AT11C_HUMAN
ID AT11C_HUMAN Reviewed; 1132 AA.
AC Q8NB49; Q5JT69; Q5JT70; Q5JT71; Q5JT72; Q5JT73; Q6ZND5; Q6ZU50; Q6ZUP7;
AC Q70IJ9; Q70IK0; Q8WX24;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Phospholipid-transporting ATPase IG;
DE EC=7.6.2.1 {ECO:0000269|PubMed:24904167, ECO:0000269|PubMed:25315773, ECO:0000269|PubMed:32493773};
DE AltName: Full=ATPase IQ;
DE AltName: Full=ATPase class VI type 11C;
DE AltName: Full=P4-ATPase flippase complex alpha subunit ATP11C;
GN Name=ATP11C {ECO:0000303|PubMed:26944472}; Synonyms=ATPIG, ATPIQ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
RP VARIANT TRP-114.
RC TISSUE=Liver;
RX PubMed=15533723; DOI=10.1016/j.ygeno.2004.08.003;
RA Andrew-Nesbit M., Bowl M.R., Harding B., Schlessinger D., Whyte M.P.,
RA Thakker R.V.;
RT "X-linked hypoparathyroidism region on Xq27 is evolutionarily conserved
RT with regions on 3q26 and 13q34 and contains a novel P-type ATPase.";
RL Genomics 84:1060-1070(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 305-1132 (ISOFORM 4), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 543-1132 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 777-1132 (ISOFORM 2).
RC TISSUE=Brain, Fetal brain, Testis, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP INTERACTION WITH TMEM30A, AND SUBCELLULAR LOCATION.
RX PubMed=21914794; DOI=10.1074/jbc.m111.281006;
RA Takatsu H., Baba K., Shima T., Umino H., Kato U., Umeda M., Nakayama K.,
RA Shin H.W.;
RT "ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes
RT to the trans-Golgi network in a CDC50 protein-independent manner.";
RL J. Biol. Chem. 286:38159-38167(2011).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-1108; SER-1116 AND
RP SER-1126, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-157 AND PRO-931.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP GLU-184 AND ASP-412.
RX PubMed=25315773; DOI=10.1074/jbc.m114.593012;
RA Takatsu H., Tanaka G., Segawa K., Suzuki J., Nagata S., Nakayama K.,
RA Shin H.W.;
RT "Phospholipid flippase activities and substrate specificities of human type
RT IV P-type ATPases localized to the plasma membrane.";
RL J. Biol. Chem. 289:33543-33556(2014).
RN [15]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PROTEOLYTIC CLEAVAGE,
RP AND MUTAGENESIS OF ASP-442; ASP-448 AND ASP-484.
RX PubMed=24904167; DOI=10.1126/science.1252809;
RA Segawa K., Kurata S., Yanagihashi Y., Brummelkamp T.R., Matsuda F.,
RA Nagata S.;
RT "Caspase-mediated cleavage of phospholipid flippase for apoptotic
RT phosphatidylserine exposure.";
RL Science 344:1164-1168(2014).
RN [16]
RP FUNCTION IN PHOSPHATIDYLSERINE FLIPPING, INVOLVEMENT IN HAXL, VARIANT HAXL
RP ASN-418, AND CHARACTERIZATION OF VARIANT HAXL ASN-418.
RX PubMed=26944472; DOI=10.3324/haematol.2016.142273;
RA Arashiki N., Takakuwa Y., Mohandas N., Hale J., Yoshida K., Ogura H.,
RA Utsugisawa T., Ohga S., Miyano S., Ogawa S., Kojima S., Kanno H.;
RT "ATP11C is a major flippase in human erythrocytes and its defect causes
RT congenital hemolytic anemia.";
RL Haematologica 101:559-565(2016).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=26567335; DOI=10.1074/jbc.m115.690727;
RA Segawa K., Kurata S., Nagata S.;
RT "Human Type IV P-type ATPases That Work as Plasma Membrane Phospholipid
RT Flippases and Their Regulation by Caspase and Calcium.";
RL J. Biol. Chem. 291:762-772(2016).
RN [18]
RP SUBCELLULAR LOCATION, DOMAIN, PHOSPHORYLATION AT SER-1116, AND MUTAGENESIS
RP OF SER-1116; LEU-1120; LEU-1121; LEU-1122 AND SER-1126.
