AMNLS_HUMAN
ID AMNLS_HUMAN Reviewed; 453 AA.
AC Q9BXJ7; Q6UX83;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein amnionless;
DE Contains:
DE RecName: Full=Soluble protein amnionless;
DE Flags: Precursor;
GN Name=AMN; ORFNames=UNQ513/PRO1028;
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].
RX PubMed=11279523; DOI=10.1038/86912;
RA Kalantry S., Manning S., Haub O., Tomihara-Newberger C., Lee H.-G.,
RA Fangman J., Disteche C.M., Manova K., Lacy E.;
RT "The amnionless gene, essential for mouse gastrulation, encodes a visceral-
RT endoderm-specific protein with an extracellular cysteine-rich domain.";
RL Nat. Genet. 27:412-416(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-230.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP PROTEIN SEQUENCE OF 300-323 AND 393-453, TISSUE SPECIFICITY, VARIANT IGS2
RP ILE-41, FUNCTION, AND ALTERNATIVE PRODUCTS.
RX PubMed=12590260; DOI=10.1038/ng1098;
RA Tanner S.M., Aminoff M., Wright F.A., Liyanarachchi S., Kuronen M.,
RA Saarinen A., Massika O., Mandel H., Broch H., de la Chapelle A.;
RT "Amnionless, essential for mouse gastrulation, is mutated in recessive
RT hereditary megaloblastic anemia.";
RL Nat. Genet. 33:426-429(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH CUBN,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=14576052; DOI=10.1182/blood-2003-08-2852;
RA Fyfe J.C., Madsen M., Hoejrup P., Christensen E.I., Tanner S.M.,
RA de la Chapelle A., He Q., Moestrup S.K.;
RT "The functional cobalamin (vitamin B12)-intrinsic factor receptor is a
RT novel complex of cubilin and amnionless.";
RL Blood 103:1573-1579(2004).
RN [6] {ECO:0007744|PDB:6GJE}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 20-357 IN COMPLEX WITH CUBN,
RP CHARACTERIZATION OF VARIANT IGS2 ILE-41, SUBUNIT, SUBCELLULAR LOCATION,
RP TOPOLOGY, DISULFIDE BONDS, AND MUTAGENESIS OF ASN-35 AND SER-37.
RX PubMed=30523278; DOI=10.1038/s41467-018-07468-4;
RA Larsen C., Etzerodt A., Madsen M., Skjodt K., Moestrup S.K.,
RA Andersen C.B.F.;
RT "Structural assembly of the megadalton-sized receptor for intestinal
RT vitamin B12 uptake and kidney protein reabsorption.";
RL Nat. Commun. 9:5204-5204(2018).
RN [7]
RP VARIANTS IGS2 ILE-41 AND PHE-234.
RX PubMed=22929189; DOI=10.1186/1750-1172-7-56;
RA Tanner S.M., Sturm A.C., Baack E.C., Liyanarachchi S., de la Chapelle A.;
RT "Inherited cobalamin malabsorption. Mutations in three genes reveal
RT functional and ethnic patterns.";
RL Orphanet J. Rare Dis. 7:56-56(2012).
RN [8]
RP VARIANT IGS2 LYS-69, AND FUNCTION.
RX PubMed=26040326; DOI=10.1186/s12881-015-0181-2;
RA Montgomery E., Sayer J.A., Baines L.A., Hynes A.M., Vega-Warner V.,
RA Johnson S., Goodship J.A., Otto E.A.;
RT "Novel compound heterozygous mutations in AMN cause Imerslund-Graesbeck
RT syndrome in two half-sisters: a case report.";
RL BMC Med. Genet. 16:35-35(2015).
RN [9]
RP INVOLVEMENT IN IGS2.
