CORO7_HUMAN
ID CORO7_HUMAN Reviewed; 925 AA.
AC P57737; B4DFD6; B4DL18; I3L416; Q17RK4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Coronin-7;
DE Short=Crn7;
DE AltName: Full=70 kDa WD repeat tumor rejection antigen homolog;
GN Name=CORO7;
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] (ISOFORM 1).
RX PubMed=15327992; DOI=10.1016/j.febslet.2004.07.066;
RA Rybakin V., Stumpf M., Schulze A., Majoul I.V., Noegel A.A., Hasse A.;
RT "Coronin 7, the mammalian POD-1 homologue, localizes to the Golgi
RT apparatus.";
RL FEBS Lett. 573:161-167(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4), AND VARIANT
RP GLN-193.
RC TISSUE=Cerebellum, Hepatoma, and Tongue;
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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Colon, and Lymphoma;
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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH AP1 COMPLEX.
RX PubMed=16905771; DOI=10.1074/jbc.m604680200;
RA Rybakin V., Gounko N.V., Spaete K., Hoening S., Majoul I.V., Duden R.,
RA Noegel A.A.;
RT "Crn7 interacts with AP-1 and is required for the maintenance of Golgi
RT morphology and protein export from the Golgi.";
RL J. Biol. Chem. 281:31070-31078(2006).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP TISSUE SPECIFICITY.
RX PubMed=21130766; DOI=10.1016/j.febslet.2010.11.049;
RA Watanabe M., Suzuki T., Kim M., Abe Y., Yoshida Y., Sugano S., Yamamoto T.;
RT "Coronin7 forms a novel E3 ubiquitin ligase complex to promote the
RT degradation of the anti-proliferative protein Tob.";
RL FEBS Lett. 585:65-70(2011).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION AT LYS-472 AND LYS-680,
RP MUTAGENESIS OF LYS-472 AND LYS-680, AND INTERACTION WITH EPS15.
RX PubMed=24768539; DOI=10.1016/j.molcel.2014.03.035;
RA Yuan W.C., Lee Y.R., Lin S.Y., Chang L.Y., Tan Y.P., Hung C.C., Kuo J.C.,
RA Liu C.H., Lin M.Y., Xu M., Chen Z.J., Chen R.H.;
RT "K33-linked polyubiquitination of coronin 7 by Cul3-KLHL20 ubiquitin E3
RT ligase regulates protein trafficking.";
RL Mol. Cell 54:586-600(2014).
CC -!- FUNCTION: F-actin regulator involved in anterograde Golgi to endosome
CC transport: upon ubiquitination via 'Lys-33'-linked ubiquitin chains by
CC the BCR(KLHL20) E3 ubiquitin ligase complex, interacts with EPS15 and
CC localizes to the trans-Golgi network, where it promotes actin
CC polymerization, thereby facilitating post-Golgi trafficking. May play a
CC role in the maintenance of the Golgi apparatus morphology.
CC {ECO:0000269|PubMed:16905771, ECO:0000269|PubMed:24768539}.
CC -!- SUBUNIT: Interacts with clathrin adapter AP1 complex. This interaction
CC takes place at Golgi membranes and not AP1-positive endosomal
CC membranes. Interacts (when ubiquitinated at Lys-472) with EPS15.
CC {ECO:0000269|PubMed:16905771, ECO:0000269|PubMed:24768539}.
CC -!- INTERACTION:
CC P57737; Q61471: Tob1; Xeno; NbExp=3; IntAct=EBI-6916167, EBI-8527498;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane. Golgi apparatus, trans-
CC Golgi network. Cytoplasmic vesicle {ECO:0000250}. Cytoplasm, cytosol
CC {ECO:0000250}. Note=Predominantly cytosolic. Detected on vesicle-like
CC cytoplasmic structures and on the cis-Golgi. Not associated with actin
CC filaments.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P57737-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P57737-2; Sequence=VSP_038152;
CC Name=3;
CC IsoId=P57737-3; Sequence=VSP_046022;
CC Name=4;
CC IsoId=P57737-4; Sequence=VSP_046752;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in the spleen,
CC peripheral leukocytes, testes, brain, thymus and small intestine.
CC {ECO:0000269|PubMed:21130766}.
CC -!- PTM: The membrane-associated form is phosphorylated on tyrosine
CC residues. {ECO:0000250}.
CC -!- PTM: Ubiquitinated via 'Lys-33'-linked ubiquitin chains by the
CC BCR(KLHL20) E3 ubiquitin ligase complex: 'Lys-33'-linked ubiquitination
CC promotes interaction with EPS15 and facilitates actin polymerization at
CC the trans-Golgi network, thereby facilitating post-Golgi trafficking.
CC Deubiquitinated by ZRANB1/TRABID. {ECO:0000269|PubMed:24768539}.
CC -!- SIMILARITY: Belongs to the WD repeat coronin family. {ECO:0000305}.