RX PubMed=29123098; DOI=10.1038/s41467-017-01338-1;
RA Takatsu H., Takayama M., Naito T., Takada N., Tsumagari K., Ishihama Y.,
RA Nakayama K., Shin H.W.;
RT "Phospholipid flippase ATP11C is endocytosed and downregulated following
RT Ca2+-mediated protein kinase C activation.";
RL Nat. Commun. 8:1423-1423(2017).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (3.90 ANGSTROMS) OF 13-1132 IN COMPLEX WITH TMEM30A
RP AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF GLN-66;
RP ARG-69; ASN-72; PHE-75; THR-93; VAL-101; VAL-352; LEU-353; ASN-355;
RP PHE-356; VAL-360; LYS-883; ASN-884 AND ASN-915.
RX PubMed=32493773; DOI=10.1074/jbc.ra120.014144;
RA Nakanishi H., Irie K., Segawa K., Hasegawa K., Fujiyoshi Y., Nagata S.,
RA Abe K.;
RT "Crystal structure of a human plasma membrane phospholipid flippase.";
RL J. Biol. Chem. 295:10180-10194(2020).
CC -!- FUNCTION: Catalytic component of a P4-ATPase flippase complex which
CC catalyzes the hydrolysis of ATP coupled to the transport of
CC aminophospholipids, phosphatidylserines (PS) and
CC phosphatidylethanolamines (PE), from the outer to the inner leaflet of
CC the plasma membrane (PubMed:25315773, PubMed:32493773, PubMed:24904167,
CC PubMed:26567335). Major PS-flippase in immune cell subsets. In
CC erythrocyte plasma membrane, it is required to maintain PS in the inner
CC leaflet preventing its exposure on the surface. This asymmetric
CC distribution is critical for the survival of erythrocytes in
CC circulation since externalized PS is a phagocytic signal for
CC erythrocyte clearance by splenic macrophages (PubMed:26944472).
CC Required for B cell differentiation past the pro-B cell stage (By
CC similarity). Seems to mediate PS flipping in pro-B cells (By
CC similarity). May be involved in the transport of cholestatic bile acids
CC (By similarity). {ECO:0000250|UniProtKB:Q9QZW0,
CC ECO:0000269|PubMed:24904167, ECO:0000269|PubMed:25315773,
CC ECO:0000269|PubMed:26944472, ECO:0000269|PubMed:32493773}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate +
CC phospholipidSide 2.; EC=7.6.2.1;
CC Evidence={ECO:0000269|PubMed:24904167, ECO:0000269|PubMed:25315773,
CC ECO:0000269|PubMed:26567335, ECO:0000269|PubMed:32493773};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O =
CC a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57262, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:24904167, ECO:0000269|PubMed:25315773,
CC ECO:0000269|PubMed:26567335, ECO:0000269|PubMed:32493773};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568;
CC Evidence={ECO:0000305|PubMed:24904167, ECO:0000305|PubMed:25315773,
CC ECO:0000305|PubMed:26567335, ECO:0000305|PubMed:32493773};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:24904167, ECO:0000269|PubMed:25315773,
CC ECO:0000269|PubMed:26567335, ECO:0000269|PubMed:32493773};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133;
CC Evidence={ECO:0000305|PubMed:24904167, ECO:0000305|PubMed:25315773,
CC ECO:0000305|PubMed:26567335, ECO:0000305|PubMed:32493773};
CC -!- ACTIVITY REGULATION: The flippase activity is inactivated by caspase-
CC mediated cleavage in apoptotic cells, allowing for PS exposure on the
CC cell surface and engulfment of apoptotic cells by macrophages. The
CC ATPase activity is up-regulated by aminophospholipids PS and PE and
CC down-regulated by Increasing intracellular Ca2+ levels.
CC {ECO:0000269|PubMed:24904167, ECO:0000269|PubMed:26567335}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 uM for ATP (in the presence of PS)
CC {ECO:0000269|PubMed:26567335};
CC KM=11 uM for ATP (in the presence of PE)
CC {ECO:0000269|PubMed:26567335};
CC Vmax=8.9 nmol/min/ug enzyme toward ATP (in the presence of PS)
CC {ECO:0000269|PubMed:26567335};
CC Vmax=6.7 nmol/min/ug enzyme toward ATP (in the presence of PE)
CC {ECO:0000269|PubMed:26567335};
CC -!- SUBUNIT: Component of a P4-ATPase flippase complex which consists of a
CC catalytic alpha subunit ATP11C and an accessory beta subunit TMEM30A.