RX PubMed=22631584; DOI=10.1111/j.1442-200x.2011.03482.x;
RA Densupsoontorn N., Sanpakit K., Vijarnsorn C., Pattaragarn A.,
RA Kangwanpornsiri C., Jatutipsompol C., Tirapongporn H., Jirapinyo P.,
RA Shah N.P., Sturm A.C., Tanner S.M.;
RT "Imerslund-Grasbeck syndrome: new mutation in amnionless.";
RL Pediatr. Int. 54:E19-E21(2012).
RN [10]
RP FUNCTION, INTERACTION WITH CUBN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP CHARACTERIZATION OF VARIANTS IGS2 ILE-41; LYS-69 AND PHE-234, AND
RP MUTAGENESIS OF LEU-59 AND GLY-254.
RX PubMed=29402915; DOI=10.1038/s41598-018-20731-4;
RA Udagawa T., Harita Y., Miura K., Mitsui J., Ode K.L., Morishita S.,
RA Urae S., Kanda S., Kajiho Y., Tsurumi H., Ueda H.R., Tsuji S., Saito A.,
RA Oka A.;
RT "Amnionless-mediated glycosylation is crucial for cell surface targeting of
RT cubilin in renal and intestinal cells.";
RL Sci. Rep. 8:2351-2351(2018).
CC -!- FUNCTION: Membrane-bound component of the endocytic receptor formed by
CC AMN and CUBN (PubMed:14576052, PubMed:30523278, PubMed:29402915).
CC Required for normal CUBN glycosylation and trafficking to the cell
CC surface (PubMed:14576052, PubMed:29402915). The complex formed by AMN
CC and CUBN is required for efficient absorption of vitamin B12
CC (PubMed:12590260, PubMed:14576052, PubMed:26040326). Required for
CC normal CUBN-mediated protein transport in the kidney (Probable).
CC {ECO:0000269|PubMed:12590260, ECO:0000269|PubMed:14576052,
CC ECO:0000269|PubMed:26040326, ECO:0000269|PubMed:29402915,
CC ECO:0000269|PubMed:30523278, ECO:0000305|PubMed:22631584,
CC ECO:0000305|PubMed:26040326}.
CC -!- SUBUNIT: Interacts (via extracellular region) with CUBN/cubilin, giving
CC rise to a huge complex containing one AMN chain and three CUBN chains.
CC {ECO:0000269|PubMed:14576052, ECO:0000269|PubMed:29402915,
CC ECO:0000269|PubMed:30523278}.
CC -!- INTERACTION:
CC Q9BXJ7; O60494: CUBN; NbExp=3; IntAct=EBI-11510881, EBI-3953632;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Apical cell membrane
CC {ECO:0000269|PubMed:14576052}; Single-pass type I membrane protein
CC {ECO:0000305|PubMed:30523278}. Cell membrane
CC {ECO:0000269|PubMed:14576052, ECO:0000269|PubMed:29402915,
CC ECO:0000269|PubMed:30523278}; Single-pass type I membrane protein
CC {ECO:0000305}. Endosome membrane {ECO:0000305|PubMed:14576052}.
CC Membrane, coated pit {ECO:0000305|PubMed:14576052}.
CC -!- SUBCELLULAR LOCATION: [Soluble protein amnionless]: Secreted
CC {ECO:0000269|PubMed:14576052}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=1;
CC Comment=At least 5 isoforms, 1, 2, 3, 4 and 5, are produced.
CC {ECO:0000305|PubMed:12590260};
CC Name=1;
CC IsoId=Q9BXJ7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Detected in proximal tubules in the kidney cortex
CC (at protein level) (PubMed:14576052, PubMed:29402915). Long isoforms
CC are highly expressed in small intestine, colon and kidney (renal
CC proximal tubule epithelial cells). Shorter isoforms are detected at
CC lower levels in testis, thymus and peripheral blood leukocytes.
CC {ECO:0000269|PubMed:12590260, ECO:0000269|PubMed:14576052,
CC ECO:0000269|PubMed:29402915}.
