Ensembl; ENST00000599757; ENSP00000473104; ENSG00000269520.
DR GeneID; 6748; -.
DR KEGG; hsa:6748; -.
DR UCSC; uc004fiv.3; human.
DR CTD; 6748; -.
DR GeneCards; GC0XP153058; -.
DR H-InvDB; HIX0016177; -.
DR HGNC; HGNC:11326; SSR4.
DR HPA; HPA045209; -.
DR MIM; 300090; gene.
DR neXtProt; NX_P51571; -.
DR PharmGKB; PA36150; -.
DR eggNOG; NOG249692; -.
DR HOGENOM; HOG000293353; -.
DR HOVERGEN; HBG002293; -.
DR InParanoid; P51571; -.
DR KO; K04571; -.
DR OMA; HRGAWNG; -.
DR PhylomeDB; P51571; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; SSR4; human.
DR GeneWiki; SSR4; -.
DR GenomeRNAi; 6748; -.
DR NextBio; 26324; -.
DR PRO; PR:P51571; -.
DR ArrayExpress; P51571; -.
DR Bgee; P51571; -.
DR CleanEx; HS_SSR4; -.
DR Genevestigator; P51571; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005784; C:Sec61 translocon complex; NAS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006412; P:translation; TAS:Reactome.
DR InterPro; IPR008855; TRAP-delta.
DR PANTHER; PTHR12731; PTHR12731; 1.
DR Pfam; PF05404; TRAP-delta; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Disulfide bond; Endoplasmic reticulum;
KW Isopeptide bond; Membrane; Polymorphism; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1 23 Potential.
FT CHAIN 24 173 Translocon-associated protein subunit
FT delta.
FT /FTId=PRO_0000033292.
FT TOPO_DOM 24 144 Lumenal (Potential).
FT TRANSMEM 145 165 Helical; (Potential).
FT TOPO_DOM 166 173 Cytoplasmic (Potential).
FT DISULFID 26 57 By similarity.
FT CROSSLNK 73 73 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VARIANT 144 144 G -> R.
FT /FTId=VAR_064161.
FT CONFLICT 109 109 E -> K (in Ref. 2).
SQ SEQUENCE 173 AA; 18999 MW; 063CD2C8F6CE368B CRC64;
MAAMASLGAL ALLLLSSLSR CSAEACLEPQ ITPSYYTTSD AVISTETVFI VEISLTCKNR
VQNMALYADV GGKQFPVTRG QDVGRYQVSW SLDHKSAHAG TYEVRFFDEE SYSLLRKAQR
NNEDISIIPP LFTVSVDHRG TWNGPWVSTE VLAAAIGLVI YYLAFSAKSH IQA
//
ID SSRD_HUMAN Reviewed; 173 AA.
AC P51571; A8K378; Q53XY1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Translocon-associated protein subunit delta;
DE Short=TRAP-delta;
DE AltName: Full=Signal sequence receptor subunit delta;
DE Short=SSR-delta;
DE Flags: Precursor;
GN Name=SSR4; Synonyms=TRAPD;
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].
RC TISSUE=Brain;
RX PubMed=7492314;
RA Holthuis J.C.M., van Riel M.C.H.M., Martens G.J.M.;
RT "Translocon-associated protein TRAP delta and a novel TRAP-like
RT protein are coordinately expressed with pro-opiomelanocortin in
RT Xenopus intermediate pituitary.";
RL Biochem. J. 312:205-213(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Liver, Placenta, and Spleen;
RX PubMed=9286695; DOI=10.1006/geno.1997.4822;
RA Brenner V., Nyakatura G., Rosenthal A., Platzer M.;
RT "Genomic organization of two novel genes on human Xq28: compact head
RT to head arrangement of IDH gamma and TRAP delta is conserved in rat
RT and mouse.";
RL Genomics 44:8-14(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Leukocyte, and Placenta;
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 [8]
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 [9]
RP VARIANT ARG-144.
RX PubMed=20598277; DOI=10.1016/j.ajhg.2010.06.008;
RA Sun Y., Almomani R., Aten E., Celli J., van der Heijden J.,
RA Venselaar H., Robertson S.P., Baroncini A., Franco B.,
RA Basel-Vanagaite L., Horii E., Drut R., Ariyurek Y., den Dunnen J.T.,
RA Breuning M.H.;
RT "Terminal osseous dysplasia is caused by a single recurrent mutation
RT in the FLNA gene.";
RL Am. J. Hum. Genet. 87:146-153(2010).
