FRAS1_MOUSE
ID FRAS1_MOUSE Reviewed; 4010 AA.
AC Q80T14; E9QPG9; Q80TC7; Q811H8; Q8BPZ4;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Extracellular matrix organizing protein FRAS1 {ECO:0000303|PubMed:32333816};
DE Flags: Precursor;
GN Name=Fras1 {ECO:0000312|MGI:MGI:2385368}; Synonyms=Kiaa1500;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND DISEASE.
RC STRAIN=NMRI; TISSUE=Brain;
RX PubMed=12766770; DOI=10.1038/ng1168;
RA Vrontou S., Petrou P., Meyer B.I., Vassilis K., Galanopoulos K., Imai K.,
RA Yanagi M., Chowdhury K., Scambler P.J., Chalepakis G.;
RT "Fras1 deficiency results in cryptophthalmos, renal agenesis and blebbed
RT phenotype in mice.";
RL Nat. Genet. 34:209-214(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2283-4010.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2646-4010.
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3228-4010.
RC STRAIN=FVB/N; TISSUE=Kidney;
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, DEVELOPMENTAL STAGE, AND DISEASE.
RX PubMed=12766769; DOI=10.1038/ng1142;
RA McGregor L.K., Makela V., Darling S.M., Vrontou S., Chalepakis G.,
RA Roberts C., Smart N., Rutland P., Prescott N., Hopkins J., Bentley E.,
RA Shaw A., Roberts E., Mueller R., Jadeja S., Philip N., Nelson J.,
RA Francannet C., Perez-Aytes A., Megarbane A., Kerr B., Wainwright B.,
RA Woolf A.S., Winter R.M., Scambler P.J.;
RT "Fraser syndrome and mouse blebbed phenotype caused by mutations in
RT FRAS1/Fras1 encoding a putative extracellular matrix protein.";
RL Nat. Genet. 34:203-208(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND DISEASE.
RX PubMed=32333816; DOI=10.1111/ejn.14759;
RA Kalpachidou T., Makrygiannis A.K., Pavlakis E., Stylianopoulou F.,
RA Chalepakis G., Stamatakis A.;
RT "Behavioural effects of extracellular matrix protein Fras1 depletion in the
RT mouse.";
RL Eur. J. Neurosci. 53:3905-3919(2021).
CC -!- FUNCTION: Involved in extracellular matrix organization
CC (PubMed:32333816). Required for the regulation of epidermal-basement
CC membrane adhesion responsible for proper organogenesis during embryonic
CC development (PubMed:12766769). Involved in brain organization and
CC function (PubMed:32333816). {ECO:0000269|PubMed:12766769,
CC ECO:0000269|PubMed:32333816}.
CC -!- INTERACTION:
CC Q80T14; Q6NVD0: Frem2; NbExp=2; IntAct=EBI-15594303, EBI-15594269;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12766769,
CC ECO:0000269|PubMed:32333816}; Single-pass type I membrane protein
CC {ECO:0000305}; Extracellular side {ECO:0000269|PubMed:12766769,
CC ECO:0000269|PubMed:32333816}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in the apical ectodermal ridge of
CC the limb buds from 10.5-12.5 dpc and expression was also detected in
CC the interdigital spaces at 14.5 dpc. Found in cells just underlying the
CC surface epithelium of the entire embryo and in the linings of the
CC peritoneal cavity and dorsal aorta. At 12 dpc, detected in the
CC mesonephric duct and in the lens (PubMed:12766769). Found in a linear
CC fashion underlying the epidermis and the basal surface of other
CC epithelia in embryos (PubMed:12766770). Found in meningeal and
CC choroidal epidermal-basement membranes in embryos and neonates
CC (PubMed:32333816). {ECO:0000269|PubMed:12766769,
CC ECO:0000269|PubMed:12766770, ECO:0000269|PubMed:32333816}.
CC -!- DOMAIN: The Calx-beta domains bind calcium with high affinity and
CC undergo a major conformational shift upon binding. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in Fras1 are the cause of blebbed (bl) phenotype,
CC which is characterized by blister formation, syndactyly, eyelid fusion
CC and renal agenesis. Subepidermal blisters are predominantly formed in
CC the head region around the eyes and at the distal part of the limbs. As
CC development proceeds blisters that are initially transparent gradually
CC become hemorrhagic and embryos die between 14.5 dpc and 16.5 dpc.
CC {ECO:0000269|PubMed:12766769, ECO:0000269|PubMed:12766770,
CC ECO:0000269|PubMed:32333816}.
