Q9VL32 (SUR_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-binding cassette sub-family C member Sur

Alternative name(s):
Sulfonylurea receptor
Short name=Dsur

Gene names

Name:	Sur
ORF Names:	CG5772

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	2171 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May function as regulatory subunit of ATP-sensitive potassium channels (KATP) and form KATP channels with a member of the ATP-sensitive inward rectifier potassium channel family By similarity. May also have channel activity by itself (in vitro). May protect the heart during hypoxia. May protect against heart failure under conditions of tachycardic stress. Ref.1 Ref.4 Ref.5
Subcellular location	Membrane; Multi-pass membrane protein Probable.
Tissue specificity	Highly expressed in adult heart. Detected at lower levels in head and abdomen. Ref.4
Developmental stage	Detected in embryonic myocardial cells and in the developing heart tube. Detected in embryonic dorsal vessels and tracheal system. Ref.1 Ref.4
Miscellaneous	Drosophila is predominantly active around dawn and dusk, and has large sleep periods during the day and during night. Knockdown of Sur reduces sleep duration during the first half of the night, but has little effect on sleep during the day (Ref.5).
Sequence similarities	Belongs to the ABC transporter superfamily. ABCC family. Conjugate transporter (TC 3.A.1.208) subfamily. [View classification] Contains 2 ABC transmembrane type-1 domains. Contains 2 ABC transporter domains.
Sequence caution	The sequence AAF06736.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Transport
Cellular component	Membrane
Domain	Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase Receptor
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from electronic annotation. Source: GOC heart development Non-traceable author statement PubMed 12027431. Source: FlyBase response to hypoxia Inferred from mutant phenotype Ref.4. Source: FlyBase
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled to transmembrane movement of substances Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2171	2171	ATP-binding cassette sub-family C member Sur		PRO_0000415415
Regions
	Topological domain	1 – 36	36	Extracellular Potential
	Transmembrane	37 – 57	21	Helical; Name=1; Potential
	Topological domain	58 – 71	14	Cytoplasmic Potential
	Transmembrane	72 – 92	21	Helical; Name=2; Potential
	Topological domain	93 – 112	20	Extracellular Potential
	Transmembrane	113 – 133	21	Helical; Name=3; Potential
	Topological domain	134 – 145	12	Cytoplasmic Potential
	Transmembrane	146 – 166	21	Helical; Name=4; Potential
	Topological domain	167 – 182	16	Extracellular Potential
	Transmembrane	183 – 203	21	Helical; Name=5; Potential
	Topological domain	204 – 224	21	Cytoplasmic Potential
	Transmembrane	225 – 245	21	Helical; Name=6; Potential
	Topological domain	246 – 299	54	Extracellular Potential
	Transmembrane	300 – 320	21	Helical; Name=7; Potential
	Topological domain	321 – 447	127	Cytoplasmic Potential
	Transmembrane	448 – 468	21	Helical; Name=8; Potential
	Topological domain	469 – 474	6	Extracellular Potential
	Transmembrane	475 – 495	21	Helical; Name=9; Potential
	Topological domain	496 – 562	67	Cytoplasmic Potential
	Transmembrane	563 – 583	21	Helical; Name=10; Potential
	Topological domain	584 – 600	17	Extracellular Potential
	Transmembrane	601 – 621	21	Helical; Name=11; Potential
	Topological domain	622 – 1409	788	Cytoplasmic Potential
	Transmembrane	1410 – 1430	21	Helical; Name=12; Potential
	Topological domain	1431 – 1468	38	Extracellular Potential
	Transmembrane	1469 – 1489	21	Helical; Name=13; Potential
	Topological domain	1490 – 1558	69	Cytoplasmic Potential
	Transmembrane	1559 – 1579	21	Helical; Name=14; Potential
	Topological domain	1580 – 1655	76	Extracellular Potential
	Transmembrane	1656 – 1676	21	Helical; Name=15; Potential
	Topological domain	1677 – 1718	42	Cytoplasmic Potential
	Transmembrane	1719 – 1739	21	Helical; Name=16; Potential
	Topological domain	1740 – 2171	432	Extracellular Potential
	Domain	344 – 622	279	ABC transmembrane type-1 1
	Domain	785 – 1014	230	ABC transporter 1
	Domain	1421 – 1715	295	ABC transmembrane type-1 2
	Domain	1930 – 2165	236	ABC transporter 2
	Nucleotide binding	822 – 829	8	ATP 1 Potential