CC {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:32493773}.
CC -!- INTERACTION:
CC Q8NB49; Q9NV96: TMEM30A; NbExp=2; IntAct=EBI-11279131, EBI-2836942;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21914794,
CC ECO:0000269|PubMed:25315773}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:25315773}; Multi-pass
CC membrane protein {ECO:0000255}. Early endosome membrane
CC {ECO:0000269|PubMed:29123098}; Multi-pass membrane protein
CC {ECO:0000255}. Recycling endosome membrane
CC {ECO:0000269|PubMed:29123098}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Efficient exit from the endoplasmic reticulum
CC requires the presence of TMEM30A. Internalized via clathrin-dependent
CC endocytosis in response to ca(2+) signaling induced by G-protein
CC coupled serotonin and histamine receptors.
CC {ECO:0000269|PubMed:29123098}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8NB49-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NB49-2; Sequence=VSP_007309;
CC Name=3;
CC IsoId=Q8NB49-3; Sequence=VSP_013373;
CC Name=4;
CC IsoId=Q8NB49-4; Sequence=VSP_013374;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:15533723,
CC ECO:0000269|PubMed:26567335}.
CC -!- DOMAIN: The di-leucine motif is required for sorting to clathrin-coated
CC endosomes upon ca(2+)-dependent PRKCA activation.
CC {ECO:0000269|PubMed:29123098}.
CC -!- PTM: Proteolytically cleaved by CASP3, CASP6 and CASP7.
CC {ECO:0000269|PubMed:24904167}.
CC -!- PTM: Phosphorylated at Ser-1116 likely by PRKCA; this creates a
CC functional di-leucine motif that is sufficient for endocytosis.
CC {ECO:0000269|PubMed:29123098}.
CC -!- DISEASE: Hemolytic anemia, congenital, X-linked (HAXL) [MIM:301015]: An
CC X-linked hematologic disease characterized by shortened survival of
CC erythrocytes due to congenital hemolysis that cannot be compensated by
CC bone marrow activity. Clinical features are mild jaundice and anemia.
CC Red cells morphology is normal. {ECO:0000269|PubMed:26944472}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IV subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03692.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC86172.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC86377.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD18440.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ580093; CAE30472.1; -; mRNA.
DR EMBL; AJ580094; CAE30473.1; -; mRNA.
DR EMBL; AL161777; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL590077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK091552; BAC03692.1; ALT_INIT; mRNA.
DR EMBL; AK125474; BAC86172.1; ALT_INIT; mRNA.
DR EMBL; AK125986; BAC86377.1; ALT_INIT; mRNA.
DR EMBL; AK131262; BAD18440.1; ALT_INIT; mRNA.
DR CCDS; CCDS14668.1; -. [Q8NB49-1]
DR CCDS; CCDS35410.1; -. [Q8NB49-3]
DR RefSeq; NP_001010986.1; NM_001010986.2. [Q8NB49-3]
DR RefSeq; NP_775965.2; NM_173694.4. [Q8NB49-1]
DR PDB; 6LKN; X-ray; 3.90 A; A/E/I/M=13-1132.
DR PDB; 7BSP; EM; 4.00 A; A=13-1094.
DR PDB; 7BSQ; EM; 3.20 A; A=13-1094.
DR PDB; 7BSS; EM; 3.30 A; A=13-1094.
DR PDB; 7BSU; EM; 3.20 A; A=13-1094.
DR PDB; 7BSV; EM; 3.00 A; A=13-1094.
DR PDB; 7BSW; EM; 3.90 A; A=13-1094.
DR PDB; 7VSG; EM; 3.90 A; A=13-1094.
DR PDB; 7VSH; EM; 3.40 A; A=13-1094.
DR PDBsum; 6LKN; -.
DR PDBsum; 7BSP; -.
DR PDBsum; 7BSQ; -.
DR PDBsum; 7BSS; -.
DR PDBsum; 7BSU; -.
DR PDBsum; 7BSV; -.
DR PDBsum; 7BSW; -.
DR PDBsum; 7VSG; -.