CC -!- DISRUPTION PHENOTYPE: Homozygous adult knockout mice display impaired
CC performance in various types of learning and memory tasks as well as
CC reduced anxiety. {ECO:0000269|PubMed:32333816}.
CC -!- SIMILARITY: Belongs to the FRAS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC34788.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC34788.1; Type=Frameshift; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ489280; CAD33519.1; -; mRNA.
DR EMBL; AC101391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC121829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC151985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK122518; BAC65800.1; -; mRNA.
DR EMBL; AK051850; BAC34788.1; ALT_SEQ; mRNA.
DR EMBL; BC044881; AAH44881.1; -; mRNA.
DR CCDS; CCDS19450.1; -.
DR RefSeq; NP_780682.3; NM_175473.3.
DR SMR; Q80T14; -.
DR BioGRID; 231125; 1.
DR CORUM; Q80T14; -.
DR DIP; DIP-61242N; -.
DR IntAct; Q80T14; 2.
DR STRING; 10090.ENSMUSP00000043250; -.
DR GlyConnect; 2307; 1 N-Linked glycan (1 site).
DR GlyGen; Q80T14; 16 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q80T14; -.
DR PhosphoSitePlus; Q80T14; -.
DR EPD; Q80T14; -.
DR MaxQB; Q80T14; -.
DR PaxDb; Q80T14; -.
DR PeptideAtlas; Q80T14; -.
DR PRIDE; Q80T14; -.
DR ProteomicsDB; 267408; -.
DR Antibodypedia; 2470; 34 antibodies from 10 providers.
DR DNASU; 231470; -.
DR Ensembl; ENSMUST00000036019; ENSMUSP00000043250; ENSMUSG00000034687.
DR GeneID; 231470; -.
DR KEGG; mmu:231470; -.
DR UCSC; uc008yfk.1; mouse.
DR CTD; 80144; -.
DR MGI; MGI:2385368; Fras1.
DR VEuPathDB; HostDB:ENSMUSG00000034687; -.
DR eggNOG; KOG1025; Eukaryota.
DR eggNOG; KOG1216; Eukaryota.
DR eggNOG; KOG1306; Eukaryota.
DR eggNOG; KOG3525; Eukaryota.
DR eggNOG; KOG3597; Eukaryota.
DR GeneTree; ENSGT00940000162130; -.
DR HOGENOM; CLU_000244_0_0_1; -.
DR InParanoid; Q80T14; -.
DR OMA; FTSVNHK; -.
DR OrthoDB; 13258at2759; -.
DR PhylomeDB; Q80T14; -.
DR TreeFam; TF316876; -.
DR BioGRID-ORCS; 231470; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Fras1; mouse.
DR PRO; PR:Q80T14; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q80T14; protein.
DR Bgee; ENSMUSG00000034687; Expressed in fourth ventricle and 210 other tissues.
DR Genevisible; Q80T14; MM.
DR GO; GO:0005604; C:basement membrane; IDA:BHF-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR GO; GO:0003338; P:metanephros morphogenesis; IMP:MGI.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:MGI.
DR GO; GO:0015031; P:protein transport; IMP:MGI.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR CDD; cd00064; FU; 12.
DR Gene3D; 2.60.40.2030; -; 5.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR039005; CSPG_rpt.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR006212; Furin_repeat.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF03160; Calx-beta; 5.
DR Pfam; PF00093; VWC; 5.
DR SMART; SM00237; Calx_beta; 5.
DR SMART; SM00181; EGF; 10.
DR SMART; SM00261; FU; 14.
DR SMART; SM00214; VWC; 6.
DR SMART; SM00215; VWC_out; 3.
DR SUPFAM; SSF141072; SSF141072; 5.
DR SUPFAM; SSF57184; SSF57184; 5.
DR PROSITE; PS51854; CSPG; 12.
DR PROSITE; PS01208; VWFC_1; 6.
