CBAR1_HUMAN
ID CBAR1_HUMAN Reviewed; 289 AA.
AC A1XBS5; A1XBS4; Q32ND3; Q6AHW7; Q8N8R1; Q96L09;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=CBY1-interacting BAR domain-containing protein 1 {ECO:0000312|HGNC:HGNC:30452};
DE Flags: Precursor;
GN Name=CIBAR1 {ECO:0000312|HGNC:HGNC:30452}; Synonyms=FAM92A, FAM92A1;
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 2), AND SUBCELLULAR LOCATION
RP (ISOFORM 3).
RX PubMed=17646714;
RA Ruan X.Z., Yan F., Zhao X.Y., Wang C.T., Song M., Yang H.S., Deng H.X.,
RA Wei Y.Q.;
RT "Identification and characterization of two novel variants of the DUF1208
RT protein FAM92A1.";
RL Mol. Cells 23:391-397(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP INTERACTION WITH CBY1, SUBCELLULAR LOCATION, FUNCTION, SUBUNIT, AND
RP MUTAGENESIS OF LYS-107; ARG-110; LYS-114; ARG-132; ARG-134 AND ARG-136.
RX PubMed=27528616; DOI=10.1128/mcb.00160-16;
RA Li F.Q., Chen X., Fisher C., Siller S.S., Zelikman K., Kuriyama R.,
RA Takemaru K.I.;
RT "BAR domain-containing FAM92 proteins interact with chibby1 to facilitate
RT ciliogenesis.";
RL Mol. Cell. Biol. 36:2668-2680(2016).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CBY1, SUBUNIT, INVOLVEMENT
RP IN PAPA9, VARIANT PAPA9 160-ARG--LYS-289 DEL, AND CHARACTERIZATION OF
RP VARIANT PAPA9 160-ARG--LYS-289 DEL.
RX PubMed=30395363; DOI=10.1002/jbmr.3594;
RA Schrauwen I., Giese A.P., Aziz A., Lafont D.T., Chakchouk I.,
RA Santos-Cortez R.L.P., Lee K., Acharya A., Khan F.S., Ullah A.,
RA Nickerson D.A., Bamshad M.J., Ali G., Riazuddin S., Ansar M., Ahmad W.,
RA Ahmed Z.M., Leal S.M.;
RT "FAM92A underlies nonsyndromic postaxial polydactyly in humans and an
RT abnormal limb and digit skeletal phenotype in mice.";
RL J. Bone Miner. Res. 34:375-386(2019).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, TRANSIT PEPTIDE, AND MUTAGENESIS
RP OF LYS-107; LYS-109; ARG-110; ARG-132; ARG-134; ARG-136; ARG-264; ARG-266
RP AND LYS-267.
RX PubMed=30404948; DOI=10.1083/jcb.201806191;
RA Wang L., Yan Z., Vihinen H., Eriksson O., Wang W., Soliymani R., Lu Y.,
RA Xue Y., Jokitalo E., Li J., Zhao H.;
RT "FAM92A1 is a BAR domain protein required for mitochondrial ultrastructure
RT and function.";
RL J. Cell Biol. 218:97-111(2019).
CC -!- FUNCTION: Acts as a positive regulator of ciliary hedgehog signaling
CC (By similarity). Probable regulator of ciliogenesis involved in limb
CC morphogenesis (PubMed:27528616, PubMed:30395363). In cooperation with
CC CBY1 it is involved in the recruitment and fusion of endosomal vesicles
CC at distal appendages during early stages of ciliogenesis
CC (PubMed:27528616, PubMed:30395363). Plays an important role in the
CC mitochondrial function and is essential for maintaining mitochondrial
CC morphology and inner membrane ultrastructure (PubMed:30404948). In
CC vitro, can generate membrane curvature through preferential interaction
CC with negatively charged phospholipids such as phosphatidylinositol 4,5-
CC bisphosphate and cardiolipin and hence orchestrate cristae shape
CC (PubMed:30404948). {ECO:0000250|UniProtKB:Q8BP22,
CC ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:30395363,
CC ECO:0000269|PubMed:30404948}.
CC -!- SUBUNIT: Homodimer (via BAR-like domain) (PubMed:27528616,
CC PubMed:30395363). Heterodimer with FAM92B (via BAR-like domains)
CC (PubMed:27528616). Interacts (via BAR-like domain) with CBY1; this
CC interaction is required for targeting FAM92A to centriole and cilium
CC basal body (PubMed:27528616, PubMed:30395363).
CC {ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:30395363}.