DR PDBsum; 7VSH; -.
DR AlphaFoldDB; Q8NB49; -.
DR SMR; Q8NB49; -.
DR BioGRID; 130370; 90.
DR ComplexPortal; CPX-6312; ATP11C-CDC50A P4-ATPase complex.
DR IntAct; Q8NB49; 35.
DR MINT; Q8NB49; -.
DR STRING; 9606.ENSP00000332756; -.
DR TCDB; 3.A.3.8.14; the p-type atpase (p-atpase) superfamily.
DR TCDB; 8.A.17.1.1; the na(+) channel auxiliary subunit Beta1-Beta4 (sca-Beta) family.
DR iPTMnet; Q8NB49; -.
DR PhosphoSitePlus; Q8NB49; -.
DR SwissPalm; Q8NB49; -.
DR BioMuta; ATP11C; -.
DR DMDM; 62512178; -.
DR EPD; Q8NB49; -.
DR jPOST; Q8NB49; -.
DR MassIVE; Q8NB49; -.
DR MaxQB; Q8NB49; -.
DR PaxDb; Q8NB49; -.
DR PeptideAtlas; Q8NB49; -.
DR PRIDE; Q8NB49; -.
DR ProteomicsDB; 72731; -. [Q8NB49-1]
DR ProteomicsDB; 72732; -. [Q8NB49-2]
DR ProteomicsDB; 72733; -. [Q8NB49-3]
DR ProteomicsDB; 72734; -. [Q8NB49-4]
DR Antibodypedia; 30516; 103 antibodies from 22 providers.
DR DNASU; 286410; -.
DR Ensembl; ENST00000327569.7; ENSP00000332756.3; ENSG00000101974.15. [Q8NB49-1]
DR Ensembl; ENST00000361648.6; ENSP00000355165.2; ENSG00000101974.15. [Q8NB49-3]
DR GeneID; 286410; -.
DR KEGG; hsa:286410; -.
DR UCSC; uc004faz.4; human. [Q8NB49-1]
DR CTD; 286410; -.
DR DisGeNET; 286410; -.
DR GeneCards; ATP11C; -.
DR HGNC; HGNC:13554; ATP11C.
DR HPA; ENSG00000101974; Tissue enhanced (liver).
DR MalaCards; ATP11C; -.
DR MIM; 300516; gene.
DR MIM; 301015; phenotype.
DR neXtProt; NX_Q8NB49; -.
DR OpenTargets; ENSG00000101974; -.
DR PharmGKB; PA25103; -.
DR VEuPathDB; HostDB:ENSG00000101974; -.
DR eggNOG; KOG0206; Eukaryota.
DR GeneTree; ENSGT00940000158878; -.
DR HOGENOM; CLU_000846_3_1_1; -.
DR InParanoid; Q8NB49; -.
DR OMA; HGHTAYQ; -.
DR OrthoDB; 587717at2759; -.
DR PhylomeDB; Q8NB49; -.
DR TreeFam; TF326897; -.
DR BRENDA; 7.6.2.1; 2681.
DR PathwayCommons; Q8NB49; -.
DR Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR SignaLink; Q8NB49; -.
DR BioGRID-ORCS; 286410; 20 hits in 712 CRISPR screens.
DR ChiTaRS; ATP11C; human.
DR GenomeRNAi; 286410; -.
DR Pharos; Q8NB49; Tbio.
DR PRO; PR:Q8NB49; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q8NB49; protein.
DR Bgee; ENSG00000101974; Expressed in seminal vesicle and 185 other tissues.
DR ExpressionAtlas; Q8NB49; baseline and differential.
DR Genevisible; Q8NB49; HS.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IPI:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0090555; F:phosphatidylethanolamine flippase activity; IDA:UniProtKB.
DR GO; GO:0140346; F:phosphatidylserine flippase activity; IDA:UniProtKB.
DR GO; GO:0090556; F:phosphatidylserine floppase activity; IEA:RHEA.
DR GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
DR GO; GO:0045332; P:phospholipid translocation; IBA:GO_Central.
DR Gene3D; 3.40.1110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030363; ATP11C.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006539; P-type_ATPase_IV.
DR InterPro; IPR032631; P-type_ATPase_N.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR032630; P_typ_ATPase_c.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR PANTHER; PTHR24092:SF38; PTHR24092:SF38; 1.