DR PROSITE; PS50184; VWFC_2; 6.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..4010
FT /note="Extracellular matrix organizing protein FRAS1"
FT /id="PRO_0000010121"
FT TOPO_DOM 26..3903
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 3904..3924
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3925..4010
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..87
FT /note="VWFC 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 92..152
FT /note="VWFC 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 156..216
FT /note="VWFC 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 218..278
FT /note="VWFC 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 282..342
FT /note="VWFC 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 358..416
FT /note="VWFC 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT REPEAT 408..459
FT /note="FU 1"
FT REPEAT 461..504
FT /note="FU 2"
FT REPEAT 506..552
FT /note="FU 3"
FT REPEAT 554..598
FT /note="FU 4"
FT REPEAT 601..646
FT /note="FU 5"
FT REPEAT 648..704
FT /note="FU 6"
FT REPEAT 707..752
FT /note="FU 7"
FT REPEAT 754..799
FT /note="FU 8"
FT REPEAT 802..851
FT /note="FU 9"
FT REPEAT 853..899
FT /note="FU 10"
FT REPEAT 902..947
FT /note="FU 11"
FT REPEAT 951..996
FT /note="FU 12"
FT REPEAT 998..1041
FT /note="FU 13"
FT REPEAT 1045..1088
FT /note="FU 14"
FT REPEAT 1101..1196
FT /note="CSPG 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1216..1307
FT /note="CSPG 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1328..1440
FT /note="CSPG 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1465..1561
FT /note="CSPG 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1597..1691
FT /note="CSPG 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1712..1812
FT /note="CSPG 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1834..1938
FT /note="CSPG 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1959..2059
FT /note="CSPG 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 2080..2179
FT /note="CSPG 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 2201..2293
FT /note="CSPG 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 2313..2406
FT /note="CSPG 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 2441..2538
FT /note="CSPG 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT DOMAIN 2545..2648
FT /note="Calx-beta 1"
FT DOMAIN 2661..2772
FT /note="Calx-beta 2"
FT DOMAIN 2786..2892
FT /note="Calx-beta 3"
FT DOMAIN 2907..3009
FT /note="Calx-beta 4"
FT DOMAIN 3027..3131
FT /note="Calx-beta 5"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XX4"
FT CARBOHYD 727
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1094
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1506
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1779
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1950
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1980
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2666
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2684
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2910
