Q99758 · ABCA3_HUMAN
- ProteinPhospholipid-transporting ATPase ABCA3
- GeneABCA3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1704 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Transports preferentially phosphatidylcholine containing short acyl chains (PubMed:27177387).
In addition plays a role as an efflux transporter of miltefosine across macrophage membranes and free cholesterol (FC) through intralumenal vesicles by removing FC from the cell as a component of surfactant and protects cells from free cholesterol toxicity (PubMed:25817392, PubMed:26903515, PubMed:27177387).
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
- 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine(in) + ATP + H2O = 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine(out) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
- ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H+ + phosphateThis reaction proceeds in the forward direction.
- 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)(in) + ATP + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol)(out) + ADP + H+ + phosphateThis reaction proceeds in the forward direction.
Activity regulation
Features
Showing features for site, binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePhospholipid-transporting ATPase ABCA3
- EC number
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ99758
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Trafficks via the Golgi, sorting vesicles (SVs) and late endosome/multivesicular body network directly to the outer membrane of lamellar bodies in AT2 lung epithelial cells or to lysosomes and lysosomal-related organelles (LROs) in other cells where undergoes proteolytic cleavage and oligosaccharide processing from high mannose type to complex type (PubMed:16959783, PubMed:20863830, PubMed:24142515, PubMed:27177387).
Oligomers formation takes place in a post-endoplasmic reticulum compartment (PubMed:27352740).
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 22-42 | Helical | ||||
Sequence: VLVTVLELFLPLLFSGILIWL | ||||||
Transmembrane | 261-283 | Helical | ||||
Sequence: YQLPLLLLLSFTYTALTIARAVV | ||||||
Transmembrane | 307-327 | Helical | ||||
Sequence: AWFLLFFLFLLIAASFMTLLF | ||||||
Transmembrane | 344-364 | Helical | ||||
Sequence: SLVLAFLLCFAISTISFSFMV | ||||||
Transmembrane | 373-393 | Helical | ||||
Sequence: MAAAFGGFLYFFTYIPYFFVA | ||||||
Transmembrane | 405-425 | Helical | ||||
Sequence: LCSCLLSNVAMAMGAQLIGKF | ||||||
Transmembrane | 447-467 | Helical | ||||
Sequence: FCFGQVLGMLLLDSVLYGLVT | ||||||
Transmembrane | 925-945 | Helical | ||||
Sequence: MVAAQVLVPLTCVTLALLAIN | ||||||
Transmembrane | 1100-1120 | Helical | ||||
Sequence: IALNLLFAMAFLASTFSILAV | ||||||
Transmembrane | 1144-1164 | Helical | ||||
Sequence: SALLWDLISFLIPSLLLLVVF | ||||||
Transmembrane | 1183-1203 | Helical | ||||
Sequence: LLLLLYGWAIIPLMYLMNFFF | ||||||
Transmembrane | 1213-1233 | Helical | ||||
Sequence: LTIFNILSGIATFLMVTIMRI | ||||||
Transmembrane | 1245-1265 | Helical | ||||
Sequence: LDHVFLVLPNHCLGMAVSSFY | ||||||
Transmembrane | 1306-1326 | Helical | ||||
Sequence: FVASMAASGCAYLILLFLIET |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Pulmonary surfactant metabolism dysfunction 3 (SMDP3)
- Note
- DescriptionA rare lung disorder due to impaired surfactant homeostasis. It is characterized by alveolar filling with floccular material that stains positive using the periodic acid-Schiff method and is derived from surfactant phospholipids and protein components. Excessive lipoproteins accumulation in the alveoli results in severe respiratory distress.
