ABCAH_RAT
ID ABCAH_RAT Reviewed; 1773 AA.
AC E9PU17; Q4H493;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=ATP-binding cassette sub-family A member 17 {ECO:0000312|RGD:1560494};
GN Name=Abca17 {ECO:0000312|RGD:1560494};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|EMBL:BAD97417.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15810880; DOI=10.1042/bj20050159;
RA Ban N., Sasaki M., Sakai H., Ueda K., Inagaki N.;
RT "Cloning of ABCA17, a novel rodent sperm-specific ABC (ATP-binding
RT cassette) transporter that regulates intracellular lipid metabolism.";
RL Biochem. J. 389:577-585(2005).
RN [2] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
CC -!- FUNCTION: Promotes cholesterol efflux from sperm which renders sperm
CC capable of fertilization. Has also been shown to decrease levels of
CC intracellular esterified neutral lipids including cholesteryl esters,
CC fatty acid esters and triacylglycerols. {ECO:0000250|UniProtKB:E9PX95}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) +
CC phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:E9PX95};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
CC Evidence={ECO:0000250|UniProtKB:E9PX95};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:E9PX95}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:E9PX95}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:E9PX95}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
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DR EMBL; AB196699; BAD97417.1; -; mRNA.
DR EMBL; AC098526; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001026807.1; NM_001031637.1.
DR RefSeq; XP_006245989.1; XM_006245927.3.
DR RefSeq; XP_006245990.1; XM_006245928.3.
DR AlphaFoldDB; E9PU17; -.
DR SMR; E9PU17; -.
DR IntAct; E9PU17; 2.
DR STRING; 10116.ENSRNOP00000057544; -.
DR GlyGen; E9PU17; 3 sites.
DR PaxDb; E9PU17; -.
DR PeptideAtlas; E9PU17; -.
DR PRIDE; E9PU17; -.
DR Ensembl; ENSRNOT00000060818; ENSRNOP00000057544; ENSRNOG00000039656.
DR GeneID; 287112; -.
DR KEGG; rno:287112; -.
DR UCSC; RGD:1560494; rat.
DR CTD; 381072; -.
DR RGD; 1560494; Abca17.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000163933; -.
DR HOGENOM; CLU_000604_19_1_1; -.
DR InParanoid; E9PU17; -.
DR OMA; FSLLCQQ; -.
DR OrthoDB; 131191at2759; -.
DR TreeFam; TF105191; -.
DR PRO; PR:E9PU17; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000039656; Expressed in testis and 3 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005319; F:lipid transporter activity; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IBA:GO_Central.
DR GO; GO:0006638; P:neutral lipid metabolic process; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR026082; ABCA.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR19229; PTHR19229; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Endoplasmic reticulum; Glycoprotein;
KW Lipid metabolism; Lipid transport; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1773
FT /note="ATP-binding cassette sub-family A member 17"
FT /id="PRO_0000436477"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 912..932