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2987
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3072
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3678
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3877
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 22
FT /note="N -> H (in Ref. 1; CAD33519)"
FT /evidence="ECO:0000305"
FT CONFLICT 1026
FT /note="L -> F (in Ref. 1; CAD33519)"
FT /evidence="ECO:0000305"
FT CONFLICT 1063
FT /note="R -> Q (in Ref. 1; CAD33519)"
FT /evidence="ECO:0000305"
FT CONFLICT 1466
FT /note="P -> H (in Ref. 1; CAD33519)"
FT /evidence="ECO:0000305"
FT CONFLICT 2020
FT /note="N -> H (in Ref. 1; CAD33519)"
FT /evidence="ECO:0000305"
FT CONFLICT 2208
FT /note="R -> K (in Ref. 1; CAD33519)"
FT /evidence="ECO:0000305"
FT CONFLICT 2310
FT /note="V -> L (in Ref. 1; CAD33519 and 3; BAC65800)"
FT /evidence="ECO:0000305"
FT CONFLICT 2314
FT /note="R -> Q (in Ref. 1; CAD33519 and 3; BAC65800)"
FT /evidence="ECO:0000305"
FT CONFLICT 2623
FT /note="G -> S (in Ref. 1; CAD33519 and 3; BAC65800)"
FT /evidence="ECO:0000305"
FT CONFLICT 2646
FT /note="G -> W (in Ref. 4; BAC34788)"
FT /evidence="ECO:0000305"
FT CONFLICT 2664
FT /note="V -> I (in Ref. 1; CAD33519 and 3; BAC65800)"
FT /evidence="ECO:0000305"
FT CONFLICT 3135
FT /note="L -> P (in Ref. 1; CAD33519 and 3; BAC65800)"
FT /evidence="ECO:0000305"
FT CONFLICT 3172
FT /note="D -> G (in Ref. 4; BAC34788)"
FT /evidence="ECO:0000305"
FT CONFLICT 3383
FT /note="Q -> R (in Ref. 1; CAD33519, 3; BAC65800 and 5;
FT AAH44881)"
FT /evidence="ECO:0000305"
FT CONFLICT 3395
FT /note="N -> D (in Ref. 1; CAD33519, 3; BAC65800 and 5;
FT AAH44881)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4010 AA; 442369 MW; 7C1DDED1C8ACEC04 CRC64;
MGVLKAWLGV ALALAEFAVL PNCEGACLYQ GSFLADATIW KPDSCQNCRC HGDIVICKPV
VCKNPRCAFE KGEVLWIAPN QCCPQCAPRT PGSCHHEGKI HEHGTEWASA PCTVCSCTHG
EVRCSHQQCT PLSCGPQELE FLAEGRCCPI CVGTGKPCSY DGHVFQDGED WQLSRCAKCV
CRNGLTQCFA AQCQPLFCNQ DEIVVRVPGK CCSQCSARSC STAGQVYEHG EQWKEDACTL
CMCDQGQVRC HKQVCPPLRC AKGQGRARHH GQCCEECATP DRSCSSGGVL RYQDEMWKGS
ACEFCMCDQG QVTCQTGECA KVACALGEEL VHLEGKCCPE CISRNGYCIY EQKAETMSSS
AREIKHVPDG EKWEEGPCKL CECREAQVTC YEPSCPPCPV ATLALVVKGQ CCPDCTPVHC
HPDCLTCSHS PDHCDLCQDP TKLLQNGRCV HSCGLGFYQA GSLCLACQPQ CSTCTNGLEC
SSCLPPLLMQ QGQCVSTCGD GFYQDHHSCA VCHESCAGCW GPTEKHCMAC RDPLQVLRDS
SCENTCGNGF YNRQGTCVAC DQSCKSCGPS SPRCLSCAEK TILHDGKCIS ECPHGYYADS
TGSCKVCHSS CASCSGPTAA HCIACIHPQT LRQGHCLPSC GEGFYPDHGI CEACHASCHT
CVGPQPSHCT QCKKPEAGLL VEQHSGENVP YGKCVSRCGT HFYLESTGLC EVCHPSCLTC
EGKSPHNCTG CESTHALLAG CCVSQCPETH FNLEGTCTEC HPSCRQCHGP LESDCVSCHP
HLTLTSGHCK TSCKEEQFLN LVGYCADCHP LCQHCVANLQ DTGSICLKCQ HARHLLLGDH
CVPECPPGHY KERGTCKTCH SSCRSCQNGG PFSCSSCDTG LVLTHIGTCS TACFPGHYLD
DNQVCQPCNR HCRSCDSQGS CTSCRDPSKV LLFGECQYES CTPQYYLDIA TKTCKECDWS
CNACTGPLRT DCLQCMDGYV LQDGVCVEQC SPQHYRDSGS CKRCDSHCVE CQGPHECTRC
EEPFLLFQAQ CVQECGKGYF ADHAKHRCIA CPQGCLRCSH KDRCHLCDHS FFLKSGLCMP
TCVPGFSGHS SNENCTDKMY TPSLHVNGSL TLGIGSMKPL DFSLLNIQHQ DGRVEDLLFH
VVSTPTNGQL LLSRNGKEVQ LEKAGHFSWK DVNEKKVRFV HSKEKLRKGY FSLKISDQQF