DR Pfam; PF16212; PhoLip_ATPase_C; 1.
DR Pfam; PF16209; PhoLip_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01652; ATPase-Plipid; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cell membrane;
KW Disease variant; Endoplasmic reticulum; Endosome;
KW Hereditary hemolytic anemia; Lipid transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1132
FT /note="Phospholipid-transporting ATPase IG"
FT /id="PRO_0000046373"
FT TOPO_DOM 1..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 86
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 312..346
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..879
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 880..900
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 901..908
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 909..929
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 930..955
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 956..976
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 977..995
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 996..1016
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1017..1026
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1027..1047
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1048..1069
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1070..1090
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1091..1132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 1116..1121
FT /note="Di-leucine motif"
FT /evidence="ECO:0000269|PubMed:29123098"
FT ACT_SITE 412
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 819
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:32493773,
FT ECO:0007744|PDB:6LKN"
FT BINDING 823
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:32493773,
FT ECO:0007744|PDB:6LKN"
FT SITE 442..443
FT /note="Cleavage; by CASP3, CASP6 and CASP7"
FT /evidence="ECO:0000269|PubMed:24904167"
FT SITE 448..449
FT /note="Cleavage; by CASP3"
FT /evidence="ECO:0000269|PubMed:24904167"
FT SITE 484..485
FT /note="Cleavage; by CASP3 and CASP7"
FT /evidence="ECO:0000269|PubMed:24904167"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1116
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29123098,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1100..1132
FT /note="RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL -> VHHLISSSA (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007309"
FT VAR_SEQ 1100..1132
FT /note="RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL -> NPNLELPMLLSYKHT
FT DSGYS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15533723"
FT /id="VSP_013373"
FT VAR_SEQ 1100..1132
FT /note="RNLSCRRASDSLSARPSVRPLLLRTFSDESNVL -> VTKRLPSSGTSAIFM
FT LSQTSSNHSFSWSE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_013374"
FT VARIANT 114
FT /note="C -> W (in dbSNP:rs2491014)"
FT /evidence="ECO:0000269|PubMed:15533723"
FT /id="VAR_021827"
FT VARIANT 157
FT /note="T -> I (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036501"
FT VARIANT 418
FT /note="T -> N (in HAXL; decreased phosphatidylserine
FT translocation from the outer to the inner leaflet of
FT erythrocytes cell membrane; dbSNP:rs1556323334)"
FT /evidence="ECO:0000269|PubMed:26944472"
FT /id="VAR_081016"
FT VARIANT 522
FT /note="Y -> C (in dbSNP:rs17281983)"
FT /id="VAR_055546"
FT VARIANT 931
FT /note="Q -> P (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036502"
FT VARIANT 972
FT /note="V -> M (in dbSNP:rs55724992)"
FT /id="VAR_061036"
FT MUTAGEN 66
FT /note="Q->A: Decreases ATPase activity."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 69
FT /note="R->A: Decreases ATPase activity."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 72
FT /note="N->A: Decreases ATPase activity."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 75
FT /note="F->A: Impairs ATPase flippase activity."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 93
FT /note="T->A: Decreases ATPase activity."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 101
FT /note="V->A: Impairs ATPase flippase activity."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 184
FT /note="E->Q: Has no effect on endoplasmic reticulum to
FT plasma membrane trafficking. Impairs ATPase flippase
FT activity."
FT /evidence="ECO:0000269|PubMed:25315773"
FT MUTAGEN 352
FT /note="V->F: Impairs ATPase flippase activity."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 353
FT /note="L->F: Decreases ATPase activity."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 355
FT /note="N->A: Impairs ATPase flippase activity."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 356
FT /note="F->N: Has no effect on ATPase flippase activity."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 360
FT /note="V->F: Decreases ATPase flippase activity."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 360
FT /note="V->I: Has minor effect on ATPase flippase activity."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 412
FT /note="D->N: Impairs endoplasmic reticulum to plasma
FT membrane trafficking."
FT /evidence="ECO:0000269|PubMed:25315773"
FT MUTAGEN 442
FT /note="D->A: Impairs caspase-mediated cleavage; when
FT associated with A-448 and A-484."
FT /evidence="ECO:0000269|PubMed:24904167"
FT MUTAGEN 448
FT /note="D->A: Impairs caspase-mediated cleavage; when
FT associated with A-442 and A-484."