CC -!- INTERACTION:
CC A1XBS5; Q9Y3M2: CBY1; NbExp=3; IntAct=EBI-2349888, EBI-947308;
CC A1XBS5-3; Q9Y3M2: CBY1; NbExp=3; IntAct=EBI-12348777, EBI-947308;
CC A1XBS5-3; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-12348777, EBI-11524851;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27528616,
CC ECO:0000269|PubMed:30404948}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:27528616}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000269|PubMed:27528616, ECO:0000269|PubMed:30395363}. Cell
CC projection, cilium {ECO:0000250|UniProtKB:Q8BP22}. Nucleus
CC {ECO:0000269|PubMed:30404948}. Mitochondrion inner membrane
CC {ECO:0000269|PubMed:30404948}; Peripheral membrane protein
CC {ECO:0000269|PubMed:30404948}; Matrix side
CC {ECO:0000269|PubMed:30404948}. Note=Weak punctate vesicular
CC distribution throughout the cytoplasm (PubMed:27528616). Localizes at
CC the distal end of mother centrioles (PubMed:27528616). Extensive
CC colocalization with CBY1 at mother centrioles (PubMed:27528616).
CC {ECO:0000269|PubMed:27528616}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus
CC {ECO:0000269|PubMed:17646714}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=FAM92A1-289 {ECO:0000303|PubMed:17646714};
CC IsoId=A1XBS5-1; Sequence=Displayed;
CC Name=2; Synonyms=FAM92A1-251 {ECO:0000303|PubMed:17646714};
CC IsoId=A1XBS5-2; Sequence=VSP_025294;
CC Name=3;
CC IsoId=A1XBS5-3; Sequence=VSP_025296;
CC Name=4;
CC IsoId=A1XBS5-4; Sequence=VSP_025295;
CC Name=5;
CC IsoId=A1XBS5-5; Sequence=VSP_025292, VSP_025293;
CC -!- DOMAIN: The BAR-like domain displays limited similarity to other BAR
CC domains. {ECO:0000305|PubMed:27528616}.
CC -!- DISEASE: Polydactyly, postaxial, A9 (PAPA9) [MIM:618219]: A form of
CC postaxial polydactyly, a condition characterized by the occurrence of
CC supernumerary digits in the upper and/or lower extremities. In
CC postaxial polydactyly type A, the extra digit is well-formed and
CC articulates with the fifth or a sixth metacarpal/metatarsal. PAPA9 is
CC an autosomal recessive condition characterized by one or more posterior
CC or postaxial digits. {ECO:0000269|PubMed:30395363}. Note=The disease
CC may be caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CIBAR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH14598.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI08708.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; DQ327715; ABC55436.1; -; mRNA.
DR EMBL; DQ327716; ABC55437.1; -; mRNA.
DR EMBL; AK096298; BAC04753.1; -; mRNA.
DR EMBL; CR627475; CAH10675.1; -; mRNA.
DR EMBL; AC010834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC120053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014598; AAH14598.2; ALT_INIT; mRNA.
DR EMBL; BC108707; AAI08708.1; ALT_INIT; mRNA.
DR CCDS; CCDS47892.1; -. [A1XBS5-1]
DR CCDS; CCDS64933.1; -. [A1XBS5-2]
DR RefSeq; NP_001269963.1; NM_001283034.1. [A1XBS5-2]
DR RefSeq; NP_660312.2; NM_145269.4. [A1XBS5-1]
DR AlphaFoldDB; A1XBS5; -.
DR SMR; A1XBS5; -.
DR BioGRID; 126476; 26.
DR IntAct; A1XBS5; 7.
DR MINT; A1XBS5; -.
DR STRING; 9606.ENSP00000429367; -.
DR iPTMnet; A1XBS5; -.
DR PhosphoSitePlus; A1XBS5; -.
DR BioMuta; FAM92A; -.
DR EPD; A1XBS5; -.
DR jPOST; A1XBS5; -.
DR MassIVE; A1XBS5; -.
DR MaxQB; A1XBS5; -.
DR PaxDb; A1XBS5; -.
DR PeptideAtlas; A1XBS5; -.
DR PRIDE; A1XBS5; -.
DR ProteomicsDB; 157; -. [A1XBS5-1]
DR ProteomicsDB; 158; -. [A1XBS5-2]
DR ProteomicsDB; 159; -. [A1XBS5-3]
DR ProteomicsDB; 160; -. [A1XBS5-4]
DR ProteomicsDB; 161; -. [A1XBS5-5]
DR Antibodypedia; 25708; 127 antibodies from 22 providers.
DR DNASU; 137392; -.
