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Rabankyrin-5 (Rank-5) (Ankyrin repeat and FYVE domain-containing protein 1) (Ankyrin repeats hooked to a zinc finger motif)

 ANFY1_HUMAN             Reviewed;        1169 AA.
Q9P2R3; A8KA65; Q5RKV4; Q9ULG5;
04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
04-AUG-2003, sequence version 2.
25-APR-2018, entry version 150.
RecName: Full=Rabankyrin-5 {ECO:0000303|PubMed:15328530};
Short=Rank-5 {ECO:0000303|PubMed:22284051};
AltName: Full=Ankyrin repeat and FYVE domain-containing protein 1;
AltName: Full=Ankyrin repeats hooked to a zinc finger motif;
Name=ANKFY1; Synonyms=ANKHZN, KIAA1255;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Fetal brain;
PubMed=10940552; DOI=10.1016/S0378-1119(00)00247-X;
Kuriyama H., Asakawa S., Minoshima S., Maruyama H., Ishii N., Ito K.,
Gejyo F., Arakawa M., Shimizu N., Kuwano R.;
"Characterization and chromosomal mapping of a novel human gene,
ANKHZN.";
Gene 253:151-160(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=10574462; DOI=10.1093/dnares/6.5.337;
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:337-345(1999).
[3]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-458 (ISOFORM 1).
TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
PROTEIN SEQUENCE OF 2-11; 145-151 AND 924-931, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Lung carcinoma;
Bienvenut W.V., Vousden K.H., Lukashchuk N.;
Submitted (MAR-2008) to UniProtKB.
[9]
FUNCTION, INTERACTION WITH RAB5A, AND SUBCELLULAR LOCATION.
PubMed=15328530; DOI=10.1371/journal.pbio.0020261;
Schnatwinkel C., Christoforidis S., Lindsay M.R.,
Uttenweiler-Joseph S., Wilm M., Parton R.G., Zerial M.;
"The Rab5 effector Rabankyrin-5 regulates and coordinates different
endocytic mechanisms.";
PLoS Biol. 2:E261-E261(2004).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
FUNCTION, INTERACTION WITH EHD1 AND VPS26A, AND MUTAGENESIS OF
421-ASN--PHE-423 AND 424-GLU-ASP-425.
PubMed=22284051; DOI=10.1111/j.1600-0854.2012.01334.x;
Zhang J., Reiling C., Reinecke J.B., Prislan I., Marky L.A.,
Sorgen P.L., Naslavsky N., Caplan S.;
"Rabankyrin-5 interacts with EHD1 and Vps26 to regulate endocytic
trafficking and retromer function.";
Traffic 13:745-757(2012).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
FUNCTION IN ENDOSOMAL TRAFFICKING AND RECEPTOR INTERNALIZATION, AND
INTERACTION WITH RHOD.
PubMed=24102721; DOI=10.1111/tra.12121;
Nehru V., Voytyuk O., Lennartsson J., Aspenstroem P.;
"RhoD binds the Rab5 effector Rabankyrin-5 and has a role in
trafficking of the platelet-derived growth factor receptor.";
Traffic 14:1242-1254(2013).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Proposed effector of Rab5. Binds to phosphatidylinositol
3-phosphate (PI(3)P). Involved in homotypic early endosome fusion
and to a lesser extent in heterotypic fusion of chlathrin-coated
vesicles with early endosomes. Involved in macropinocytosis; the
function is dependent on Rab5-GTP. Required for correct endosomal
localization. Involved in the internalization and trafficking of
activated tyrosine kinase receptors such as PDGFRB. Regulates the
subcellular localization of the retromer complex in a EHD1-
dependent manner. Involved in endosome-to-Golgi transport and
biosynthetic transport to late endosomes and lysosomes indicative
for a regulation of retromer complex-mediated retrograde
transport. {ECO:0000269|PubMed:15328530,
ECO:0000269|PubMed:22284051, ECO:0000269|PubMed:24102721}.
-!- SUBUNIT: Interacts with RAB5A (in GTP-bound form). Interacts with
RHOD (independent of GTP-loaded status). Interacts with EHD1.