CC -!- FUNCTION: TRAP proteins are part of a complex whose function is to
CC bind calcium to the ER membrane and thereby regulate the retention
CC of ER resident proteins.
CC -!- SUBUNIT: Heterotetramer of TRAP-alpha, TRAP-beta, TRAP-delta and
CC TRAP-gamma.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass
CC type I membrane protein.
CC -!- SIMILARITY: Belongs to the TRAP-delta family.
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DR EMBL; X90583; CAA62211.1; -; mRNA.
DR EMBL; Z68129; CAA92215.1; -; Genomic_DNA.
DR EMBL; Z69043; CAA93157.1; -; mRNA.
DR EMBL; BT007192; AAP35856.1; -; mRNA.
DR EMBL; AK290493; BAF83182.1; -; mRNA.
DR EMBL; U52111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471172; EAW72811.1; -; Genomic_DNA.
DR EMBL; BC003371; AAH03371.1; -; mRNA.
DR EMBL; BC032351; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S59865; S59865.
DR RefSeq; NP_001191455.1; NM_001204526.1.
DR RefSeq; NP_006271.1; NM_006280.2.
DR UniGene; Hs.409223; -.
DR ProteinModelPortal; P51571; -.
DR IntAct; P51571; 14.
DR MINT; MINT-1160772; -.
DR STRING; 9606.ENSP00000317331; -.
DR PhosphoSite; P51571; -.
DR DMDM; 1711550; -.
DR PaxDb; P51571; -.
DR PRIDE; P51571; -.
DR DNASU; 6748; -.
DR Ensembl; ENST00000320857; ENSP00000317331; ENSG00000180879.
DR Ensembl; ENST00000370086; ENSP00000359103; ENSG00000180879.
DR Ensembl; ENST00000370087; ENSP00000359104; ENSG00000180879.
DR Ensembl; ENST00000594475; ENSP00000471489; ENSG00000269520.
DR Ensembl; ENST00000599490; ENSP00000470405; ENSG00000269520.
DR Ensembl; ENST00000599757; ENSP00000473104; ENSG00000269520.
DR GeneID; 6748; -.
DR KEGG; hsa:6748; -.
DR UCSC; uc004fiv.3; human.
DR CTD; 6748; -.
DR GeneCards; GC0XP153058; -.
DR H-InvDB; HIX0016177; -.
DR HGNC; HGNC:11326; SSR4.
DR HPA; HPA045209; -.
DR MIM; 300090; gene.
DR neXtProt; NX_P51571; -.
DR PharmGKB; PA36150; -.
DR eggNOG; NOG249692; -.
DR HOGENOM; HOG000293353; -.
DR HOVERGEN; HBG002293; -.
DR InParanoid; P51571; -.
DR KO; K04571; -.
DR OMA; HRGAWNG; -.
DR PhylomeDB; P51571; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_71; Gene Expression.
DR ChiTaRS; SSR4; human.
DR GeneWiki; SSR4; -.
DR GenomeRNAi; 6748; -.
DR NextBio; 26324; -.
DR PRO; PR:P51571; -.
DR ArrayExpress; P51571; -.
DR Bgee; P51571; -.
DR CleanEx; HS_SSR4; -.
DR Genevestigator; P51571; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005784; C:Sec61 translocon complex; NAS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006412; P:translation; TAS:Reactome.
DR InterPro; IPR008855; TRAP-delta.
DR PANTHER; PTHR12731; PTHR12731; 1.
DR Pfam; PF05404; TRAP-delta; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Disulfide bond; Endoplasmic reticulum;
KW Isopeptide bond; Membrane; Polymorphism; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT SIGNAL 1 23 Potential.
FT CHAIN 24 173 Translocon-associated protein subunit
FT delta.
FT /FTId=PRO_0000033292.
FT TOPO_DOM 24 144 Lumenal (Potential).
FT TRANSMEM 145 165 Helical; (Potential).
FT TOPO_DOM 166 173 Cytoplasmic (Potential).
FT DISULFID 26 57 By similarity.
FT CROSSLNK 73 73 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VARIANT 144 144 G -> R.
FT /FTId=VAR_064161.
FT CONFLICT 109 109 E -> K (in Ref. 2).