DR Ensembl; ENST00000423990.6; ENSP00000401774.2; ENSG00000188343.14. [A1XBS5-2]
DR Ensembl; ENST00000452913.6; ENSP00000391671.2; ENSG00000188343.14. [A1XBS5-3]
DR Ensembl; ENST00000518116.5; ENSP00000428065.1; ENSG00000188343.14. [A1XBS5-4]
DR Ensembl; ENST00000518322.6; ENSP00000429367.1; ENSG00000188343.14. [A1XBS5-1]
DR GeneID; 137392; -.
DR KEGG; hsa:137392; -.
DR MANE-Select; ENST00000518322.6; ENSP00000429367.1; NM_145269.5; NP_660312.2.
DR UCSC; uc064onr.1; human. [A1XBS5-1]
DR CTD; 137392; -.
DR DisGeNET; 137392; -.
DR GeneCards; CIBAR1; -.
DR HGNC; HGNC:30452; CIBAR1.
DR HPA; ENSG00000188343; Tissue enriched (testis).
DR MalaCards; CIBAR1; -.
DR MIM; 617273; gene.
DR MIM; 618219; phenotype.
DR neXtProt; NX_A1XBS5; -.
DR OpenTargets; ENSG00000188343; -.
DR Orphanet; 93334; Postaxial polydactyly type A.
DR VEuPathDB; HostDB:ENSG00000188343; -.
DR eggNOG; ENOG502QQ0N; Eukaryota.
DR GeneTree; ENSGT00390000010285; -.
DR HOGENOM; CLU_072172_1_0_1; -.
DR InParanoid; A1XBS5; -.
DR OMA; HIIAETE; -.
DR OrthoDB; 1324464at2759; -.
DR PhylomeDB; A1XBS5; -.
DR TreeFam; TF324316; -.
DR PathwayCommons; A1XBS5; -.
DR SignaLink; A1XBS5; -.
DR BioGRID-ORCS; 137392; 10 hits in 1042 CRISPR screens.
DR ChiTaRS; FAM92A; human.
DR GenomeRNAi; 137392; -.
DR Pharos; A1XBS5; Tbio.
DR PRO; PR:A1XBS5; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; A1XBS5; protein.
DR Bgee; ENSG00000188343; Expressed in left testis and 150 other tissues.
DR ExpressionAtlas; A1XBS5; baseline and differential.
DR Genevisible; A1XBS5; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IBA:GO_Central.
DR GO; GO:0097546; C:ciliary base; IDA:UniProtKB.
DR GO; GO:0035869; C:ciliary transition zone; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0030061; C:mitochondrial crista; IMP:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IMP:UniProtKB.
DR GO; GO:0035108; P:limb morphogenesis; IMP:UniProtKB.
DR GO; GO:0061024; P:membrane organization; IDA:UniProtKB.
DR GO; GO:0097749; P:membrane tubulation; IMP:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
DR CDD; cd07598; BAR_FAM92; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR035590; BAR_CBAR1/2.
DR InterPro; IPR009602; CBAR/FAM92.
DR PANTHER; PTHR21223; PTHR21223; 1.
DR Pfam; PF06730; FAM92; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Disease variant; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleus; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:30404948"
FT CHAIN 48..289
FT /note="CBY1-interacting BAR domain-containing protein 1"
FT /id="PRO_0000287080"
FT REGION 10..220
FT /note="BAR-like"
FT /evidence="ECO:0000305|PubMed:27528616"
FT REGION 265..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 107..178
FT /evidence="ECO:0000255"
FT VAR_SEQ 89..97
FT /note="ERLEAKVVE -> WSEITVSLL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_025292"
FT VAR_SEQ 98..289
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_025293"
FT VAR_SEQ 182..219
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17646714"
FT /id="VSP_025294"
FT VAR_SEQ 220..289
FT /note="VFRNSLYAPDYSSRLDIVRANSKSPLQRSLSAKCVSGTGQVSTCRLRKDQQA
FT EDDEDDELDVTEEENFLK -> RWSFAMLPRLVLNSWGSSDPPALASQSVRFSEILCMH
FT QIIHLV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025295"
FT VAR_SEQ 260..289
FT /note="VSTCRLRKDQQAEDDEDDELDVTEEENFLK -> EAGWAATCQTLI (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025296"
FT VARIANT 160..289
FT /note="Missing (in PAPA9; does not form homodimers; does
FT not interact with CBY1; does not localize to cilium basal
FT body)"
FT /evidence="ECO:0000269|PubMed:30395363"
FT /id="VAR_081578"
FT VARIANT 222
FT /note="R -> Q (in dbSNP:rs36117362)"
FT /id="VAR_062190"
FT MUTAGEN 107
FT /note="K->A: Reduced membrane-binding and significant
FT reduction in membrane remodeling activity; when associated
FT with A-109 and A-110."