CC -!- DOMAIN: The complex formed by AMN and CUBN is composed of a 400
CC Angstrom long stem and a globular crown region. The stem region is
CC probably formed by AMN and the CUBN N-terminal region, including the
CC EGF-like domains. The crown is probably formed by the CUBN CUB domains.
CC {ECO:0000250|UniProtKB:F1SAM7}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:14576052}.
CC -!- PTM: A soluble form arises by proteolytic removal of the membrane
CC anchor. {ECO:0000269|PubMed:14576052}.
CC -!- DISEASE: Imerslund-Grasbeck syndrome 2 (IGS2) [MIM:618882]: A form of
CC Imerslund-Grasbeck syndrome, a rare autosomal recessive disorder
CC characterized by vitamin B12 deficiency commonly resulting in
CC megaloblastic anemia, which is responsive to parenteral vitamin B12
CC therapy and appears in infancy or early childhood. Clinical
CC manifestations include failure to thrive, infections and neurological
CC damage. Mild proteinuria, with no signs of kidney disease, is present
CC in about half of the patients. {ECO:0000269|PubMed:12590260,
CC ECO:0000269|PubMed:22631584, ECO:0000269|PubMed:22929189,
CC ECO:0000269|PubMed:26040326, ECO:0000269|PubMed:29402915,
CC ECO:0000269|PubMed:30523278}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: The role of Amn in embryonic development seems to be
CC species specific. In mice, null mutations lead to embryonic lethality.
CC Human mutations give rise to much milder symptoms. {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; AF328788; AAK28532.1; -; mRNA.
DR EMBL; AL117209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY358468; AAQ89949.1; -; mRNA.
DR CCDS; CCDS9977.1; -. [Q9BXJ7-1]
DR RefSeq; NP_112205.2; NM_030943.3. [Q9BXJ7-1]
DR PDB; 6GJE; X-ray; 2.30 A; A=20-359.
DR PDBsum; 6GJE; -.
DR AlphaFoldDB; Q9BXJ7; -.
DR SMR; Q9BXJ7; -.
DR BioGRID; 123571; 1.
DR ComplexPortal; CPX-5774; Cubam cobalamin uptake receptor complex.
DR CORUM; Q9BXJ7; -.
DR IntAct; Q9BXJ7; 2.
DR STRING; 9606.ENSP00000299155; -.
DR DrugBank; DB00115; Cyanocobalamin.
DR DrugBank; DB00200; Hydroxocobalamin.
DR DrugCentral; Q9BXJ7; -.
DR GlyGen; Q9BXJ7; 1 site.
DR iPTMnet; Q9BXJ7; -.
DR PhosphoSitePlus; Q9BXJ7; -.
DR BioMuta; AMN; -.
DR DMDM; 296434395; -.
DR jPOST; Q9BXJ7; -.
DR MassIVE; Q9BXJ7; -.
DR MaxQB; Q9BXJ7; -.
DR PaxDb; Q9BXJ7; -.
DR PeptideAtlas; Q9BXJ7; -.
DR PRIDE; Q9BXJ7; -.
DR ProteomicsDB; 79440; -. [Q9BXJ7-1]
DR Antibodypedia; 13; 55 antibodies from 22 providers.
DR DNASU; 81693; -.
DR Ensembl; ENST00000299155.10; ENSP00000299155.6; ENSG00000166126.11. [Q9BXJ7-1]
DR GeneID; 81693; -.
DR KEGG; hsa:81693; -.
DR MANE-Select; ENST00000299155.10; ENSP00000299155.6; NM_030943.4; NP_112205.2.
DR UCSC; uc001ymg.5; human. [Q9BXJ7-1]
DR CTD; 81693; -.
DR DisGeNET; 81693; -.
DR GeneCards; AMN; -.
DR HGNC; HGNC:14604; AMN.
DR HPA; ENSG00000166126; Group enriched (intestine, kidney, liver).
