DRS2/YAL026C Protein Information

Standard Name	Drs2p 1
Systematic Name	Yal026cp
Alias	Fun38p , Swa3p
ORF Classification	Verified
Description	Aminophospholipid translocase (flippase) that maintains membrane lipid asymmetry in post-Golgi secretory vesicles; contributes to clathrin-coated vesicle formation and endocytosis; mutations in human homolog ATP8B1 result in liver disease (2, 3, 4, 5, 6, 7)
Name Description	Deficiency of Ribosomal Subunits 1

Experimental Data
Molecules/cell	606 8

Predicted Sequence	Formatted Sequence or sequence in FASTA format
Length (a.a.)	1,355
Molecular Weight (Da)	153,764
Isoelectric Point (pI)	5.14

Click on image for expanded interactive view

Post-translational Modifications	PhosphoGRID \| PhosphoPep Database
Domains/motifs	See the graphical view and list of proteins that share domains/motifs in common with Drs2p (InterPro)
Transmembrane Domains	There are 9 total predicted transmembrane domains (TMHMM)
Physical Interactions	There are 49 total physical interactions (BioGRID)
Homologs	PDB Homologs \| BLASTP \| BLASTP v. fungi \| Fungal Alignment \| Synteny Viewer
External Sequence Databases	EBI: UPI0001F7BD26 \| P39524 MIPS: YAL026C NCBI: 171114 \| 330443374 \| 341940251 \| 595560 \| 728905 \| NP_009376.2 \| NM_001178171.2 GenBank/EMBL/DDBJ: DAA06962.2 \| L01795 \| U12980
External Classifications	EC: 3.6.3.1 [Phospholipid-translocating ATPase] TC: 3.A.3.8 [The Aminophospholipid-ATPase (PLA) Family]

Amino Acid Sequence (or in FASTA format)
1 MNDDRETPPK RKPGEDDTLF DIDFLDDTTS HSGSRSKVTN SHANANYIPP 51 SHVLPEETID LDADDDNIEN DVHENLFMSN NHDDQTSWNA NRFDSDAYQP 101 QSLRAVKPPG LFARFGNGLK NAFTFKRKKG PESFEMNHYN AVTNNELDDN 151 YLDSRNKFNI KILFNRYILR KNVGDAEGNG EPRVIHINDS LANSSFGYSD 201 NHISTTKYNF ATFLPKFLFQ EFSKYANLFF LCTSAIQQVP HVSPTNRYTT 251 IGTLLVVLIV SAMKECIEDI KRANSDKELN NSTAEIFSEA HDDFVEKRWI 301 DIRVGDIIRV KSEEPIPADT IILSSSEPEG LCYIETANLD GETNLKIKQS 351 RVETAKFIDV KTLKNMNGKV VSEQPNSSLY TYEGTMTLND RQIPLSPDQM 401 ILRGATLRNT AWIFGLVIFT GHETKLLRNA TATPIKRTAV EKIINRQIIA 451 LFTVLIVLIL ISSIGNVIMS TADAKHLSYL YLEGTNKAGL FFKDFLTFWI 501 LFSNLVPISL FVTVELIKYY QAFMIGSDLD LYYEKTDTPT VVRTSSLVEE 551 LGQIEYIFSD KTGTLTRNIM EFKSCSIAGH CYIDKIPEDK TATVEDGIEV 601 GYRKFDDLKK KLNDPSDEDS PIINDFLTLL ATCHTVIPEF QSDGSIKYQA 651 ASPDEGALVQ GGADLGYKFI IRKPNSVTVL LEETGEEKEY QLLNICEFNS 701 TRKRMSAIFR FPDGSIKLFC KGADTVILER LDDEANQYVE ATMRHLEDYA 751 SEGLRTLCLA MRDISEGEYE EWNSIYNEAA TTLDNRAEKL DEAANLIEKN 801 LILIGATAIE DKLQDGVPET IHTLQEAGIK IWVLTGDRQE TAINIGMSCR 851 LLSEDMNLLI INEETRDDTE RNLLEKINAL NEHQLSTHDM NTLALVIDGK 901 SLGFALEPEL EDYLLTVAKL CKAVICCRVS PLQKALVVKM VKRKSSSLLL 951 AIGDGANDVS MIQAAHVGVG ISGMEGMQAA RSADIAVGQF KFLKKLLLVH 1001 GSWSYQRISV AILYSFYKNT ALYMTQFWYV FANAFSGQSI MESWTMSFYN 1051 LFFTVWPPFV IGVFDQFVSS RLLERYPQLY KLGQKGQFFS VYIFWGWIIN 1101 GFFHSAIVFI GTILIYRYGF ALNMHGELAD HWSWGVTVYT TSVIIVLGKA 1151 ALVTNQWTKF TLIAIPGSLL FWLIFFPIYA SIFPHANISR EYYGVVKHTY 1201 GSGVFWLTLI VLPIFALVRD FLWKYYKRMY EPETYHVIQE MQKYNISDSR 1251 PHVQQFQNAI RKVRQVQRMK KQRGFAFSQA EEGGQEKIVR MYDTTQKRGK 1301 YGELQDASAN PFNDNNGLGS NDFESAEPFI ENPFADGNQN SNRFSSSRDD 1351 ISFDI*

Amino Acid Sequence (or in FASTA format)