- See alsoMIM:610921
Natural variants in SMDP3
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_084240 | 43 | R>L | in SMDP3; uncertain significance | |
VAR_023497 | 101 | L>P | in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro; dbSNP:rs121909182 | |
VAR_084241 | 215 | Q>K | in SMDP3; loss of lamellar bodies membrane location; loss of proteolytic cleavage; increases cellular free cholesterol and phosphatidylcholine transport; loss of vesicles formation; increases free cholesterol induced cell death; loss of protein oligomerization; dbSNP:rs879159551 | |
VAR_084242 | 280 | R>C | in SMDP3; uncertain significance; does not affect protein oligomerization; dbSNP:rs201299260 | |
VAR_084243 | 288 | R>K | in SMDP3; uncertain significance; does not affect protein oligomerization; dbSNP:rs117603931 | |
VAR_084244 | 292 | E>V | in SMDP3; uncertain significance; does not affect lamellar bodies membrane location; does not affect proteolytic cleavage; affects lamellar bodies formation; does not affect cholesterol and phosphatidylcholine transport; decreases vesicles formation; does not affect free cholesterol induced cell death; dbSNP:rs149989682 | |
VAR_023498 | 568 | N>D | in SMDP3; does not affect location in intracellular vesicle membrane; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro; does not affect protein expression; does not affect multivesicular bodies and lamellar bodies location; affects multivesicular bodies and lamellar bodies development; loss of phosphatidylcholine transport; does not affect cholesterol transport; dbSNP:rs121909184 | |
VAR_084245 | 579 | L>P | in SMDP3; uncertain significance | |
VAR_084246 | 605 | R>Q | in SMDP3; uncertain significance; dbSNP:rs760006956 | |
VAR_084247 | 690 | E>K | in SMDP3; dbSNP:rs2141707325 | |
VAR_084248 | 982 | L>P | in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; dbSNP:rs1402761450 | |
VAR_084249 | 1076 | N>K | in SMDP3; uncertain significance; dbSNP:rs2093663770 | |
VAR_084250 | 1114 | T>M | in SMDP3; dbSNP:rs891579143 | |
VAR_084251 | 1221 | G>S | in SMDP3; does not affect intracellular vesicle membrane location; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity | |
VAR_084252 | 1301 | P>L | in SMDP3; dbSNP:rs762699052 | |
VAR_084253 | 1302 | G>E | in SMDP3; uncertain significance; dbSNP:rs2093657978 | |
VAR_084254 | 1388 | K>N | in SMDP3; decreases phosphatidylcholine transport; increases protein abundance; does not affect folding in the endoplasmic reticulum; decreases proteolytic processing; affects lamellar bodies development; reduces free cholesterol transport | |
VAR_084255 | 1399 | V>M | in SMDP3; dbSNP:rs763166660 | |
VAR_023499 | 1553 | L>P | in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; dbSNP:rs121909183 | |
VAR_084256 | 1561-1704 | missing | in SMDP3 | |
VAR_084257 | 1580 | L>P | in SMDP3; does not affect location in intracellular vesicle membrane; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro; affects the intracellular vesicles development; decreases phosphatidylcholine transport | |
VAR_084258 | 1589-1704 | missing | in SMDP3 | |
VAR_023500 | 1591 | Q>P | in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; dbSNP:rs28936691 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_084240 | 43 | in SMDP3; uncertain significance | |||
Sequence: R → L | ||||||
Mutagenesis | 53 | Does not affect N-glycosylation. Does not affect protein expression. Does not affect lamellar body membrane location. | ||||