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1088..1108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1134..1154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1166..1186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1198..1218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1236..1256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1293..1313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 525..758
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1369..1602
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1690..1773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1690..1709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1710..1773
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 561..568
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1404..1411
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 341
FT /note="T -> P (in Ref. 1; BAD97417)"
FT /evidence="ECO:0000305"
FT CONFLICT 664
FT /note="I -> M (in Ref. 1; BAD97417)"
FT /evidence="ECO:0000305"
FT CONFLICT 1222
FT /note="K -> I (in Ref. 1; BAD97417)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1773 AA; 199859 MW; 98B93F73ED2E4D15 CRC64;
MAPFKKLKLL LWKNFVLKKR KTLVTVLETL MPVLFSAIVL YLRLNSMPRN KANTNYPAVD
VSLLPVYFHN YPLKSKFQLV YIPSKSETLK AVTEVVEQTF AVDFEVLGFP SVSLFENYII
KDPKSFYVLV GIVFHHDFNS SNEPLPLVVK YDLRFSYVQR NSISPPRHLF FQEDIEGWCT
AFLYPPNLSQ APREFSYADG GHPGYNKEGF LAIQHAVDKA IMLHHAPKAA LDMFKNLQVS
VQRFPSGSHI QDPFLVILQN EFPLLLMLSF ICVELIITNS ILLEKERKQK EYMYLMGLEN
WLHWVAWFIT FFLSALVTVS GMTVLFCTKM NGVAVFRNSN TTLIFIFLMC FAIATIFFAF
MMSTFFQRAH VGTVIGGIVF FFTYLPYMYI TFSYHQRTYS QKILSCLFSN VAMAMGVRFI
SLFEAEGTGI QWRNMGSVWG DFSFTQVLVM LLLDSFLYCL VAFLVESLFP RKIGMPKSWY
IFAKCPLWRK KSFPVIPPLL VIGDPEKTSK GDFLQDEPAG HINAIEIQHL YKVFYTGRSK
CIAVKDLSMN LYKGQITVLL GHNGAGKTTV CSVLTGLIPP SKGHAYIHGC EISKDMVRIR
KNVGWCPQHD ILFDNFTVTD HLYFYGQLKG LSHQDCHEKI EEMLHTLGLE DKRNSRSKFL
SGGIKRKLAI GIALIAGSKV LILDEPTSGM DSSSRRAIWD LLQQQKGDRT VLLTTHFMDE
ADLLGDRIAI LAKGELQCCG TPSFLKQKYG AGYYMTIIKT PLCDTEKLAK VIYHHIPNAI
LESRIGEEMI FTLPKKAMPR FEALFADLEQ RQTELGISTF GASVTTMEEV FIRVCKLADP
STNVLTEKRP SLRHLPRNHR VPVDRIKCLH SRIFSLSSDQ PIRLNTGFSL LCQQFYAMLL
KKVAFSRRNW MLVLSVQILL PLVIIMLSLS FFNFKLRKLD NVPLELTLQT YGQTIVPFFI
AENSRLDPQL SDNFVKMLVA AGQVPLRIQG SVENFLLKKA KEAPEDFDKL YVVAASFEDV
NDHTTVKALF NNQAYHSPSL ALALVDNVLF KLLSGANASI TTTNYPQPQT AMELSETILY
QGPKGHYLVV NFLFGIAFLS SSFSILTVGE KSIKSKNLQF LSGVSMAAFW LSALLWDLIS
FLVPTLLLVL VFFWYKEEAF AHPQSIPAVV LIMMLYGWAI IPLVYTVSFS FKTPGSGCVK
LVAMLTFLSI SPVVLVTVTS EKDLGYTELS DTLDHIFLIF PGHCLGMAFS NLYYNFEIKK
FCNAKNLSDI DCNDVLEGYV VQKNIYAWES LGIGKYLTAL AILGPVYITL LFLTEANAFC
ALKARLSGFF CKQKLRMLLN VTGAEDEDVL EEAENIKYHL DTLIKKSPLV VKELSKVYKE
KVPLLAVNKV SFVVKEKECF GLLGLNGAGK TSIFNMLTRE QPITSGDAFV KGFNIRTDMA
KVQQWIGYCP EFDALLNFMT GREMLVMHAR IRGIPECHIK TCVDMILENL LMCVYADKLV
KTYSDGNKRV LSTAIALLGE PTVILLDEPS TGMDPVARRL VWDAVGRVRE SGKTIVITSH
SMEECEALCT RLAIMVQGQF KCLGSPQHLK SRFGSGYSLQ AKVRRKWQQQ MLEEFKAFVD
LTFPGSSLED EHQSMVQYYL PGQNLSWAKV FGIMEQAKKD YVLEDYSISQ LSLEDIFLSF
TRPVPDTKEN IQQGQAALDS SLSPSNSRPI SSPPSSPPSS PPSSPPSRPP SRPSQPPSRP
PSRHPSSPSQ PPSRPPSRHP SSPSQPPSEP VLL
