USA1_YEAST » U1 SNP1-associating protein 1

USA1_YEAST » U1 SNP1-associating protein 1
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Topology in Endoplasmic reticulum membrane
Topologylumenal side
cytoplasmic side
USA1_YEAST » U1 SNP1-associating protein 1 »
Hydrophobic Thickness 27.8 ± 3.6 Å
Tilt Angle 23 ± 5°
ΔGtransfer -19.9 kcal/mol
ΔGfold -8.4 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING
Topology In
TM Segments 564-582 (564-587)
Pathways none
PDB none
OPM none
Complexes none
Interactions none
Domains none
UniProt annotation for USA1_YEAST » U1 SNP1-associating protein 1
FUNCTION: Scaffold protein of the endoplasmic reticulum-associated degradation (ERAD) (also known as endoplasmic reticulum quality control, ERQC) pathway involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD- M). Has multiple functions in ERAD including recruitment of DER1 to the HRD1 ubiquitin ligase, and regulation of HRD1 activity. Involved in oligomerization of HRD1, which is required for ERAD-L, and in HRD1 autoubiquitination and degradation.
UniProt features for USA1_YEAST » U1 SNP1-associating protein 1
CHAIN 1 838 U1 SNP1-associating protein 1.

DOMAIN 259 318 Ubiquitin-like.

REGION 31 240 Required for ERAD-L function.

REGION 319 418 Important for HRD1 oligomer formation.

REGION 345 535 Interaction with HRD1.

REGION 437 490 Required for ERAD-L function and HRD1 oligomer formation.

REGION 584 838 Interaction with DER1.

Amino Acid Sequence for USA1_YEAST » U1 SNP1-associating protein 1
MSEYLAQTPC KFTIWSSEID LIRTNLLVNA HPLSTVGRLL QYIHYQIYKQ LRAIYQPEEQ CTNSEIPHTP LNSINTYFLS YEGRELSATC LLKDITSSSH PDSNHFIRLQ LEKRTSPSGS AFDLEYDMEG EFNSMNIQFE INTLSSQRIF NSMEPNLPIG TTLARLEKLA LERIKDFEKS AGNLCGIKED HSVSDLQGFI IKGKQTPMFL NYGSDSDYYK DLNLVDLIGI DFAPAHNSFF TFLFKMNHEQ NSHIANDEER FVLEFISDAT LSITQMNVKP DTTVKQVKDF ICSVYTHSLN LRRNDIKLIY KGQLLHENNF AGNSSKISEY IKEPHEVKVH VQINQEYTES GPGFWNEVFN NPNIFQFMPP DTRSQSPVSF APTQGRSPAA IRGEERGIPY VTESGNDIVP TDELYRKCII NGDEVVFIPV SELNPQSSYL SVIKGDYGEI KIPISSNDYR INGDNILLSP SAIEQLESAL NFKIERPRDS TLLHPSGEHV RAADNTSSAN DNNTVENDES AWNRRVVRPL RNSFPLLLVL IRTFYLIGYN SLVPFFIILE FGSFLPWKYI ILLSLLFIFR TVWNTQEVWN LWRDYLHLNE IDEVKFSQIK EFINSNSLTL NFYKKCKDTQ SAIDLLMIPN LHEQRLSVYS KYDIEYDTNT PDVGQLNLLF IKVLSGEIPK DALDELFKEF FELYETTRNM NTLYPQDSLN ELLLMIWKES QKKDINTLPK YRRWFQTLCS QIAEHNVLDV VLRYIIPDPV NDRVITAVIK NFVLFWVTLL PYVKEKLDDI VAQRARDREQ PAPSAQQQEN EDEALIIPDE EEPTATGAQP HLYIPDED