Sequence: N → Q | ||||||
Natural variant | VAR_023497 | 101 | in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro; dbSNP:rs121909182 | |||
Sequence: L → P | ||||||
Mutagenesis | 124 | Loss of N-glycosylation. Reduces protein expression by 50%. Affects anterograde trafficking; when associated with Q-140. Reduces protein expression by 85%; when associated with Q-140. Does not affect lamellar body membrane location. | ||||
Sequence: N → Q | ||||||
Natural variant | VAR_025061 | 140 | in dbSNP:rs45447801 | |||
Sequence: N → H | ||||||
Mutagenesis | 140 | Loss of N-glycosylation. Reduces protein expression by 50%. Affects anterograde trafficking; when associated with Q-124. Reduces protein expression by 85%; when associated with Q-140. Does not affect lamellar body membrane location. | ||||
Sequence: N → Q | ||||||
Mutagenesis | 173-174 | Loss of proteolytic processing. | ||||
Sequence: LK → AA | ||||||
Natural variant | VAR_084241 | 215 | in SMDP3; loss of lamellar bodies membrane location; loss of proteolytic cleavage; increases cellular free cholesterol and phosphatidylcholine transport; loss of vesicles formation; increases free cholesterol induced cell death; loss of protein oligomerization; dbSNP:rs879159551 | |||
Sequence: Q → K | ||||||
Natural variant | VAR_084242 | 280 | in SMDP3; uncertain significance; does not affect protein oligomerization; dbSNP:rs201299260 | |||
Sequence: R → C | ||||||
Natural variant | VAR_084243 | 288 | in SMDP3; uncertain significance; does not affect protein oligomerization; dbSNP:rs117603931 | |||
Sequence: R → K | ||||||
Natural variant | VAR_035728 | 290 | in a breast cancer sample; somatic mutation | |||
Sequence: L → M | ||||||
Natural variant | VAR_084244 | 292 | in SMDP3; uncertain significance; does not affect lamellar bodies membrane location; does not affect proteolytic cleavage; affects lamellar bodies formation; does not affect cholesterol and phosphatidylcholine transport; decreases vesicles formation; does not affect free cholesterol induced cell death; dbSNP:rs149989682 | |||
Sequence: E → V | ||||||
Natural variant | VAR_023498 | 568 | in SMDP3; does not affect location in intracellular vesicle membrane; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro; does not affect protein expression; does not affect multivesicular bodies and lamellar bodies location; affects multivesicular bodies and lamellar bodies development; loss of phosphatidylcholine transport; does not affect cholesterol transport; dbSNP:rs121909184 | |||
Sequence: N → D | ||||||
Natural variant | VAR_084245 | 579 | in SMDP3; uncertain significance | |||
Sequence: L → P | ||||||
Natural variant | VAR_084246 | 605 | in SMDP3; uncertain significance; dbSNP:rs760006956 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_084247 | 690 | in SMDP3; dbSNP:rs2141707325 | |||
Sequence: E → K | ||||||
Mutagenesis | 693 | Does not affect protein oligomerization. | ||||
Sequence: S → L | ||||||
Natural variant | VAR_025062 | 766 | in dbSNP:rs45592239 | |||
Sequence: P → S | ||||||
Natural variant | VAR_035729 | 801 | in a breast cancer sample; somatic mutation | |||
Sequence: E → D | ||||||
Mutagenesis | 945 | Does not affect lamellar body membrane location. Does not affect protein expression. Does not affect proteolytic processing. | ||||
Sequence: N → Q | ||||||
Natural variant | VAR_084248 | 982 | in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; dbSNP:rs1402761450 | |||
Sequence: L → P | ||||||