DR MalaCards; AMN; -.
DR MIM; 605799; gene.
DR MIM; 618882; phenotype.
DR neXtProt; NX_Q9BXJ7; -.
DR OpenTargets; ENSG00000166126; -.
DR Orphanet; 35858; Imerslund-Graesbeck syndrome.
DR PharmGKB; PA134962814; -.
DR VEuPathDB; HostDB:ENSG00000166126; -.
DR eggNOG; ENOG502QUUQ; Eukaryota.
DR GeneTree; ENSGT00390000007463; -.
DR HOGENOM; CLU_050471_0_0_1; -.
DR InParanoid; Q9BXJ7; -.
DR OMA; PWICADL; -.
DR OrthoDB; 827066at2759; -.
DR PhylomeDB; Q9BXJ7; -.
DR TreeFam; TF323790; -.
DR PathwayCommons; Q9BXJ7; -.
DR Reactome; R-HSA-3359462; Defective AMN causes MGA1.
DR Reactome; R-HSA-3359463; Defective CUBN causes MGA1.
DR Reactome; R-HSA-8964011; HDL clearance.
DR Reactome; R-HSA-9758881; Uptake of dietary cobalamins into enterocytes.
DR SignaLink; Q9BXJ7; -.
DR BioGRID-ORCS; 81693; 15 hits in 1068 CRISPR screens.
DR GeneWiki; Amnionless; -.
DR GenomeRNAi; 81693; -.
DR Pharos; Q9BXJ7; Tbio.
DR PRO; PR:Q9BXJ7; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9BXJ7; protein.
DR Bgee; ENSG00000166126; Expressed in mucosa of transverse colon and 167 other tissues.
DR ExpressionAtlas; Q9BXJ7; baseline and differential.
DR Genevisible; Q9BXJ7; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-KW.
DR GO; GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0031528; C:microvillus membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IPI:ComplexPortal.
DR GO; GO:0038024; F:cargo receptor activity; IDA:MGI.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR GO; GO:0009235; P:cobalamin metabolic process; IDA:MGI.
DR GO; GO:0015889; P:cobalamin transport; IDA:UniProtKB.
DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IDA:UniProtKB.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:UniProtKB.
DR GO; GO:0097017; P:renal protein absorption; IEA:Ensembl.
DR InterPro; IPR026112; AMN.
DR PANTHER; PTHR14995; PTHR14995; 1.
DR Pfam; PF14828; Amnionless; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Cell membrane; Coated pit;
KW Developmental protein; Direct protein sequencing; Disease variant;
KW Disulfide bond; Endosome; Glycoprotein; Membrane; Protein transport;
KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:14576052"
FT CHAIN 20..453
FT /note="Protein amnionless"
FT /id="PRO_0000020702"
FT CHAIN 20..?