SQ SEQUENCE 173 AA; 18999 MW; 063CD2C8F6CE368B CRC64;
MAAMASLGAL ALLLLSSLSR CSAEACLEPQ ITPSYYTTSD AVISTETVFI VEISLTCKNR
VQNMALYADV GGKQFPVTRG QDVGRYQVSW SLDHKSAHAG TYEVRFFDEE SYSLLRKAQR
NNEDISIIPP LFTVSVDHRG TWNGPWVSTE VLAAAIGLVI YYLAFSAKSH IQA
//
MIM
300090
*RECORD*
*FIELD* NO
300090
*FIELD* TI
*300090 SIGNAL SEQUENCE RECEPTOR, DELTA; SSR4
;;TRANSLOCON-ASSOCIATED PROTEIN, DELTA SUBUNIT; TRAPD
read more*FIELD* TX
Brenner et al. (1997) described 2 novel genes that are located in the
Xq28 region, are driven by a bidirectional promoter located between
them, and encode proteins involved in unrelated biochemical pathways
located in different compartments of the cell. Translocon-associated
protein (TRAP)-delta subunit is assumed to be involved in the secretion
of proteins. The highest concentration of TRAP-delta transcripts was
observed in pancreas, where large quantities of lipases, nucleases, and
proteases are synthesized and secreted. The second gene, IDH3G (300089),
encodes the gamma subunit of the NAD(+)-dependent isocitrate
dehydrogenase, which is involved in the energy metabolism of the cell.
Correspondingly, the highest expression levels are in tissues with
increased energy turnover, like heart, skeletal muscle, and brain. IDH3G
and TRAP-delta were found to be arranged in a compact head-to-head
manner. The nontranscribed intergenic region represents only 133 bp and
is embedded in a CpG island. Brenner et al. (1997) concluded that the
CpG island functions as a bidirectional promoter to initiate the
transcription of both functionally unrelated genes with quite distinct
expression patterns. The authors showed that in rat and mouse this area
is similarly compact, representing less than 249 bp in rat and not more
than 164 bp in mouse. In both species, this intergenic region is
embedded in a CpG island and is highly conserved, with nucleotide
identity values ranging from 70.1% between human and rat to 92.6%
between mouse and rat.
*FIELD* RF
1. Brenner, V.; Nyakatura, G.; Rosenthal, A.; Platzer, M.: Genomic
organization of two novel genes on human Xq28: compact head to head
arrangement of IDH-gamma and TRAP-delta is conserved in rat and mouse. Genomics 44:
8-14, 1997.
*FIELD* CD
Victor A. McKusick: 9/26/1997
*FIELD* ED
mark: 11/04/1997
mark: 9/26/1997
*RECORD*
*FIELD* NO
300090
*FIELD* TI
*300090 SIGNAL SEQUENCE RECEPTOR, DELTA; SSR4
;;TRANSLOCON-ASSOCIATED PROTEIN, DELTA SUBUNIT; TRAPD
read more*FIELD* TX
Brenner et al. (1997) described 2 novel genes that are located in the
Xq28 region, are driven by a bidirectional promoter located between
them, and encode proteins involved in unrelated biochemical pathways
located in different compartments of the cell. Translocon-associated
protein (TRAP)-delta subunit is assumed to be involved in the secretion
of proteins. The highest concentration of TRAP-delta transcripts was
observed in pancreas, where large quantities of lipases, nucleases, and
proteases are synthesized and secreted. The second gene, IDH3G (300089),
encodes the gamma subunit of the NAD(+)-dependent isocitrate
dehydrogenase, which is involved in the energy metabolism of the cell.
Correspondingly, the highest expression levels are in tissues with
increased energy turnover, like heart, skeletal muscle, and brain. IDH3G
and TRAP-delta were found to be arranged in a compact head-to-head
manner. The nontranscribed intergenic region represents only 133 bp and
is embedded in a CpG island. Brenner et al. (1997) concluded that the
CpG island functions as a bidirectional promoter to initiate the
transcription of both functionally unrelated genes with quite distinct
expression patterns. The authors showed that in rat and mouse this area
is similarly compact, representing less than 249 bp in rat and not more
than 164 bp in mouse. In both species, this intergenic region is
embedded in a CpG island and is highly conserved, with nucleotide
identity values ranging from 70.1% between human and rat to 92.6%
between mouse and rat.
*FIELD* RF
1. Brenner, V.; Nyakatura, G.; Rosenthal, A.; Platzer, M.: Genomic
organization of two novel genes on human Xq28: compact head to head
arrangement of IDH-gamma and TRAP-delta is conserved in rat and mouse. Genomics 44:
8-14, 1997.
*FIELD* CD
Victor A. McKusick: 9/26/1997
*FIELD* ED
mark: 11/04/1997
mark: 9/26/1997