Natural variant | VAR_035730 | 1069 | in a breast cancer sample; somatic mutation | |||
Sequence: H → Q | ||||||
Natural variant | VAR_084249 | 1076 | in SMDP3; uncertain significance; dbSNP:rs2093663770 | |||
Sequence: N → K | ||||||
Natural variant | VAR_084250 | 1114 | in SMDP3; dbSNP:rs891579143 | |||
Sequence: T → M | ||||||
Natural variant | VAR_084251 | 1221 | in SMDP3; does not affect intracellular vesicle membrane location; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity | |||
Sequence: G → S | ||||||
Mutagenesis | 1221 | Decreases ATP hydrolysis activity of 15% compared to the wild-type. | ||||
Sequence: G → A | ||||||
Mutagenesis | 1221 | Decreases ATP hydrolysis activity of 36% compared to the wild-type. | ||||
Sequence: G → T | ||||||
Mutagenesis | 1221 | Decreases ATP hydrolysis activity of 18% compared to the wild-type. | ||||
Sequence: G → V | ||||||
Natural variant | VAR_084252 | 1301 | in SMDP3; dbSNP:rs762699052 | |||
Sequence: P → L | ||||||
Natural variant | VAR_084253 | 1302 | in SMDP3; uncertain significance; dbSNP:rs2093657978 | |||
Sequence: G → E | ||||||
Natural variant | VAR_084254 | 1388 | in SMDP3; decreases phosphatidylcholine transport; increases protein abundance; does not affect folding in the endoplasmic reticulum; decreases proteolytic processing; affects lamellar bodies development; reduces free cholesterol transport | |||
Sequence: K → N | ||||||
Natural variant | VAR_084255 | 1399 | in SMDP3; dbSNP:rs763166660 | |||
Sequence: V → M | ||||||
Natural variant | VAR_023499 | 1553 | in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; dbSNP:rs121909183 | |||
Sequence: L → P | ||||||
Natural variant | VAR_084256 | 1561-1704 | in SMDP3 | |||
Sequence: Missing | ||||||
Natural variant | VAR_084257 | 1580 | in SMDP3; does not affect location in intracellular vesicle membrane; does not affect proteolytic cleavage; does not affect N-glycosylation; loss of ATP hydrolysis activity; decreases ATP binding in vitro; affects the intracellular vesicles development; decreases phosphatidylcholine transport | |||
Sequence: L → P | ||||||
Mutagenesis | 1580 | Decreases ATP hydrolysis activity of 13% compared to the wild-type. | ||||
Sequence: L → A | ||||||
Mutagenesis | 1580 | Decreases ATP hydrolysis activity of 13% compared to the wild-type. | ||||
Sequence: L → F | ||||||
Mutagenesis | 1580 | Decreases ATP hydrolysis activity of 56% compared to the wild-type. | ||||
Sequence: L → V | ||||||
Natural variant | VAR_084258 | 1589-1704 | in SMDP3 | |||
Sequence: Missing | ||||||
Natural variant | VAR_023500 | 1591 | in SMDP3; loss of intracellular vesicle membrane location; loss of proteolytic cleavage; does not affect N-glycosylation; dbSNP:rs28936691 | |||
Sequence: Q → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 2,040 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000093293 | 1-1704 | UniProt | Phospholipid-transporting ATPase ABCA3 | |||
Sequence: MAVLRQLALLLWKNYTLQKRKVLVTVLELFLPLLFSGILIWLRLKIQSENVPNATIYPGQSIQELPLFFTFPPPGDTWELAYIPSHSDAAKTVTETVRRALVINMRVRGFPSEKDFEDYIRYDNCSSSVLAAVVFEHPFNHSKEPLPLAVKYHLRFSYTRRNYMWTQTGSFFLKETEGWHTTSLFPLFPNPGPREPTSPDGGEPGYIREGFLAVQHAVDRAIMEYHADAATRQLFQRLTVTIKRFPYPPFIADPFLVAIQYQLPLLLLLSFTYTALTIARAVVQEKERRLKEYMRMMGLSSWLHWSAWFLLFFLFLLIAASFMTLLFCVKVKPNVAVLSRSDPSLVLAFLLCFAISTISFSFMVSTFFSKANMAAAFGGFLYFFTYIPYFFVAPRYNWMTLSQKLCSCLLSNVAMAMGAQLIGKFEAKGMGIQWRDLLSPVNVDDDFCFGQVLGMLLLDSVLYGLVTWYMEAVFPGQFGVPQPWYFFIMPSYWCGKPRAVAGKEEEDSDPEKALRNEYFEAEPEDLVAGIKIKHLSKVFRVGNKDRAAVRDLNLNLYEGQITVLLGHNGAGKTTTLSMLTGLFPPTSGRAYISGYEISQDMVQIRKSLGLCPQHDILFDNLTVAEHLYFYAQLKGLSRQKCPEEVKQMLHIIGLEDKWNSRSRFLSGGMRRKLSIGIALIAGSKVLILDEPTSGMDAISRRAIWDLLQRQKSDRTIVLTTHFMDEADLLGDRIAIMAKGELQCCGSSLFLKQKYGAGYHMTLVKEPHCNPEDISQLVHHHVPNATLESSAGAELSFILPRESTHRFEGLFAKLEKKQKELGIASFGASITTMEEVFLRVGKLVDSSMDIQAIQLPALQYQHERRASDWAVDSNLCGAMDPSDGIGALIEEERTAVKLNTGLALHCQQFWAMFLKKAAYSWREWKMVAAQVLVPLTCVTLALLAINYSSELFDDPMLRLTLGEYGRTVVPFSVPGTSQLGQQLSEHLKDALQAEGQEPREVLGDLEEFLIFRASVEGGGFNERCLVAASFRDVGERTVVNALFNNQAYHSPATALAVVDNLLFKLLCGPHASIVVSNFPQPRSALQAAKDQFNEGRKGFDIALNLLFAMAFLASTFSILAVSERAVQAKHVQFVSGVHVASFWLSALLWDLISFLIPSLLLLVVFKAFDVRAFTRDGHMADTLLLLLLYGWAIIPLMYLMNFFFLGAATAYTRLTIFNILSGIATFLMVTIMRIPAVKLEELSKTLDHVFLVLPNHCLGMAVSSFYENYETRRYCTSSEVAAHYCKKYNIQYQENFYAWSAPGVGRFVASMAASGCAYLILLFLIETNLLQRLRGILCALRRRRTLTELYTRMPVLPEDQDVADERTRILAPSPDSLLHTPLIIKELSKVYEQRVPLLAVDRLSLAVQKGECFGLLGFNGAGKTTTFKMLTGEESLTSGDAFVGGHRISSDVGKVRQRIGYCPQFDALLDHMTGREMLVMYARLRGIPERHIGACVENTLRGLLLEPHANKLVRTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIIITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGSGYSLRAKVQSEGQQEALEEFKAFVDLTFPGSVLEDEHQGMVHYHLPGRDLSWAKVFGILEKAKEKYGVDDYSVSQISLEQVFLSFAHLQPPTAEEGR | |||||||
Glycosylation | 14 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 53 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 124 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 140 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Chain | PRO_0000452297 | 175-1704 | UniProt | 150 Kda mature form | |||
Sequence: ETEGWHTTSLFPLFPNPGPREPTSPDGGEPGYIREGFLAVQHAVDRAIMEYHADAATRQLFQRLTVTIKRFPYPPFIADPFLVAIQYQLPLLLLLSFTYTALTIARAVVQEKERRLKEYMRMMGLSSWLHWSAWFLLFFLFLLIAASFMTLLFCVKVKPNVAVLSRSDPSLVLAFLLCFAISTISFSFMVSTFFSKANMAAAFGGFLYFFTYIPYFFVAPRYNWMTLSQKLCSCLLSNVAMAMGAQLIGKFEAKGMGIQWRDLLSPVNVDDDFCFGQVLGMLLLDSVLYGLVTWYMEAVFPGQFGVPQPWYFFIMPSYWCGKPRAVAGKEEEDSDPEKALRNEYFEAEPEDLVAGIKIKHLSKVFRVGNKDRAAVRDLNLNLYEGQITVLLGHNGAGKTTTLSMLTGLFPPTSGRAYISGYEISQDMVQIRKSLGLCPQHDILFDNLTVAEHLYFYAQLKGLSRQKCPEEVKQMLHIIGLEDKWNSRSRFLSGGMRRKLSIGIALIAGSKVLILDEPTSGMDAISRRAIWDLLQRQKSDRTIVLTTHFMDEADLLGDRIAIMAKGELQCCGSSLFLKQKYGAGYHMTLVKEPHCNPEDISQLVHHHVPNATLESSAGAELSFILPRESTHRFEGLFAKLEKKQKELGIASFGASITTMEEVFLRVGKLVDSSMDIQAIQLPALQYQHERRASDWAVDSNLCGAMDPSDGIGALIEEERTAVKLNTGLALHCQQFWAMFLKKAAYSWREWKMVAAQVLVPLTCVTLALLAINYSSELFDDPMLRLTLGEYGRTVVPFSVPGTSQLGQQLSEHLKDALQAEGQEPREVLGDLEEFLIFRASVEGGGFNERCLVAASFRDVGERTVVNALFNNQAYHSPATALAVVDNLLFKLLCGPHASIVVSNFPQPRSALQAAKDQFNEGRKGFDIALNLLFAMAFLASTFSILAVSERAVQAKHVQFVSGVHVASFWLSALLWDLISFLIPSLLLLVVFKAFDVRAFTRDGHMADTLLLLLLYGWAIIPLMYLMNFFFLGAATAYTRLTIFNILSGIATFLMVTIMRIPAVKLEELSKTLDHVFLVLPNHCLGMAVSSFYENYETRRYCTSSEVAAHYCKKYNIQYQENFYAWSAPGVGRFVASMAASGCAYLILLFLIETNLLQRLRGILCALRRRRTLTELYTRMPVLPEDQDVADERTRILAPSPDSLLHTPLIIKELSKVYEQRVPLLAVDRLSLAVQKGECFGLLGFNGAGKTTTFKMLTGEESLTSGDAFVGGHRISSDVGKVRQRIGYCPQFDALLDHMTGREMLVMYARLRGIPERHIGACVENTLRGLLLEPHANKLVRTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIIITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGSGYSLRAKVQSEGQQEALEEFKAFVDLTFPGSVLEDEHQGMVHYHLPGRDLSWAKVFGILEKAKEKYGVDDYSVSQISLEQVFLSFAHLQPPTAEEGR | |||||||
Glycosylation | 620 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 783 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 866 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1434 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Localization at intracellular vesicles is accompanied by processing of oligosaccharide from high mannose type to complex type (PubMed:16959783, PubMed:27177387).
