AP1AR_HUMAN
ID AP1AR_HUMAN Reviewed; 302 AA.
AC Q63HQ0; B2RCV7; Q96GG6; Q9H0V0; Q9P1L4;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=AP-1 complex-associated regulatory protein;
DE AltName: Full=2c18;
DE AltName: Full=Adaptor-related protein complex 1-associated regulatory protein;
DE AltName: Full=Gamma-1-adaptin brefeldin A resistance protein;
DE Short=GBAR;
DE Short=Gamma-BAR;
DE AltName: Full=Gamma-A1-adaptin and kinesin interactor;
DE Short=Gadkin;
GN Name=AP1AR; Synonyms=C4orf16; ORFNames=PRO0971;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Endometrium, and Fetal brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Pancreas;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-302.
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 121 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AP1G1.
RX PubMed=15775984; DOI=10.1038/sj.emboj.7600600;
RA Neubrand V.E., Will R.D., Moebius W., Poustka A., Wiemann S., Schu P.,
RA Dotti C.G., Pepperkok R., Simpson J.C.;
RT "Gamma-BAR, a novel AP-1-interacting protein involved in post-Golgi
RT trafficking.";
RL EMBO J. 24:1122-1133(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-228, 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [10]
RP FUNCTION, INTERACTION WITH AP1G1; KIF5B AND KLC2, AND MUTAGENESIS OF
RP TRP-210.
RX PubMed=19706427; DOI=10.1073/pnas.0904268106;
RA Schmidt M.R., Maritzen T., Kukhtina V., Higman V.A., Doglio L., Barak N.N.,
RA Strauss H., Oschkinat H., Dotti C.G., Haucke V.;
RT "Regulation of endosomal membrane traffic by a Gadkin/AP-1/kinesin KIF5
RT complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15344-15349(2009).
RN [11]
RP PALMITOYLATION, SUBCELLULAR LOCATION, INTERACTION WITH AP1G1, AND
RP MUTAGENESIS OF 4-CYS-CYS-5; CYS-9; TRP-260 AND PHE-264.
RX PubMed=19965873; DOI=10.1074/jbc.m109.049197;
RA Maritzen T., Schmidt M.R., Kukhtina V., Higman V.A., Strauss H.,
RA Volkmer R., Oschkinat H., Dotti C.G., Haucke V.;
RT "A novel subtype of AP-1-binding motif within the palmitoylated trans-Golgi
RT network/endosomal accessory protein Gadkin/gamma-BAR.";
RL J. Biol. Chem. 285:4074-4086(2010).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21525240; DOI=10.1091/mbc.e11-03-0193;
RA Laulagnier K., Schieber N.L., Maritzen T., Haucke V., Parton R.G.,
RA Gruenberg J.;
RT "Role of AP1 and Gadkin in the traffic of secretory endo-lysosomes.";
RL Mol. Biol. Cell 22:2068-2082(2011).
RN [13]
RP FUNCTION, ASSOCIATION WITH THE ARP2/3 COMPLEX, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF TRP-210.
RX PubMed=22689987; DOI=10.1073/pnas.1206468109;
RA Maritzen T., Zech T., Schmidt M.R., Krause E., Machesky L.M., Haucke V.;
RT "Gadkin negatively regulates cell spreading and motility via sequestration
RT of the actin-nucleating ARP2/3 complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:10382-10387(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-226 AND THR-228, AND
RP 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).
CC -!- FUNCTION: Necessary for adaptor protein complex 1 (AP-1)-dependent
CC transport between the trans-Golgi network and endosomes. Regulates the
CC membrane association of AP1G1/gamma1-adaptin, one of the subunits of
CC the AP-1 adaptor complex. The direct interaction with AP1G1/gamma1-
CC adaptin attenuates the release of the AP-1 complex from membranes.
CC Regulates endosomal membrane traffic via association with AP-1 and
CC KIF5B thus linking kinesin-based plus-end-directed microtubular
CC transport to AP-1-dependent membrane traffic. May act as effector of
CC AP-1 in calcium-induced endo-lysosome secretion. Inhibits Arp2/3
CC complex function; negatively regulates cell spreading, size and
CC motility via intracellular sequestration of the Arp2/3 complex.