CC -!- CAUTION: Reported to form a E3 ubiquitin-ligase complex and promote
CC degradation of TOB1 (PubMed:21130766). Additional evidence is however
CC required to confirm these data. {ECO:0000305|PubMed:21130766}.
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DR EMBL; AK025674; BAB15211.1; -; mRNA.
DR EMBL; AK294045; BAG57397.1; -; mRNA.
DR EMBL; AK296807; BAG59380.1; -; mRNA.
DR EMBL; AC012676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85307.1; -; Genomic_DNA.
DR EMBL; BC032732; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC117289; AAI17290.1; -; mRNA.
DR EMBL; BC117291; AAI17292.1; -; mRNA.
DR CCDS; CCDS10513.1; -. [P57737-1]
DR CCDS; CCDS55982.1; -. [P57737-2]
DR CCDS; CCDS58417.1; -. [P57737-4]
DR RefSeq; NP_001188401.1; NM_001201472.1. [P57737-4]
DR RefSeq; NP_001188402.1; NM_001201473.1. [P57737-2]
DR RefSeq; NP_078811.3; NM_024535.4. [P57737-1]
DR AlphaFoldDB; P57737; -.
DR BioGRID; 122728; 46.
DR BioGRID; 1529373; 15.
DR IntAct; P57737; 19.
DR MINT; P57737; -.
DR STRING; 9606.ENSP00000251166; -.
DR GlyGen; P57737; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P57737; -.
DR MetOSite; P57737; -.
DR PhosphoSitePlus; P57737; -.
DR BioMuta; CORO7; -.
DR DMDM; 259016200; -.
DR EPD; P57737; -.
DR jPOST; P57737; -.
DR MassIVE; P57737; -.
DR MaxQB; P57737; -.
DR PaxDb; P57737; -.
DR PeptideAtlas; P57737; -.
DR PRIDE; P57737; -.
DR ProteomicsDB; 47379; -.
DR ProteomicsDB; 57024; -. [P57737-1]
DR ProteomicsDB; 57025; -. [P57737-2]
DR Antibodypedia; 61575; 142 antibodies from 21 providers.
DR DNASU; 79585; -.
DR Ensembl; ENST00000251166.9; ENSP00000251166.4; ENSG00000262246.6. [P57737-1]
DR Ensembl; ENST00000537233.6; ENSP00000440460.2; ENSG00000262246.6. [P57737-4]
DR Ensembl; ENST00000574025.5; ENSP00000461702.1; ENSG00000262246.6. [P57737-2]
DR Ensembl; ENST00000614702.4; ENSP00000482646.1; ENSG00000282725.1. [P57737-1]
DR Ensembl; ENST00000617235.2; ENSP00000483187.2; ENSG00000282725.1. [P57737-4]
DR Ensembl; ENST00000631534.1; ENSP00000488867.1; ENSG00000282725.1. [P57737-2]
DR GeneID; 79585; -.
DR KEGG; hsa:79585; -.
DR MANE-Select; ENST00000251166.9; ENSP00000251166.4; NM_024535.5; NP_078811.3.
DR UCSC; uc002cwh.5; human. [P57737-1]
DR CTD; 79585; -.
DR DisGeNET; 79585; -.
DR GeneCards; CORO7; -.
DR HGNC; HGNC:26161; CORO7.
DR HPA; ENSG00000262246; Tissue enhanced (bone).
DR MIM; 611668; gene.
DR neXtProt; NX_P57737; -.
DR OpenTargets; ENSG00000262246; -.
DR PharmGKB; PA134910806; -.
DR VEuPathDB; HostDB:ENSG00000262246; -.
DR eggNOG; KOG1445; Eukaryota.
DR eggNOG; KOG3442; Eukaryota.
DR GeneTree; ENSGT00940000156606; -.
DR HOGENOM; CLU_006604_0_0_1; -.
DR InParanoid; P57737; -.
DR OMA; VMQGEVN; -.
DR OrthoDB; 552726at2759; -.
DR PhylomeDB; P57737; -.
DR TreeFam; TF314280; -.
DR PathwayCommons; P57737; -.
DR SignaLink; P57737; -.
DR BioGRID-ORCS; 79585; 13 hits in 999 CRISPR screens.
DR GenomeRNAi; 79585; -.
DR Pharos; P57737; Tbio.
DR PRO; PR:P57737; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P57737; protein.
DR Bgee; ENSG00000262246; Expressed in granulocyte and 92 other tissues.
DR ExpressionAtlas; P57737; baseline and differential.
DR Genevisible; P57737; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030041; P:actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
DR GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
DR GO; GO:0006895; P:Golgi to endosome transport; IMP:UniProtKB.
DR GO; GO:0035332; P:positive regulation of hippo signaling; IMP:FlyBase.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR027331; CORO7.
DR InterPro; IPR015505; Coronin.
DR InterPro; IPR015048; DUF1899.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR10856; PTHR10856; 1.
DR PANTHER; PTHR10856:SF20; PTHR10856:SF20; 1.
