ABCAH_MOUSE
ID ABCAH_MOUSE Reviewed; 1733 AA.
AC E9PX95; Q4H4D7;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=ATP-binding cassette sub-family A member 17 {ECO:0000312|MGI:MGI:3625331};
GN Name=Abca17 {ECO:0000312|MGI:MGI:3625331};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:BAD97416.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND GLYCOSYLATION.
RC STRAIN=C57BL/6N {ECO:0000312|EMBL:BAD97416.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAD97416.1};
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:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND CATALYTIC ACTIVITY.
RX PubMed=22237709; DOI=10.14670/hh-27.317;
RA Morales C.R., Ni X., Smith C.E., Inagaki N., Hermo L.;
RT "ABCA17 mediates sterol efflux from mouse spermatozoa plasma membranes.";
RL Histol. Histopathol. 27:317-328(2012).
CC -!- FUNCTION: Promotes cholesterol efflux from sperm which renders sperm
CC capable of fertilization (PubMed:22237709). Has also been shown to
CC decrease levels of intracellular esterified neutral lipids including
CC cholesteryl esters, fatty acid esters and triacylglycerols
CC (PubMed:15810880). {ECO:0000269|PubMed:15810880,
CC ECO:0000269|PubMed:22237709}.
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:0000305|PubMed:22237709};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052;
CC Evidence={ECO:0000305|PubMed:22237709};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15810880}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:22237709}.
CC -!- TISSUE SPECIFICITY: In the testis, detected predominantly in elongated
CC spermatids at the late stage of germ cell development and in sperm,
CC with no expression detected in immature germ cells such as
CC spermatogonia and spermatocytes or in somatic cells such as Sertoli
CC cells (at protein level) (PubMed:15810880). Expressed in the head and
CC tail midpiece of elongated spermatids and sperm (at protein level)
CC (PubMed:22237709). Expressed exclusively in the testis
CC (PubMed:15810880, PubMed:22237709). {ECO:0000269|PubMed:15810880,
CC ECO:0000269|PubMed:22237709}.
CC -!- DEVELOPMENTAL STAGE: Detected in the testis at low levels at postnatal
CC day 5 but increases at postnatal days 20 and 45 (at protein level).
CC {ECO:0000269|PubMed:22237709}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15810880}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCA family.
CC {ECO:0000305}.
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DR EMBL; AB112584; BAD97416.1; -; mRNA.
DR EMBL; AC117577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS37485.1; -.
DR RefSeq; NP_001026792.2; NM_001031621.2.
DR RefSeq; XP_006524539.1; XM_006524476.3.
DR RefSeq; XP_006524540.1; XM_006524477.3.
DR RefSeq; XP_006524541.1; XM_006524478.3.
DR RefSeq; XP_006524542.1; XM_006524479.3.
DR RefSeq; XP_017173021.1; XM_017317532.1.
DR RefSeq; XP_017173022.1; XM_017317533.1.
DR AlphaFoldDB; E9PX95; -.
DR SMR; E9PX95; -.
DR STRING; 10090.ENSMUSP00000112538; -.
DR TCDB; 3.A.1.211.26; the atp-binding cassette (abc) superfamily.
DR GlyGen; E9PX95; 1 site.
DR MaxQB; E9PX95; -.
DR PaxDb; E9PX95; -.
DR PRIDE; E9PX95; -.
DR ProteomicsDB; 296468; -.
DR Ensembl; ENSMUST00000039324; ENSMUSP00000046218; ENSMUSG00000035435.
DR Ensembl; ENSMUST00000121226; ENSMUSP00000112538; ENSMUSG00000035435.
DR GeneID; 381072; -.
DR KEGG; mmu:381072; -.
DR UCSC; uc008avk.1; mouse.
DR CTD; 381072; -.
DR MGI; MGI:3625331; Abca17.
DR VEuPathDB; HostDB:ENSMUSG00000035435; -.
DR eggNOG; KOG0059; Eukaryota.
DR GeneTree; ENSGT00940000163933; -.
DR HOGENOM; CLU_000604_19_1_1; -.
DR InParanoid; E9PX95; -.
DR OMA; FSLLCQQ; -.
DR OrthoDB; 131191at2759; -.
DR PhylomeDB; E9PX95; -.
DR TreeFam; TF105191; -.
DR BioGRID-ORCS; 381072; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Abca17; mouse.
DR PRO; PR:E9PX95; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; E9PX95; protein.
DR Bgee; ENSMUSG00000035435; Expressed in spermatid and 20 other tissues.