Interacts with VPS26A; the interaction is indepenedent of EHD1 and
is indicative for an association with the cargo recognition
subcomplex of the retromer complex. {ECO:0000269|PubMed:15328530,
ECO:0000269|PubMed:22284051, ECO:0000269|PubMed:24102721}.
-!- INTERACTION:
Q9H4M9:EHD1; NbExp=8; IntAct=EBI-2513908, EBI-490691;
Q9NZN3:EHD3; NbExp=3; IntAct=EBI-2513908, EBI-2870749;
P60520:GABARAPL2; NbExp=2; IntAct=EBI-2513908, EBI-720116;
P20339:RAB5A; NbExp=2; IntAct=EBI-2513908, EBI-399437;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10940552}.
Endosome membrane {ECO:0000269|PubMed:10940552}; Peripheral
membrane protein {ECO:0000269|PubMed:10940552}. Early endosome
{ECO:0000269|PubMed:15328530}. Note=Also associated with endosomal
membranes. Localizes to macropinosomes.
{ECO:0000269|PubMed:15328530}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9P2R3-1; Sequence=Displayed;
Name=2;
IsoId=Q9P2R3-2; Sequence=VSP_035607;
Name=4;
IsoId=Q9P2R3-4; Sequence=VSP_041447;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: High expression in whole adult brain and
intermediate expression in all other tissues and specific brain
regions examined, including fetal brain.
{ECO:0000269|PubMed:10574462, ECO:0000269|PubMed:10940552}.
-!- SEQUENCE CAUTION:
Sequence=AAH52308.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=BAA86569.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB037360; BAA90300.1; -; mRNA.
EMBL; AB033081; BAA86569.2; ALT_INIT; mRNA.
EMBL; AK292930; BAF85619.1; -; mRNA.
EMBL; AC087292; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC087742; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471108; EAW90448.1; -; Genomic_DNA.
EMBL; BC052308; AAH52308.1; ALT_SEQ; mRNA.
CCDS; CCDS42236.1; -. [Q9P2R3-2]
CCDS; CCDS58502.1; -. [Q9P2R3-4]
CCDS; CCDS82038.1; -. [Q9P2R3-1]
RefSeq; NP_001244928.1; NM_001257999.2. [Q9P2R3-4]
RefSeq; NP_001316992.1; NM_001330063.1. [Q9P2R3-1]
RefSeq; NP_057460.3; NM_016376.4. [Q9P2R3-2]
UniGene; Hs.696087; -.
ProteinModelPortal; Q9P2R3; -.
SMR; Q9P2R3; -.
BioGrid; 119564; 34.
DIP; DIP-46068N; -.
IntAct; Q9P2R3; 24.
STRING; 9606.ENSP00000459775; -.
iPTMnet; Q9P2R3; -.
PhosphoSitePlus; Q9P2R3; -.
BioMuta; ANKFY1; -.
DMDM; 33514905; -.
EPD; Q9P2R3; -.
MaxQB; Q9P2R3; -.
PaxDb; Q9P2R3; -.
PeptideAtlas; Q9P2R3; -.
PRIDE; Q9P2R3; -.
DNASU; 51479; -.
Ensembl; ENST00000341657; ENSP00000343362; ENSG00000185722. [Q9P2R3-1]
Ensembl; ENST00000570535; ENSP00000459943; ENSG00000185722. [Q9P2R3-4]
Ensembl; ENST00000574367; ENSP00000459775; ENSG00000185722. [Q9P2R3-2]
GeneID; 51479; -.
KEGG; hsa:51479; -.
UCSC; uc002fxn.4; human. [Q9P2R3-1]
CTD; 51479; -.
DisGeNET; 51479; -.
EuPathDB; HostDB:ENSG00000185722.16; -.
GeneCards; ANKFY1; -.
H-InvDB; HIX0013439; -.
H-InvDB; HIX0173682; -.
HGNC; HGNC:20763; ANKFY1.
HPA; HPA024513; -.
HPA; HPA024522; -.
HPA; HPA065849; -.
MIM; 607927; gene.
neXtProt; NX_Q9P2R3; -.
OpenTargets; ENSG00000185722; -.
PharmGKB; PA134984226; -.
eggNOG; KOG0504; Eukaryota.
eggNOG; KOG4591; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00910000144044; -.
HOGENOM; HOG000022583; -.