FSEPQLINIQ AFSTQAPYVL RNEVLHVSKG ERATITTQLL DIRDDDNPQD VVVNVLDPPL
HGQLLQMPPA PAASIYQFHL DELSRGLLLY AHDGSDSTSD IIVFQANDGH SFQNILFHVK
NIPKNDRALR LVTNSMVWVP EGGMLKITNR ILKAQAPGVR ADDIIYKITH SRPQFGEVVL
LMNLPADSPA GPAEEGHHLP DGRMATPIST FTQQDIDDGV VWYRHLGAPT QSDSFRFQVS
SATSAQEHLE SHMFNIAILP QAPEAPKLSL GTSLHMTARE DGLSVIQPQS LSFVKAESPS
GKIIYNITVP LHPNQGIIEH RDRPHSPIQY FTQEDINQGQ IMYRPPVAPP HLQEIMAFSF
AGLPESVKFY FTVSDGQHTS PEMALTIHLL HSDLQPPAFQ VKAPLLEVSP GGRTSLGLQL
LVRDAQVVPE ELFFQLQKSP QHGMLVKYTA KSSVTMAAGD TFTYDEVERN VLQYVHDGSS
AWEDSLEISV TDGLTVTTSE VKVEVSPSEN RGPRLAPGSS LSMTVASQHT AIITRSHLAY
VDDSSSDPEI WIRLSSLPLY GVLFRSSGPD MDELSGDSNF TMEDINKKNI RYSAVFETDG
HSVTDGFHFS VSDMDGNHVD NQVFTITVTP AENPPHIIAF ADLITVDEGG RAPLSLHHFF
ATEDQDNLQD DAVIKLSALP KYGCIENTGT GDRFGPGANS ELEASFPIQD VLENYIYYFQ
SVHESIEPTH DVFSFYVSDG SGRSEIHSIN ITIERKNDEP PRMTLRPLGV RLSSGVAISN
SSLSLQDLDT PDNELIFVLM KKPDHGHLLR RSTASDPLEN GTVLDQGSSF TYQDVLAGLV
GYLPGDIYMA VDEFRFSLTD GLHVDTGRME IYIELPSTNI PHLAINRGLQ LSAGSVARIT
EQHLKATDTD SEAGQVVYIM KEDPGAGRLL MAKADNLEQI SVRGPIRSFT QADVSQGQIE
YSHGPGEPGG SFAFKFDVVD GEGNKLADQS FSIGVLEDKS PPVVITNRGL VLDENSVEKI
TTAQLSATDQ DSKPTELIYR ITTQPQLGHL EHVASPGIQI SSFTQADLAS RNVQYVRSSG
TGKQSDAFSF VLSDGLHEVT QTFPITIHPV DDARPLVQNR GMRVQEGVRK TITEFELKAV
DVDTEAESIT FTIVQPPRHG TIERTARGQR FHQTSSFTME DIYQNRVSYS HDGSNSLKDR
FTFTVSDGTN PFFIIEEGGE EIMTAAPQQF HVDILPVDDG TPRIVTNLGL QWLEYMDGKA
TNLITKKELL TVDPDTEDSQ LIYEVTTGPM HGYLENKLQP GRAAATFTQE HVNLGLIRYV
LYEEKIQKVM DSFQFLVKDS KPNVVSDNVF HIQWSLISFK YTSYNVSEKA GSVSVTVQRT
GNLNQYAIVL CRTEQGTASS SSHPGQQDYM EYAGQVQFDE GEGTKSCTVI INDDDVFENI
ESFTVGLSMP AYALLGEFTQ AKVVINDTED EPTLEFDKKT YRVNESAGFL FAPIKRQGDS
SSTVSAVCYT VPKSAMGSSL YALESGSDFK SRGRSAESRV IFGPGVTVST CDVMVIDDSE
YEEEEEFEIA LADASNNARI GRQAVAKVLI SGPNDASTVS LGNTAFTISE DAGTVKIPVI
RHGTDLSTFT SVWCATRPSD PASATPGVDY VPSSRKVEFG PGITEQYCTL TILDDTQYPV
IEGLETFVVF LSSAQGAELT KPSQAVIAIN DTFQDVPSMQ FSKDLLLVKE KEGVLHIPII
RSGDLSYESS VRCYTQGHSA QVMEDFEERR NADSSRITFL KGQKTKNCTV YIHDDSMFEP
EEQFRVYLGH PLGNHWSGAR IGKNSVATVT ISNDEDAPTI EFEEAAYQVR EPAGPEAIAV
LSIKVIRRGD QNRTSKIRCS TRDGSAQSGV DYYPKSRVLK FSPGVDHIFF KVEILSNEDR
EWHESFSLVL GPDDLVEAVL GDVTTATVTI LDQEAAGSLI LPAPPIVVTL ADYDHVEELA
KEGVKKAPSP GYPLVCVTPC DPRYPRYAVM KERCSEAGIN QTSVQFSWEV AAPTDGNGAR
SPFETITDNT PFTSVNHKVL DSIYFSRRFH VRCVAKAVDK VGHVGTPLRS NVVTIGTDSA
ICHTPVVAGT ARGFQAQSFI ATLKYLDVKH KEHPNRIHIS VQIPHQDGML PLISTMPLHN
LHFLLSESIY RHQHVCSNLV TAQDLRGLAE AGFLNDAGFH STALGPGYDR PFQFDSSVRE
PKTIQLYRHL NLKSCVWTFD AYYDMTELID VCGGSVTADF QVRDSAQSFL TVHVPLYVSY
IYVTAPRGWA SLEHHTEMEF SFFYDTVLWR TGIQTDSVLS ARLQIIRIYI REDGRLVIEF
KTHAKFRGQF VIEHHTLPDV KSFILTPDHL GGIQFDLQLL WSAQTFDSPH QLWRATSSYN
RKDYSGEYTI YLIPCTVQPT QPWVDPGEKA LACTAHAPER FLIPIAFQQT NRPVPVVYSL
NTEFQLCNNE KVFLMDPNTS DMSLAEMDYK GAFSKGQILY GRVLWNPEQN LHSAYKLQLE
KVYLCTGKDG YVPFFDPTGT IYNEGPQYGC IQPNKHLKHR FLLLDRSQPE VTDKYFHDVP
FEAHFASELP DFQVVSSMPG VDGFTLKVDA LYKVEAGHQW YLQVIYIIGP DSTSRPRVQR
SLTVSLRRHQ RDLVDPSGWL SLDDSLIYDN EGDQVKNGTN MKSLNLEMQE PVIAASLSQT
GASIGSALAA IMLLLLLFLV ACFVTRKCQK QKKKQPPEDT LEEYPLNTKV DVAKRNADKV
EKNANRQYCT VRNVNILSDN EGYYTFKGAK VKKLNLEVRV HNNLQDGTEV