	Nucleotide binding	1964 – 1971	8	ATP 2 Potential
Experimental info
	Sequence conflict	34 – 35	2	VR → CA in AAF06736. Ref.1
	Sequence conflict	54	1	C → Y in AAF06736. Ref.1
	Sequence conflict	77	1	L → I in AAF06736. Ref.1
	Sequence conflict	85	1	D → E in AAF06736. Ref.1
	Sequence conflict	413	1	M → V in AAF06736. Ref.1
	Sequence conflict	433	1	S → G in AAF06736. Ref.1
	Sequence conflict	444	1	N → S in AAF06736. Ref.1
	Sequence conflict	731	1	R → G in AAF06736. Ref.1
	Sequence conflict	1022	1	K → E in AAF06736. Ref.1
	Sequence conflict	1603	1	A → T in AAF06736. Ref.1
	Sequence conflict	1757	1	H → Q in AAF06736. Ref.1
	Sequence conflict	1763 – 1766	4	Missing in AAF06736. Ref.1
	Sequence conflict	1772	1	A → T in AAF06736. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9VL32 [UniParc]. Last modified March 3, 2009. Version 4. Checksum: 5BA7802AD742B6D2	FASTA	2,171	242,375
	10 20 30 40 50 60 MKQLFNIIHC DHLNGHVRSI YDNLNTDICG IDRVRRVFTF FSIFLLLFGL MFVCSRYKKC 70 80 90 100 110 120 HKTLLTFHNG RAAISLLLLA LNSFDLARIF LPHQNVRNLN RLFQSSPRDL NYLVVIGSGE 130 140 150 160 170 180 LWNALFSTLL TLMLMLYHRM VERKKATVFL YASTAVEALT FALLSNELFE LVRYEDFLEL 190 200 210 220 230 240 QTCLVAMSAM CMVSLAMLDG LTVYKECYHD DYLDDYGKIG YKHSMATFYS KSCFWWLTPL 250 260 270 280 290 300 LWLGYKEPLE LEDLGQMKLE DSARSHYDHF LYIYTEKKKK SNSSPSLWYC YIKNSWQMFA 310 320 330 340 350 360 LGGILKLAGD LFALIGPLAI QKIVEYIEQL YAQASEPPAK SPGNEVANVL LSTSRILGTE 370 380 390 400 410 420 FDEVFGTNID KGLIYRKSLL LNADGGCDSS DSAGQVQSTS STSDEKQKND DSMATPEHVD 430 440 450 460 470 480 NPSEPNISHD IGSITNHMTE DTRNIMEFFL IIHYAWAIPF KIAVVIYLLY MNLGISAVIG 490 500 510 520 530 540 SIACIVIMTP LQFFIGNAMS KNAEVIAGYT DERLKRIHDT LVGIKVIKLN AWDEVFLKKI 550 560 570 580 590 600 QEARRKELKY LNKDATFWTL MAVLTHIATV LITFVTLGVY VWLHRDQEFD LNASRLFSSL 610 620 630 640 650 660 ALFQQLTVPL LIFPITVPII IAARVSTRRL ERFLKSSEIQ KQFEGIRNMA RILSKSDASL 670 680 690 700 710 720 DMYETQEKSN MTMRTAQAEN RLNEKRLAQK SQTPELATNS TPLLQNAEES AEDISPSTVQ 730 740 750 760 770 780 ELGHNKLVQQ RRELLRNTPY VAIRPPKMRG SVMERPVEFS VIRARNTDSW RRDSLLLKMP 790 800 810 820 830 840 DDIAVSINDG LFTWQPQSQM PVVQLHVPGI IVPKGKLTIV VGKNGSGKTS LLSALLMEMP 850 860 870 880 890 900 LLAGNMFWHK TCTISYVSQQ PWLLNDTIRE NILFGESFRP KRYDFVLEAC ALKPDIELMP 910 920 930 940 950 960 RGDLSIIGER GINISGGQRQ RIAIARAIYS SANVVIMDDP LASLDNEVGE HIFQHCIREM 970 980 990 1000 1010 1020 LQKSNRTFIL VTQQLHRIKE AEYLIAIKDG RVEACGSYAD IELMQPRITA EWNAIIAMAK 1030 1040 1050 1060 1070 1080 AKNDNPSQNP GEKTAGERWK LLKNVSKLGL QRSISVTMDA NVACHADAID GSGCISVANM 1090 1100 1110 1120 1130 1140 QSNVVEEDDQ VSVSYPIGNA SCGGFNLQRK RSSIYGSRHL MYDVPLPIDE CQGDDVIMRP 1150 1160 1170 1180 1190 1200 RRRHTLGRRG SRNTNSSHRL SGLSTLTATS ESSSISGDVL SRSVLATSCS SYAESSVDGG 1210 1220 1230 1240 1250 1260 DLATAAPEPR VQSWQPPQHV THHQPLSRNA SSPPAMEVAN PDVKKSEEAR RSNTSSESPL 1270 1280 1290 1300 1310 1320 DDHVRGSFQQ FLRRMSMRRS NKPKNHHHPL SATNSILSIS EESPPVVHFP ASILATDGNK 1330 1340 1350 1360 1370 1380 NETQSEEKPK KCVNIDSKET TINCDDNCYS ASDKELRANV TSSPADQEQH NERHVLAEVA 1390 1400 1410 1420 1430 1440 GESGRESMPL ARLAIDTERK YGKISDDIYL MYIRAAGLPI ITIFFITALI WQCLRVYTDI 1450 1460 1470 1480 1490 1500 WLQQWSNVHG RVASKGHVVL HPSEQDHEVT YYFRMYAAIS CVCIIMALVS TPAGQYAGCN 1510 1520 1530 1540 1550 1560 ARRNLHDKLL QTILHKTLHF FQVTPLGRIV NRFSNDMAVI DKKIAATGQR LLQFTLLCLS 1570 1580 1590 1600 1610 1620 AILINVTITP WILVLTLPIC GAYYLIQKFY RCSARELQRI ENATNSPVIS HLSETIQGVT 1630 1640 1650 1660 1670 1680 TIRAFNQQTR FTEILFKRLE ANTIAYALLN TSHRWLGVSL DYLGGCIVFV ATVTALTAAS 1690 1700 1710 1720 1730 1740 VSCRRHYEAT TSPSASASPS PFETYAVTKS PSELRPSPSL VGLAINYTLL VPIYLNWVVK 1750 1760 1770 1780 1790 1800 LLADMEMYAG SVERIAHYAQ GQDADADADA DADADVDADL DHEPSSNEDV SAEVDRSSQS 1810 1820 1830 1840 1850 1860 DAGDKVYPGA TTAAGDVDED GDQQRIGGAR GGGGDCGYRQ GHENGAEANA DKLNAGNVTG 1870 1880 1890 1900 1910 1920 DGNHLNFHHP PATAGDKVEQ ATTKTSVIKD KQLPPQQDDK DKKVVLPNEP ARKLERYQSV 1930 1940 1950 1960 1970 1980 PISWPQRGDI HFDNVSLRYE GQKQNVISNL TLKIPAGQRI GICGRTGSGK SSLGLSLFGV 1990 2000 2010 2020 2030 2040 LQTTRGHIYI DDVDIQRIRP DELRTRLSII PQDVHLFNAT IRENLDPHGY FQDLQLWNCL 2050 2060 2070 2080 2090 2100 ELAQLKEFVN GHLPLGLDTV ICDGGLNLSA GHRQLLCLAR AILRGSVCLV LDEATSVLDS 2110 2120 2130 2140 2150 2160 STESALLKAA DLAFRGRTII TIAHRLTTIL DYDRLIVLDQ GRIVEDGNPR ELQQLEGSVF 2170 RGLLEKGASK W