HOVERGEN; HBG050501; -.
InParanoid; Q9P2R3; -.
KO; K20129; -.
OMA; MLRWIYT; -.
OrthoDB; EOG091G0ITN; -.
PhylomeDB; Q9P2R3; -.
TreeFam; TF351263; -.
ChiTaRS; ANKFY1; human.
GeneWiki; ANKFY1; -.
GenomeRNAi; 51479; -.
PRO; PR:Q9P2R3; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000185722; -.
CleanEx; HS_ANKFY1; -.
ExpressionAtlas; Q9P2R3; baseline and differential.
Genevisible; Q9P2R3; HS.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005768; C:endosome; IDA:HPA.
GO; GO:0010008; C:endosome membrane; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
GO; GO:0044354; C:macropinosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:1901981; F:phosphatidylinositol phosphate binding; IDA:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; IDA:UniProtKB.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
GO; GO:0034058; P:endosomal vesicle fusion; IDA:UniProtKB.
GO; GO:0090160; P:Golgi to lysosome transport; IMP:UniProtKB.
GO; GO:0048549; P:positive regulation of pinocytosis; IDA:UniProtKB.
GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
CDD; cd00204; ANK; 7.
Gene3D; 1.25.40.20; -; 7.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR011333; SKP1/BTB/POZ_sf.
InterPro; IPR000306; Znf_FYVE.
InterPro; IPR017455; Znf_FYVE-rel.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF00023; Ank; 2.
Pfam; PF12796; Ank_2; 3.
Pfam; PF00651; BTB; 1.
Pfam; PF01363; FYVE; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 21.
SMART; SM00225; BTB; 1.
SMART; SM00064; FYVE; 1.
SUPFAM; SSF48403; SSF48403; 4.
SUPFAM; SSF54695; SSF54695; 1.
SUPFAM; SSF57903; SSF57903; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 12.
PROSITE; PS50097; BTB; 1.
PROSITE; PS50178; ZF_FYVE; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ANK repeat; Complete proteome;
Cytoplasm; Direct protein sequencing; Endocytosis; Endosome; Membrane;
Metal-binding; Phosphoprotein; Reference proteome; Repeat; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.8}.
CHAIN 2 1169 Rabankyrin-5.
/FTId=PRO_0000066890.
DOMAIN 68 130 BTB. {ECO:0000255|PROSITE-
ProRule:PRU00037}.
REPEAT 217 247 ANK 1.
REPEAT 255 284 ANK 2.
REPEAT 288 317 ANK 3.
REPEAT 322 362 ANK 4.
REPEAT 366 396 ANK 5.
REPEAT 490 519 ANK 6.
REPEAT 542 572 ANK 7.
REPEAT 588 617 ANK 8.
REPEAT 621 650 ANK 9.
REPEAT 654 683 ANK 10.
REPEAT 687 716 ANK 11.
REPEAT 724 753 ANK 12.
REPEAT 769 798 ANK 13.
REPEAT 802 832 ANK 14.
REPEAT 836 865 ANK 15.
REPEAT 870 899 ANK 16.
REPEAT 905 934 ANK 17.
REPEAT 938 967 ANK 18.
REPEAT 971 1001 ANK 19.
REPEAT 1005 1037 ANK 20.
REPEAT 1043 1072 ANK 21.
ZN_FING 1104 1164 FYVE-type. {ECO:0000255|PROSITE-
ProRule:PRU00091}.
REGION 650 759 Interaction with RHOD and RAB5A.
{ECO:0000269|PubMed:24102721}.
MOTIF 421 423 NPF.
MOD_RES 2 2 N-acetylalanine. {ECO:0000269|Ref.8}.
MOD_RES 270 270 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 4 MAEE -> MPTPRDCGRLRSRAGRSRAGAACSRGAPRAARE
ALDCRRCRDAGGK (in isoform 4).
{ECO:0000303|PubMed:10574462}.
/FTId=VSP_041447.
VAR_SEQ 650 650 V -> VS (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_035607.
MUTAGEN 421 423 NPF->APA: Disrupts interaction with EHD1.
{ECO:0000269|PubMed:22284051}.
MUTAGEN 424 425 ED->AA: Decreases interaction with EHD1.
{ECO:0000269|PubMed:22284051}.