DR Pfam; PF08953; DUF1899; 2.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM01166; DUF1899; 2.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Golgi apparatus; Isopeptide bond; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport; Ubl conjugation;
KW WD repeat.
FT CHAIN 1..925
FT /note="Coronin-7"
FT /id="PRO_0000050934"
FT REPEAT 75..115
FT /note="WD 1"
FT REPEAT 124..163
FT /note="WD 2"
FT REPEAT 166..205
FT /note="WD 3"
FT REPEAT 209..253
FT /note="WD 4"
FT REPEAT 542..582
FT /note="WD 5"
FT REPEAT 592..632
FT /note="WD 6"
FT REPEAT 635..674
FT /note="WD 7"
FT REPEAT 728..768
FT /note="WD 8"
FT REGION 419..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2V7"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35828"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D2V7"
FT CROSSLNK 472
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:24768539"
FT CROSSLNK 680
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:24768539"
FT VAR_SEQ 78..162
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038152"
FT VAR_SEQ 78..95
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046752"
FT VAR_SEQ 925
FT /note="D -> AKYLAQIIVMGVQVVGRAFARALRQEFAASRAAADARGRAGHRSAAA
FT SNLSGLSLQEAQQILNVSKLSPEEVQKNYEHLFKVNDKSVGGSFYLQSKVVRAKERLDE
FT ELKIQAQEDREKGQMPHT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046022"
FT VARIANT 174
FT /note="A -> V (in dbSNP:rs17137007)"
FT /id="VAR_057585"
FT VARIANT 193
FT /note="R -> Q (in dbSNP:rs3747579)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_057586"
FT VARIANT 257
FT /note="L -> S (in dbSNP:rs35357594)"
FT /id="VAR_057587"
FT VARIANT 403
FT /note="A -> T (in dbSNP:rs9928967)"
FT /id="VAR_057588"
FT MUTAGEN 472
FT /note="K->R: Impaired ability to regulate the anterograde
FT Golgi to endosome transport."
FT /evidence="ECO:0000269|PubMed:24768539"
FT MUTAGEN 680
FT /note="K->R: Does not affect ability to regulate the
FT anterograde Golgi to endosome transport."
FT /evidence="ECO:0000269|PubMed:24768539"
FT CONFLICT 324
FT /note="S -> G (in Ref. 2; BAB15211)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="S -> G (in Ref. 2; BAB15211)"
FT /evidence="ECO:0000305"
FT CONFLICT 848
FT /note="A -> T (in Ref. 2; BAB15211)"
FT /evidence="ECO:0000305"
FT CONFLICT P57737-3:1037
FT /note="Q -> K (in Ref. 4; BC032732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 925 AA; 100605 MW; FC8680F8CCB409C0 CRC64;
MNRFRVSKFR HTEARPPRRE SWISDIRAGT APSCRNHIKS SCSLIAFNSD RPGVLGIVPL
QGQGEDKRRV AHLGCHSDLV TDLDFSPFDD FLLATGSADR TVKLWRLPGP GQALPSAPGV
VLGPEDLPVE VLQFHPTSDG ILVSAAGTTV KVWDAAKQQP LTELAAHGDL VQSAVWSRDG
ALVGTACKDK QLRIFDPRTK PRASQSTQAH ENSRDSRLAW MGTWEHLVST GFNQMREREV
KLWDTRFFSS ALASLTLDTS LGCLVPLLDP DSGLLVLAGK GERQLYCYEV VPQQPALSPV
TQCVLESVLR GAALVPRQAL AVMSCEVLRV LQLSDTAIVP IGYHVPRKAV EFHEDLFPDT
AGCVPATDPH SWWAGDNQQV QKVSLNPACR PHPSFTSCLV PPAEPLPDTA QPAVMETPVG
DADASEGFSS PPSSLTSPST PSSLGPSLSS TSGIGTSPSL RSLQSLLGPS SKFRHAQGTV
LHRDSHITNL KGLNLTTPGE SDGFCANKLR VAVPLLSSGG QVAVLELRKP GRLPDTALPT
LQNGAAVTDL AWDPFDPHRL AVAGEDARIR LWRVPAEGLE EVLTTPETVL TGHTEKICSL
RFHPLAANVL ASSSYDLTVR IWDLQAGADR LKLQGHQDQI FSLAWSPDGQ QLATVCKDGR
VRVYRPRSGP EPLQEGPGPK GGRGARIVWV CDGRCLLVSG FDSQSERQLL LYEAEALAGG
PLAVLGLDVA PSTLLPSYDP DTGLVLLTGK GDTRVFLYEL LPESPFFLEC NSFTSPDPHK
GLVLLPKTEC DVREVELMRC LRLRQSSLEP VAFRLPRVRK EFFQDDVFPD TAVIWEPVLS
AEAWLQGANG QPWLLSLQPP DMSPVSQAPR EAPARRAPSS AQYLEEKSDQ QKKEELLNAM
VAKLGNREDP LPQDSFEGVD EDEWD