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel sulfonylurea receptor family member expressed in the embryonic Drosophila dorsal vessel and tracheal system." Nasonkin I., Alikasifoglu A., Ambrose C., Cahill P., Cheng M., Sarniak A., Egan M., Thomas P.M. J. Biol. Chem. 274:29420-29425(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"The ATP-sensitive potassium (KATP) channel-encoded dSUR gene is required for Drosophila heart function and is regulated by tinman." Akasaka T., Klinedinst S., Ocorr K., Bustamante E.L., Kim S.K., Bodmer R. Proc. Natl. Acad. Sci. U.S.A. 103:11999-12004(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
[5]	"A K(ATP) channel gene effect on sleep duration: from genome-wide association studies to function in Drosophila." Allebrandt K.V., Amin N., Muller-Myhsok B., Esko T., Teder-Laving M., Azevedo R.V., Hayward C., van Mill J., Vogelzangs N., Green E.W., Melville S.A., Lichtner P., Wichmann H.E., Oostra B.A., Janssens A.C., Campbell H., Wilson J.F., Hicks A.A. , Pramstaller P.P., Dogas Z., Rudan I., Merrow M., Penninx B., Kyriacou C.P., Metspalu A., van Duijn C.M., Meitinger T., Roenneberg T. Mol. Psychiatry 18:122-132(2013) [PubMed] [Europe PMC] [Abstract] Cited for: POSSIBLE FUNCTION IN REGULATION OF SLEEP PATTERN.
+	Additional computationally mapped references.