CONFLICT 48 48 E -> K (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 115 115 M -> V (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 207 207 A -> P (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 235 235 F -> S (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 270 270 S -> N (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 283 291 DMVDKSGWS -> AWWPRVLE (in Ref. 1;
BAA90300). {ECO:0000305}.
CONFLICT 299 300 RG -> E (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 322 322 A -> C (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 336 337 KK -> RN (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 379 379 N -> D (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 385 385 Q -> H (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 645 645 Q -> R (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 652 654 TQD -> PQA (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 687 687 K -> E (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 713 713 D -> G (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 784 784 Missing (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 795 795 N -> D (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 798 798 A -> P (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 807 807 I -> C (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 827 829 DIH -> ISS (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 835 835 R -> K (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 849 849 N -> D (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 860 860 E -> G (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 874 874 F -> S (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 889 889 F -> S (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 901 901 V -> A (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 905 905 S -> P (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 913 913 A -> V (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 916 916 A -> E (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 933 933 N -> T (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 940 940 Q -> K (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 949 949 Q -> E (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 962 962 G -> A (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 1120 1120 T -> A (in Ref. 1; BAA90300).
{ECO:0000305}.
CONFLICT 1157 1157 N -> T (in Ref. 1; BAA90300).
{ECO:0000305}.
SEQUENCE 1169 AA; 128399 MW; 589297CA4ACDDB56 CRC64;
MAEEEVAKLE KHLMLLRQEY VKLQKKLAET EKRCALLAAQ ANKESSSESF ISRLLAIVAD
LYEQEQYSDL KIKVGDRHIS AHKFVLAARS DSWSLANLSS TKELDLSDAN PEVTMTMLRW
IYTDELEFRE DDVFLTELMK LANRFQLQLL RERCEKGVMS LVNVRNCIRF YQTAEELNAS
TLMNYCAEII ASHWDDLRKE DFSSMSAQLL YKMIKSKTEY PLHKAIKVER EDVVFLYLIE
MDSQLPGKLN EADHNGDLAL DLALSRRLES IATTLVSHKA DVDMVDKSGW SLLHKGIQRG
DLFAATFLIK NGAFVNAATL GAQETPLHLV ALYSSKKHSA DVMSEMAQIA EALLQAGANP
NMQDSKGRTP LHVSIMAGNE YVFSQLLQCK QLDLELKDHE GSTALWLAVQ HITVSSDQSV
NPFEDVPVVN GTSFDENSFA ARLIQRGSHT DAPDTATGNC LLQRAAGAGN EAAALFLATN
GAHVNHRNKW GETPLHTACR HGLANLTAEL LQQGANPNLQ TEEALPLPKE AASLTSLADS
VHLQTPLHMA IAYNHPDVVS VILEQKANAL HATNNLQIIP DFSLKDSRDQ TVLGLALWTG
MHTIAAQLLG SGAAINDTMS DGQTLLHMAI QRQDSKSALF LLEHQADINV RTQDGETALQ
LAIRNQLPLV VDAICTRGAD MSVPDEKGNP PLWLALANNL EDIASTLVRH GCDATCWGPG
PGGCLQTLLH RAIDENNEPT ACFLIRSGCD VNSPRQPGAN GEGEEEARDG QTPLHLAASW
GLEETVQCLL EFGANVNAQD AEGRTPIHVA ISSQHGVIIQ LLVSHPDIHL NVRDRQGLTP
FACAMTFKNN KSAEAILKRE SGAAEQVDNK GRNFLHVAVQ NSDIESVLFL ISVHANVNSR
VQDASKLTPL HLAVQAGSEI IVRNLLLAGA KVNELTKHRQ TALHLAAQQD LPTICSVLLE
NGVDFAAVDE NGNNALHLAV MHGRLNNIRV LLTECTVDAE AFNLRGQSPL HILGQYGKEN
AAAIFDLFLE CMPGYPLDKP DADGSTVLLL AYMKGNANLC RAIVRSGARL GVNNNQGVNI
FNYQVATKQL LFRLLDMLSK EPPWCDGSYC YECTARFGVT TRKHHCRHCG RLLCHKCSTK
EIPIIKFDLN KPVRVCNICF DVLTLGGVS


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