CC {ECO:0000269|PubMed:15775984, ECO:0000269|PubMed:19706427,
CC ECO:0000269|PubMed:21525240, ECO:0000269|PubMed:22689987}.
CC -!- SUBUNIT: Interacts (via coiled-coil domain) with AP1G1 (via GAE
CC domain). Interacts with KIF5B. Associates with the Arp2/3 complex.
CC {ECO:0000269|PubMed:15775984, ECO:0000269|PubMed:19706427,
CC ECO:0000269|PubMed:19965873}.
CC -!- INTERACTION:
CC Q63HQ0-2; Q07866-2: KLC1; NbExp=3; IntAct=EBI-12016808, EBI-11979975;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network. Late
CC endosome. Early endosome. Note=Localizes to the juxta-nuclear Golgi
CC region and to tubular structures throughout the cytoplasm, which are
CC highly mobile and cycle between the juxta-nuclear area and the cell
CC periphery.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q63HQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q63HQ0-2; Sequence=VSP_015339;
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:19965873}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF71037.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL136628; CAB66563.1; -; mRNA.
DR EMBL; BX647702; CAH56145.1; -; mRNA.
DR EMBL; AK315299; BAG37704.1; -; mRNA.
DR EMBL; AC109347; AAY40962.1; -; Genomic_DNA.
DR EMBL; BC009485; AAH09485.1; -; mRNA.
DR EMBL; AF116612; AAF71037.1; ALT_INIT; mRNA.
DR CCDS; CCDS3696.1; -. [Q63HQ0-1]
DR CCDS; CCDS47125.1; -. [Q63HQ0-2]
DR RefSeq; NP_001121898.1; NM_001128426.2. [Q63HQ0-2]
DR RefSeq; NP_061039.3; NM_018569.5. [Q63HQ0-1]
DR AlphaFoldDB; Q63HQ0; -.
DR SMR; Q63HQ0; -.
DR BioGRID; 120667; 23.
DR CORUM; Q63HQ0; -.
DR ELM; Q63HQ0; -.
DR IntAct; Q63HQ0; 6.
DR STRING; 9606.ENSP00000274000; -.
DR iPTMnet; Q63HQ0; -.
DR PhosphoSitePlus; Q63HQ0; -.
DR SwissPalm; Q63HQ0; -.
DR BioMuta; AP1AR; -.
DR DMDM; 73917693; -.
DR EPD; Q63HQ0; -.
DR jPOST; Q63HQ0; -.
DR MassIVE; Q63HQ0; -.
DR MaxQB; Q63HQ0; -.
DR PaxDb; Q63HQ0; -.
DR PeptideAtlas; Q63HQ0; -.
DR PRIDE; Q63HQ0; -.
DR ProteomicsDB; 65888; -. [Q63HQ0-1]
DR ProteomicsDB; 65889; -. [Q63HQ0-2]
DR Antibodypedia; 48718; 26 antibodies from 11 providers.
DR DNASU; 55435; -.
DR Ensembl; ENST00000274000.10; ENSP00000274000.5; ENSG00000138660.12. [Q63HQ0-1]
DR Ensembl; ENST00000309703.10; ENSP00000309023.6; ENSG00000138660.12. [Q63HQ0-2]
DR GeneID; 55435; -.
DR KEGG; hsa:55435; -.
DR MANE-Select; ENST00000274000.10; ENSP00000274000.5; NM_018569.6; NP_061039.3.
DR UCSC; uc003iaj.6; human. [Q63HQ0-1]
DR CTD; 55435; -.
DR DisGeNET; 55435; -.
DR GeneCards; AP1AR; -.
DR HGNC; HGNC:28808; AP1AR.
DR HPA; ENSG00000138660; Low tissue specificity.
DR MIM; 610851; gene.
DR neXtProt; NX_Q63HQ0; -.
DR OpenTargets; ENSG00000138660; -.
DR PharmGKB; PA165663153; -.
DR VEuPathDB; HostDB:ENSG00000138660; -.
DR eggNOG; ENOG502QQP6; Eukaryota.
DR GeneTree; ENSGT00390000002219; -.
DR HOGENOM; CLU_088812_0_0_1; -.
DR InParanoid; Q63HQ0; -.