       1  MNDDRETPPK RKPGEDDTLF DIDFLDDTTS HSGSRSKVTN SHANANYIPP
      51  SHVLPEETID LDADDDNIEN DVHENLFMSN NHDDQTSWNA NRFDSDAYQP
     101  QSLRAVKPPG LFARFGNGLK NAFTFKRKKG PESFEMNHYN AVTNNELDDN
     151  YLDSRNKFNI KILFNRYILR KNVGDAEGNG EPRVIHINDS LANSSFGYSD
     201  NHISTTKYNF ATFLPKFLFQ EFSKYANLFF LCTSAIQQVP HVSPTNRYTT
     251  IGTLLVVLIV SAMKECIEDI KRANSDKELN NSTAEIFSEA HDDFVEKRWI
     301  DIRVGDIIRV KSEEPIPADT IILSSSEPEG LCYIETANLD GETNLKIKQS
     351  RVETAKFIDV KTLKNMNGKV VSEQPNSSLY TYEGTMTLND RQIPLSPDQM
     401  ILRGATLRNT AWIFGLVIFT GHETKLLRNA TATPIKRTAV EKIINRQIIA
     451  LFTVLIVLIL ISSIGNVIMS TADAKHLSYL YLEGTNKAGL FFKDFLTFWI
     501  LFSNLVPISL FVTVELIKYY QAFMIGSDLD LYYEKTDTPT VVRTSSLVEE
     551  LGQIEYIFSD KTGTLTRNIM EFKSCSIAGH CYIDKIPEDK TATVEDGIEV
     601  GYRKFDDLKK KLNDPSDEDS PIINDFLTLL ATCHTVIPEF QSDGSIKYQA
     651  ASPDEGALVQ GGADLGYKFI IRKPNSVTVL LEETGEEKEY QLLNICEFNS
     701  TRKRMSAIFR FPDGSIKLFC KGADTVILER LDDEANQYVE ATMRHLEDYA
     751  SEGLRTLCLA MRDISEGEYE EWNSIYNEAA TTLDNRAEKL DEAANLIEKN
     801  LILIGATAIE DKLQDGVPET IHTLQEAGIK IWVLTGDRQE TAINIGMSCR
     851  LLSEDMNLLI INEETRDDTE RNLLEKINAL NEHQLSTHDM NTLALVIDGK
     901  SLGFALEPEL EDYLLTVAKL CKAVICCRVS PLQKALVVKM VKRKSSSLLL
     951  AIGDGANDVS MIQAAHVGVG ISGMEGMQAA RSADIAVGQF KFLKKLLLVH
    1001  GSWSYQRISV AILYSFYKNT ALYMTQFWYV FANAFSGQSI MESWTMSFYN
    1051  LFFTVWPPFV IGVFDQFVSS RLLERYPQLY KLGQKGQFFS VYIFWGWIIN
    1101  GFFHSAIVFI GTILIYRYGF ALNMHGELAD HWSWGVTVYT TSVIIVLGKA
    1151  ALVTNQWTKF TLIAIPGSLL FWLIFFPIYA SIFPHANISR EYYGVVKHTY
    1201  GSGVFWLTLI VLPIFALVRD FLWKYYKRMY EPETYHVIQE MQKYNISDSR
    1251  PHVQQFQNAI RKVRQVQRMK KQRGFAFSQA EEGGQEKIVR MYDTTQKRGK
    1301  YGELQDASAN PFNDNNGLGS NDFESAEPFI ENPFADGNQN SNRFSSSRDD
    1351  ISFDI*

external links for Drs2p

Homologs	Interaction Resources	Protein databases/Other	Localization Resources
BLASTP (NCBI)	BioGRID	SCOP Superfamily	Organelle DB
Ashbya (AGD)	BOND	GPMdb (Mass Spec.)	YPL+
Aspergillus (AspGD)	BioPIXIE	MIPS	YeastGFP
Candida (CGD)	CYC2008 (complexes)	Pfam domains	YeastRC Public Image Repository
Candida (CandidaDB)	Complexome	TCDB
YGOB	DIP	YeastRC Structure Prediction (Seattle)
YOGY	GeneMANIA

References cited on this page View Complete Literature Guide for Drs2p

1)	Ripmaster TL, et al. (1993) DRS1 to DRS7, novel genes required for ribosome assembly and function in Saccharomyces cerevisiae. Mol Cell Biol 13(12):7901-12
2)	Chen CY, et al. (1999) Role for Drs2p, a P-type ATPase and potential aminophospholipid translocase, in yeast late Golgi function. J Cell Biol 147(6):1223-36
3)	Gall WE, et al. (2002) Drs2p-dependent formation of exocytic clathrin-coated vesicles in vivo. Curr Biol 12(18):1623-7
4)	Pomorski T, et al. (2003) Drs2p-related P-type ATPases Dnf1p and Dnf2p are required for phospholipid translocation across the yeast plasma membrane and serve a role in endocytosis. Mol Biol Cell 14(3):1240-54
5)	Natarajan P, et al. (2004) Drs2p-coupled aminophospholipid translocase activity in yeast Golgi membranes and relationship to in vivo function. Proc Natl Acad Sci U S A 101(29):10614-9
6)	Alder-Baerens N, et al. (2006) Loss of P4 ATPases Drs2p and Dnf3p disrupts aminophospholipid transport and asymmetry in yeast post-Golgi secretory vesicles. Mol Biol Cell 17(4):1632-42
7)	Bull LN, et al. (1998) A gene encoding a P-type ATPase mutated in two forms of hereditary cholestasis. Nat Genet 18(3):219-24
8)	Ghaemmaghami S, et al. (2003) Global analysis of protein expression in yeast. Nature 425(6959):737-41