DR ExpressionAtlas; E9PX95; baseline and differential.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
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; IDA:MGI.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
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; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein 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..1733
FT /note="ATP-binding cassette sub-family A member 17"
FT /id="PRO_0000436476"
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 906..926
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1082..1102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1128..1148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1160..1180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1192..1212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1230..1250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1287..1307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 519..752
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1366..1599
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1681..1733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1681..1702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1703..1733
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 555..562
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1401..1408
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 67
FT /note="Y -> C (in Ref. 1; BAD97416)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="T -> M (in Ref. 1; BAD97416)"
FT /evidence="ECO:0000305"
FT CONFLICT 652
FT /note="K -> R (in Ref. 1; BAD97416)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="G -> D (in Ref. 1; BAD97416)"
FT /evidence="ECO:0000305"
FT CONFLICT 1166
FT /note="I -> L (in Ref. 1; BAD97416)"
FT /evidence="ECO:0000305"
FT CONFLICT 1350..1355
FT /note="AETIKR -> TEAIKH (in Ref. 1; BAD97416)"
FT /evidence="ECO:0000305"
FT CONFLICT 1361
FT /note="V -> I (in Ref. 1; BAD97416)"
FT /evidence="ECO:0000305"
FT CONFLICT 1378
FT /note="K -> E (in Ref. 1; BAD97416)"
FT /evidence="ECO:0000305"
FT CONFLICT 1394
FT /note="E -> G (in Ref. 1; BAD97416)"
FT /evidence="ECO:0000305"
FT CONFLICT 1578
FT /note="K -> E (in Ref. 1; BAD97416)"
FT /evidence="ECO:0000305"
FT CONFLICT 1593
FT /note="S -> G (in Ref. 1; BAD97416)"
FT /evidence="ECO:0000305"
FT CONFLICT 1694
FT /note="V -> A (in Ref. 1; BAD97416)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1733 AA; 196020 MW; 91CAA7309F01BF81 CRC64;
MEVLKKLKLL LWKNFILKRR KTLITLLEML MPLLFCAIVL YLRLNSMPRK KSSTNYPAVD
VSLLPVYFYN YPLKSKFQLA YIPSKSETLK AVTEVVEQTF AVDFEVLGFP SVPLFEDYII
KDPKSFYILV GIIFHHDFNS SNEPLPLVVK YDLRFSYVQR NFVSPPRHLF FQEEIEGWCT
AFLYPPNLSQ APREFSYADG GNPGYNKEGF LAIQHAVDKA IMRHHAPKAA LNMFKDLHVL
VQRFPFGPHI QDPFLVILQN EFPLLLMLSF ICVELIITNS VLSEKERKQK EYMSMMGVES
WLHWVAWFIT FFISVSITVS VMTVLFCTKI NRVAVFRNSN PTLIFIFLMC FAIATIFFAF
MMSTFFQRAH VGTVIGGTVF FFTYLPYMYI TFSYHQRTYT QKILSCLFSN VAMATGVRFI
SLFEAEGTGI QWRNIGSVWG DFSFAQVLGM LLLDSFLYCL IAFLVESLFP RKFGIPKSWY
IFAKKPVPEI PPLLNIGDPE KPSKGNFMQD EPTNQMNTIE IQHLYKVFYS GRSKRTAIRD
LSMNLYKGQV TVLLGHNGAG KTTVCSVLTG LITPSKGHAY IHGCEISKDM VQIRKSLGWC
PQHDILFDNF TVTDHLYFYG QLKGLSPQDC HEQTQEMLHL LGLKDKWNSR SKFLSGGMKR
KLSIGIALIA GSKVLILDEP TSGLDSPSRR AIWDLLQQQK GDRTVLLTTH FMDEADLLGD
RIAILAKGEL QCCGSPSFLK QKYGAGYYMT IIKTPLCDTS KLSEVIYHHI PNAVLESNIG
EEMIVTLPKK TIHRFEALFN DLELRQTELG ISTFATSVTT MEEVFIRVCK LADPSTNVLT
EKRHSLHPLP RHHRVPVDRI KCLHSGTFPV STEQPMRLNT GFCLLCQQFY AMLLKKITYS
RRNWMLVLSV QVLLPLAIIM LSLTFFNFKL RKLDNVPLEL TLQTYGQTIV PFFIAENSHL
DPQLSDDFVK MLVAAGQVPL RIQGSVEDFL LKKAKEAPEG FDKLYVVAAS FEDVNNHTTV
KALFNNQAYH SPSLALTLVD NLLFKLLSGA NASITTTNYP QPQTAIEVSE SILYQGPKGH
YLVVNFLFGI AFLSSSFSIL TVGEKSVKSK SLQFVSGVST AVFWLSALLW DLISFLVPTL
LLVLVFLWYK EEAFAHHESI PAVVLIMMLY GWAVIPLVYT VSFSFNTPGS ACVKLVVMLT
FLSISPVVLV TVTSEKDLGY TELSDSLDHI FLILPGHCLG MALSNLYYNF ELKKFCSAKN
LSDIDCNDVL EGYVVQENIY AWESLGIGKY LTALAVLGPV YITMLFLTEA NAFYVLKSRL
SGFFPSFWKE KSGMIFDVAE PEDEDVLEEA ETIKRYLETL VKKNPLVVKE VSKVYKDKVP
LLAVNKVSFV VKEEECFGLL GLNGAGKTSI FNMLTSEQPI TSGDAFVKGF NIKSDIAKVR
QWIGYCPEFD ALLNFMTGRE MLVMYARIRG IPECHIKACV DLILENLLMC VCADKLVKTY
SGGNKRMLST GIALVGEPAV ILLDEPSTGM DPVARRLLWD TVERVRESGK TIVITSHSME
ECEALCTRLA IMVQGQFKCL GSPQHLKSKF GISYSLQAKV RRKWQQQMLE EFKAFVDLTF
PGSNLEDEHQ NMLQYYLPGP NLSWAKVFSI MEQAKKDYML EDYSISQLSL EDIFLNFTRP
ESSTKEQIQQ EQAVLASPSP PSNSRPISSP PSRLSSPTPK PLPSPPPSEP ILL