FT /evidence="ECO:0000269|PubMed:30404948"
FT MUTAGEN 107
FT /note="K->E: Abolishes ability to induce membrane
FT remodeling in the presence of CBY1; when associated with E-
FT 110; E-114; E-132; E-134 and E-136."
FT /evidence="ECO:0000269|PubMed:27528616"
FT MUTAGEN 109
FT /note="K->A: Reduced membrane-binding and significant
FT reduction in membrane remodeling activity; when associated
FT with A-107 and A-110."
FT /evidence="ECO:0000269|PubMed:30404948"
FT MUTAGEN 110
FT /note="R->A: Reduced membrane-binding and significant
FT reduction in membrane remodeling activity; when associated
FT with A-107 and A-109."
FT /evidence="ECO:0000269|PubMed:30404948"
FT MUTAGEN 110
FT /note="R->E: Abolishes ability to induce membrane
FT remodeling in the presence of CBY1; when associated with E-
FT 107;E-114; E-132; E-134 and E-136."
FT /evidence="ECO:0000269|PubMed:27528616"
FT MUTAGEN 114
FT /note="K->E: Abolishes ability to induce membrane
FT remodeling in the presence of CBY1; when associated with E-
FT 107; E-110; E-132; E-134 and E-136."
FT /evidence="ECO:0000269|PubMed:27528616"
FT MUTAGEN 132
FT /note="R->A: Reduced membrane-binding and significant
FT reduction in membrane remodeling activity; when associated
FT with A-134 and A-136."
FT /evidence="ECO:0000269|PubMed:30404948"
FT MUTAGEN 132
FT /note="R->E: Abolishes ability to induce membrane
FT remodeling in the presence of CBY1; when associated with E-
FT 107; E-110; E-114; E-134 and E-136."
FT /evidence="ECO:0000269|PubMed:27528616"
FT MUTAGEN 134
FT /note="R->A: Reduced membrane-binding and significant
FT reduction in membrane remodeling activity; when associated
FT with A-132 and A-136."
FT /evidence="ECO:0000269|PubMed:30404948"
FT MUTAGEN 134
FT /note="R->E: Abolishes ability to induce membrane
FT remodeling in the presence of CBY1; when associated with E-
FT 107; E-110; E-114; E-132 and E-136."
FT /evidence="ECO:0000269|PubMed:27528616"
FT MUTAGEN 136
FT /note="R->A: Reduced membrane-binding and significant
FT reduction in membrane remodeling activity; when associated
FT with A-132 and A-134."
FT /evidence="ECO:0000269|PubMed:30404948"
FT MUTAGEN 136
FT /note="R->E: Abolishes ability to induce membrane
FT remodeling in the presence of CBY1; when associated with E-
FT 107; E-110; E-114; E-132 and E-134."
FT /evidence="ECO:0000269|PubMed:27528616"
FT MUTAGEN 264
FT /note="R->A: Reduced membrane-binding and significant
FT reduction in membrane remodeling activity; when associated
FT with A-266 and A-267."
FT /evidence="ECO:0000269|PubMed:30404948"
FT MUTAGEN 266
FT /note="R->A: Reduced membrane-binding and significant
FT reduction in membrane remodeling activity; when associated
FT with A-264 and A-267."
FT /evidence="ECO:0000269|PubMed:30404948"
FT MUTAGEN 267
FT /note="K->A: Reduced membrane-binding and significant
FT reduction in membrane remodeling activity; when associated
FT with A-264 and A-266."
FT /evidence="ECO:0000269|PubMed:30404948"
FT CONFLICT 137
FT /note="N -> S (in Ref. 1; ABC55436)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="E -> G (in Ref. 2; BAC04753)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="V -> I (in Ref. 1; ABC55437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 33431 MW; CC95F1A4217FDCA5 CRC64;
MMRRTLENRN AQTKQLQTAV SNVEKHFGEL CQIFAAYVRK TARLRDKADL LVNEINAYAA
TETPHLKLGL MNFADEFAKL QDYRQAEVER LEAKVVEPLK TYGTIVKMKR DDLKATLTAR
NREAKQLTQL ERTRQRNPSD RHVISQAETE LQRAAMDASR TSRHLEETIN NFERQKMKDI
KTIFSEFITI EMLFHGKALE VYTAAYQNIQ NIDEDEDLEV FRNSLYAPDY SSRLDIVRAN
SKSPLQRSLS AKCVSGTGQV STCRLRKDQQ AEDDEDDELD VTEEENFLK