DR OMA; PNTEYSW; -.
DR PhylomeDB; Q63HQ0; -.
DR TreeFam; TF335676; -.
DR PathwayCommons; Q63HQ0; -.
DR SignaLink; Q63HQ0; -.
DR BioGRID-ORCS; 55435; 8 hits in 1074 CRISPR screens.
DR ChiTaRS; AP1AR; human.
DR GeneWiki; AP1AR; -.
DR GenomeRNAi; 55435; -.
DR Pharos; Q63HQ0; Tbio.
DR PRO; PR:Q63HQ0; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q63HQ0; protein.
DR Bgee; ENSG00000138660; Expressed in cortical plate and 191 other tissues.
DR ExpressionAtlas; Q63HQ0; baseline and differential.
DR Genevisible; Q63HQ0; HS.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0030133; C:transport vesicle; IDA:LIFEdb.
DR GO; GO:0035650; F:AP-1 adaptor complex binding; IDA:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; IDA:UniProtKB.
DR GO; GO:2000146; P:negative regulation of cell motility; IEA:Ensembl.
DR GO; GO:0001920; P:negative regulation of receptor recycling; IMP:UniProtKB.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IMP:MGI.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IEA:Ensembl.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0048203; P:vesicle targeting, trans-Golgi to endosome; IDA:UniProtKB.
DR InterPro; IPR031483; AP1AR.
DR PANTHER; PTHR34529; PTHR34529; 1.
DR Pfam; PF15745; AP1AR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Endosome; Golgi apparatus; Lipoprotein;
KW Palmitate; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..302
FT /note="AP-1 complex-associated regulatory protein"
FT /id="PRO_0000089432"
FT REGION 78..138
FT /note="Interaction with AP1G1"
FT REGION 188..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..215
FT /note="Sufficient for association with the Arp2/3 complex"
FT COILED 80..138
FT /evidence="ECO:0000255"
FT COMPBIAS 188..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 228
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 94..126
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015339"
FT VARIANT 297
FT /note="T -> I (in dbSNP:rs34900583)"
FT /id="VAR_050769"
FT MUTAGEN 4..5
FT /note="CC->SS: Loss of association with membranes, no
FT effect on interaction with AP1G1; when associated with 9-
FT S."
FT /evidence="ECO:0000269|PubMed:19965873"
FT MUTAGEN 9
FT /note="C->S: Loss of association with membranes, no effect
FT on interaction with AP1G1; when associated with 4-S-S-5."
FT /evidence="ECO:0000269|PubMed:19965873"
FT MUTAGEN 210
FT /note="W->A: Loss of association with the Arp2/3 complex
FT and endosomal colocalization. Abolishes interaction with
FT KLC2, no effect on interaction with AP1G1."
FT /evidence="ECO:0000269|PubMed:19706427,
FT ECO:0000269|PubMed:22689987"
FT MUTAGEN 260
FT /note="W->L: Decreases interaction with AP1G1; when
FT associated with L-264."
FT /evidence="ECO:0000269|PubMed:19965873"
FT MUTAGEN 264
FT /note="F->L: Decreases interaction with AP1G1; when
FT associated with L-260."
FT /evidence="ECO:0000269|PubMed:19965873"
FT CONFLICT 89
FT /note="K -> E (in Ref. 1; CAB66563)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="N -> D (in Ref. 2; BAG37704)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="K -> E (in Ref. 4; AAH09485)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 302 AA; 34280 MW; 0827B5EC95DC133A CRC64;
MGNCCWTQCF GLLRKEAGRL QRVGGGGGSK YFRTCSRGEH LTIEFENLVE SDEGESPGSS
HRPLTEEEIV DLRERHYDSI AEKQKDLDKK IQKELALQEE KLRLEEEALY AAQREAARAA
KQRKLLEQER QRIVQQYHPS NNGEYQSSGP EDDFESCLRN MKSQYEVFRS SRLSSDATVL
TPNTESSCDL MTKTKSTSGN DDSTSLDLEW EDEEGMNRML PMRERSKTEE DILRAALKYS
NKKTGSNPTS ASDDSNGLEW ENDFVSAEMD DNGNSEYSGF VNPVLELSDS GIRHSDTDQQ
TR