FT /evidence="ECO:0000269|PubMed:24904167"
FT MUTAGEN 484
FT /note="D->A: Impairs caspase-mediated cleavage; when
FT associated with A-442 and A-448."
FT /evidence="ECO:0000269|PubMed:24904167"
FT MUTAGEN 883
FT /note="K->A: Decreases ATPase flippase activity."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 884
FT /note="N->A: Decreases ATPase flippase activity."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 915
FT /note="N->A: Decreases ATPase flippase activity."
FT /evidence="ECO:0000269|PubMed:32493773"
FT MUTAGEN 1116
FT /note="S->A: Impairs sorting to endosomal compartments in
FT response to ca(2+) signaling."
FT /evidence="ECO:0000269|PubMed:29123098"
FT MUTAGEN 1116
FT /note="S->D: Localizes to endosomal compartments in the
FT absence of ca(2+) signaling."
FT /evidence="ECO:0000269|PubMed:29123098"
FT MUTAGEN 1120
FT /note="L->A: Impairs sorting to endosomal compartments in
FT response to ca(2+) signaling."
FT /evidence="ECO:0000269|PubMed:29123098"
FT MUTAGEN 1121
FT /note="L->A: Impairs sorting to endosomal compartments in
FT response to ca(2+) signaling."
FT /evidence="ECO:0000269|PubMed:29123098"
FT MUTAGEN 1122
FT /note="L->A: Has no effect on sorting to endosomal
FT compartments in response to ca(2+) signaling."
FT /evidence="ECO:0000269|PubMed:29123098"
FT MUTAGEN 1126
FT /note="S->A: Decreases sorting to endosomal compartments in
FT response to ca(2+) signaling."
FT /evidence="ECO:0000269|PubMed:29123098"
FT CONFLICT 537
FT /note="L -> P (in Ref. 3; BAC86377)"
FT /evidence="ECO:0000305"
FT CONFLICT 873
FT /note="I -> V (in Ref. 3; BAC86377)"
FT /evidence="ECO:0000305"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 92..123
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:7BSV"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:7BSQ"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:7VSH"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:7BSV"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 286..316
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 333..336
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 339..354
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 360..373
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 375..379
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 381..385
FT /evidence="ECO:0007829|PDB:7BSV"
FT TURN 386..389
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 397..402
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:7BSV"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 423..429
FT /evidence="ECO:0007829|PDB:7BSQ"
FT STRAND 459..461
FT /evidence="ECO:0007829|PDB:7BSQ"
FT HELIX 462..470
FT /evidence="ECO:0007829|PDB:7BSQ"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:7BSQ"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:7BSQ"
FT HELIX 499..510
FT /evidence="ECO:0007829|PDB:7BSQ"
FT STRAND 519..523
FT /evidence="ECO:0007829|PDB:7BSQ"
FT STRAND 528..530
FT /evidence="ECO:0007829|PDB:7BSQ"
FT STRAND 535..541
FT /evidence="ECO:0007829|PDB:7BSQ"
FT TURN 545..547
FT /evidence="ECO:0007829|PDB:7BSQ"
FT STRAND 549..555
FT /evidence="ECO:0007829|PDB:7BSQ"
FT STRAND 561..567
FT /evidence="ECO:0007829|PDB:7BSQ"
FT TURN 570..572
FT /evidence="ECO:0007829|PDB:7BSQ"
FT TURN 573..575
FT /evidence="ECO:0007829|PDB:7VSH"
FT HELIX 578..580
FT /evidence="ECO:0007829|PDB:7BSQ"
FT HELIX 581..593
FT /evidence="ECO:0007829|PDB:7BSQ"
FT STRAND 597..606
FT /evidence="ECO:0007829|PDB:7BSQ"
FT HELIX 608..622
FT /evidence="ECO:0007829|PDB:7BSQ"
FT HELIX 628..636
FT /evidence="ECO:0007829|PDB:7BSQ"
FT STRAND 639..652
FT /evidence="ECO:0007829|PDB:7BSQ"
FT HELIX 659..668
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 672..676
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 681..688
FT /evidence="ECO:0007829|PDB:7BSV"
FT TURN 689..692