N-linked glycosylation at Asn-124 and Asn-140 is required for stability and efficient anterograde trafficking and prevents from proteasomal degradation (PubMed:24142515).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in the lung in an AT2-cell-specific manner (PubMed:11718719, PubMed:8706931).
Weakly expressed in placenta, kidney and liver (PubMed:8706931).
Also expressed in medullary thyroid carcinoma cells (MTC) and in C-cell carcinoma (PubMed:8706931).
Induction
Down-regulated by L. V. panamensis infection (PubMed:26903515).
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 530-763 | ABC transporter 1 | ||||
Sequence: IKIKHLSKVFRVGNKDRAAVRDLNLNLYEGQITVLLGHNGAGKTTTLSMLTGLFPPTSGRAYISGYEISQDMVQIRKSLGLCPQHDILFDNLTVAEHLYFYAQLKGLSRQKCPEEVKQMLHIIGLEDKWNSRSRFLSGGMRRKLSIGIALIAGSKVLILDEPTSGMDAISRRAIWDLLQRQKSDRTIVLTTHFMDEADLLGDRIAIMAKGELQCCGSSLFLKQKYGAGYHMTLV | ||||||
Domain | 1381-1614 | ABC transporter 2 | ||||
Sequence: LIIKELSKVYEQRVPLLAVDRLSLAVQKGECFGLLGFNGAGKTTTFKMLTGEESLTSGDAFVGGHRISSDVGKVRQRIGYCPQFDALLDHMTGREMLVMYARLRGIPERHIGACVENTLRGLLLEPHANKLVRTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIIITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGSGYSLRAK |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q99758-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,704
- Mass (Da)191,362
- Last updated2006-01-24 v2
- Checksum606735C504839D0D
Q99758-2
- Name2
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0Y3H2 | H0Y3H2_HUMAN | ABCA3 | 1646 |
Features
Showing features for sequence conflict, alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U78735 EMBL· GenBank· DDBJ | AAC50967.1 EMBL· GenBank· DDBJ | mRNA | ||
X97187 EMBL· GenBank· DDBJ | CAA65825.1 EMBL· GenBank· DDBJ | mRNA | ||
AB070929 EMBL· GenBank· DDBJ | BAB86781.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ073080 EMBL· GenBank· DDBJ | AAY57325.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471112 EMBL· GenBank· DDBJ | EAW85515.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC020724 EMBL· GenBank· DDBJ | AAH20724.1 EMBL· GenBank· DDBJ | mRNA | ||
BC062779 EMBL· GenBank· DDBJ | AAH62779.1 EMBL· GenBank· DDBJ | mRNA | ||
AC009065 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC098805 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC106820 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC140895 EMBL· GenBank· DDBJ | AAI40896.1 EMBL· GenBank· DDBJ | mRNA | ||
BC146866 EMBL· GenBank· DDBJ | AAI46867.1 EMBL· GenBank· DDBJ | mRNA |