FT /note="Soluble protein amnionless"
FT /id="PRO_0000447651"
FT TOPO_DOM 20..357
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:30523278"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 379..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 202..254
FT /note="VWFC"
FT REGION 67..87
FT /note="Interaction with CUBN"
FT /evidence="ECO:0000269|PubMed:30523278"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 43..96
FT /evidence="ECO:0000269|PubMed:30523278,
FT ECO:0007744|PDB:6GJE"
FT DISULFID 137..213
FT /evidence="ECO:0000269|PubMed:30523278,
FT ECO:0007744|PDB:6GJE"
FT DISULFID 205..211
FT /evidence="ECO:0000269|PubMed:30523278,
FT ECO:0007744|PDB:6GJE"
FT DISULFID 223..249
FT /evidence="ECO:0000269|PubMed:30523278,
FT ECO:0007744|PDB:6GJE"
FT DISULFID 234..250
FT /evidence="ECO:0000269|PubMed:30523278,
FT ECO:0007744|PDB:6GJE"
FT DISULFID 239..253
FT /evidence="ECO:0000269|PubMed:30523278,
FT ECO:0007744|PDB:6GJE"
FT VARIANT 41
FT /note="T -> I (in IGS2; reduced presence at the cell
FT membrane; loss of interaction with CUBN; reduced CUBN
FT expression at the cell surface; dbSNP:rs119478058)"
FT /evidence="ECO:0000269|PubMed:12590260,
FT ECO:0000269|PubMed:22929189, ECO:0000269|PubMed:29402915,
FT ECO:0000269|PubMed:30523278"
FT /id="VAR_015733"
FT VARIANT 69
FT /note="M -> K (in IGS2; loss of interaction with CUBN;
FT strongly reduced CUBN expression at the cell surface;
FT dbSNP:rs375774640)"
FT /evidence="ECO:0000269|PubMed:26040326"
FT /id="VAR_081906"
FT VARIANT 234
FT /note="C -> F (in IGS2; loss of interaction with CUBN;
FT strongly reduced CUBN expression at the cell surface;
FT dbSNP:rs386834176)"
FT /evidence="ECO:0000269|PubMed:22929189,
FT ECO:0000269|PubMed:29402915"
FT /id="VAR_081907"
FT MUTAGEN 35
FT /note="N->Q: Loss of expression at the cell membrane."
FT /evidence="ECO:0000269|PubMed:30523278"
FT MUTAGEN 37
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:30523278"
FT MUTAGEN 59
FT /note="L->P: Loss of interaction with CUBN and strongly
FT reduced CUBN expression at the cell surface."
FT /evidence="ECO:0000269|PubMed:29402915"
FT MUTAGEN 254
FT /note="G->E: Loss of interaction with CUBN and strongly
FT reduced CUBN expression at the cell surface."
FT /evidence="ECO:0000269|PubMed:29402915"
FT CONFLICT 241
FT /note="S -> F (in Ref. 1; AAK28532)"
FT /evidence="ECO:0000305"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:6GJE"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:6GJE"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 62..70
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:6GJE"
FT TURN 91..98
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6GJE"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:6GJE"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 161..168
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:6GJE"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:6GJE"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6GJE"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:6GJE"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 252..261
FT /evidence="ECO:0007829|PDB:6GJE"
FT HELIX 267..276
FT /evidence="ECO:0007829|PDB:6GJE"
FT TURN 277..280
FT /evidence="ECO:0007829|PDB:6GJE"
FT HELIX 282..284
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 287..296
FT /evidence="ECO:0007829|PDB:6GJE"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 305..313
FT /evidence="ECO:0007829|PDB:6GJE"
FT HELIX 320..339
FT /evidence="ECO:0007829|PDB:6GJE"
FT STRAND 341..348
FT /evidence="ECO:0007829|PDB:6GJE"
SQ SEQUENCE 453 AA; 47754 MW; 40AA14EF186A6009 CRC64;
MGVLGRVLLW LQLCALTQAV SKLWVPNTDF DVAANWSQNR TPCAGGAVEF PADKMVSVLV
QEGHAVSDML LPLDGELVLA SGAGFGVSDV GSHLDCGAGE PAVFRDSDRF SWHDPHLWRS
GDEAPGLFFV DAERVPCRHD DVFFPPSASF RVGLGPGASP VRVRSISALG RTFTRDEDLA
VFLASRAGRL RFHGPGALSV GPEDCADPSG CVCGNAEAQP WICAALLQPL GGRCPQAACH
SALRPQGQCC DLCGAVVLLT HGPAFDLERY RARILDTFLG LPQYHGLQVA VSKVPRSSRL
READTEIQVV LVENGPETGG AGRLARALLA DVAENGEALG VLEATMRESG AHVWGSSAAG
LAGGVAAAVL LALLVLLVAP PLLRRAGRLR WRRHEAAAPA GAPLGFRNPV FDVTASEELP
LPRRLSLVPK AAADSTSHSY FVNPLFAGAE AEA