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 699..702
FT /evidence="ECO:0007829|PDB:7BSV"
FT TURN 705..707
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 710..712
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 713..722
FT /evidence="ECO:0007829|PDB:7BSV"
FT TURN 723..728
FT /evidence="ECO:0007829|PDB:7BSV"
FT TURN 747..749
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 750..755
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 756..764
FT /evidence="ECO:0007829|PDB:7BSV"
FT TURN 765..767
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 770..772
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 774..783
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 788..792
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 797..805
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 808..810
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 814..821
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 824..827
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 830..835
FT /evidence="ECO:0007829|PDB:7BSV"
FT TURN 843..847
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 848..851
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 853..855
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 857..862
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 865..893
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 894..896
FT /evidence="ECO:0007829|PDB:7BSV"
FT TURN 897..899
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 908..913
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 914..918
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 922..926
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 935..938
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 942..948
FT /evidence="ECO:0007829|PDB:7BSV"
FT TURN 949..951
FT /evidence="ECO:0007829|PDB:7BSU"
FT HELIX 952..954
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 956..980
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 982..984
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 986..989
FT /evidence="ECO:0007829|PDB:7BSQ"
FT HELIX 995..1017
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 1023..1043
FT /evidence="ECO:0007829|PDB:7BSV"
FT STRAND 1049..1052
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 1059..1062
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 1063..1065
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 1067..1079
FT /evidence="ECO:0007829|PDB:7BSV"
FT HELIX 1082..1090
FT /evidence="ECO:0007829|PDB:7BSV"
SQ SEQUENCE 1132 AA; 129477 MW; 74B63B20A5C6E49D CRC64;
MQMVPSLPPA SECAGEEKRV GTRTVFVGNH PVSETEAYIA QRFCDNRIVS SKYTLWNFLP
KNLFEQFRRI ANFYFLIIFL VQVTVDTPTS PVTSGLPLFF VITVTAIKQG YEDCLRHRAD
NEVNKSTVYI IENAKRVRKE SEKIKVGDVV EVQADETFPC DLILLSSCTT DGTCYVTTAS
LDGESNCKTH YAVRDTIALC TAESIDTLRA AIECEQPQPD LYKFVGRINI YSNSLEAVAR
SLGPENLLLK GATLKNTEKI YGVAVYTGME TKMALNYQGK SQKRSAVEKS INAFLIVYLF
ILLTKAAVCT TLKYVWQSTP YNDEPWYNQK TQKERETLKV LKMFTDFLSF MVLFNFIIPV
SMYVTVEMQK FLGSFFISWD KDFYDEEINE GALVNTSDLN EELGQVDYVF TDKTGTLTEN
SMEFIECCID GHKYKGVTQE VDGLSQTDGT LTYFDKVDKN REELFLRALC LCHTVEIKTN
DAVDGATESA ELTYISSSPD EIALVKGAKR YGFTFLGNRN GYMRVENQRK EIEEYELLHT
LNFDAVRRRM SVIVKTQEGD ILLFCKGADS AVFPRVQNHE IELTKVHVER NAMDGYRTLC
VAFKEIAPDD YERINRQLIE AKMALQDREE KMEKVFDDIE TNMNLIGATA VEDKLQDQAA
ETIEALHAAG LKVWVLTGDK METAKSTCYA CRLFQTNTEL LELTTKTIEE SERKEDRLHE
LLIEYRKKLL HEFPKSTRSF KKAWTEHQEY GLIIDGSTLS LILNSSQDSS SNNYKSIFLQ
ICMKCTAVLC CRMAPLQKAQ IVRMVKNLKG SPITLSIGDG ANDVSMILES HVGIGIKGKE
GRQAARNSDY SVPKFKHLKK LLLAHGHLYY VRIAHLVQYF FYKNLCFILP QFLYQFFCGF
SQQPLYDAAY LTMYNICFTS LPILAYSLLE QHINIDTLTS DPRLYMKISG NAMLQLGPFL
YWTFLAAFEG TVFFFGTYFL FQTASLEENG KVYGNWTFGT IVFTVLVFTV TLKLALDTRF
WTWINHFVIW GSLAFYVFFS FFWGGIIWPF LKQQRMYFVF AQMLSSVSTW LAIILLIFIS
LFPEILLIVL KNVRRRSARR NLSCRRASDS LSARPSVRPL LLRTFSDESN VL