Web resources

Protein Spotlight

On The Other Side - Issue 139 of June 2012

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF167431 mRNA. Translation: AAF06736.1. Different initiation. AE014134 Genomic DNA. Translation: AAF52866.4.
RefSeq	NP_477472.2. NM_058124.3.
UniGene	Dm.382.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	7227.FBpp0288707.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0290268; FBpp0288707; FBgn0028675.
GeneID	34350.
KEGG	dme:Dmel_CG5772.
Organism-specific databases
CTD	34350.
FlyBase	FBgn0028675. Sur.
Phylogenomic databases
GeneTree	ENSGT00700000105225.
InParanoid	Q9VL32.
OMA	TARERWK.
PhylomeDB	Q9VL32.
Gene expression databases
Bgee	Q9VL32.
Family and domain databases
InterPro	IPR003593. AAA+_ATPase. IPR003439. ABC_transporter-like. IPR017871. ABC_transporter_CS. IPR017940. ABC_transporter_type1. IPR001140. ABC_transptr_TM_dom. IPR011527. ABC_transptrTM_dom_typ1. IPR027417. P-loop_NTPase. [Graphical view]
Pfam	PF00664. ABC_membrane. 2 hits. PF00005. ABC_tran. 2 hits. [Graphical view]
SMART	SM00382. AAA. 2 hits. [Graphical view]
SUPFAM	SSF90123. ABC_TM_1. 2 hits. SSF52540. SSF52540. 2 hits.
PROSITE	PS50929. ABC_TM1F. 2 hits. PS00211. ABC_TRANSPORTER_1. 1 hit. PS50893. ABC_TRANSPORTER_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SUR. drosophila.
GenomeRNAi	34350.
NextBio	788061.

Entry information

Entry name

SUR_DROME

Accession

Primary (citable) accession number: Q9VL32
Secondary accession number(s): Q9U6Z2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 22, 2012
Last sequence update:	March 3, 2009
Last modified:	May 29, 2013
This is version 105 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project