TRFM_HUMAN
ID TRFM_HUMAN Reviewed; 738 AA.
AC P08582; Q9BQE2;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 204.
DE RecName: Full=Melanotransferrin {ECO:0000312|HGNC:HGNC:7037};
DE AltName: Full=Melanoma-associated antigen p97;
DE AltName: CD_antigen=CD228;
DE Flags: Precursor;
GN Name=MELTF {ECO:0000312|HGNC:HGNC:7037}; Synonyms=MAP97, MFI2;
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).
RC TISSUE=Melanoma;
RX PubMed=2419904; DOI=10.1073/pnas.83.5.1261;
RA Rose T.M., Plowman G.D., Teplow D.B., Dreyer W.J., Hellstroem K.E.,
RA Brown J.P.;
RT "Primary structure of the human melanoma-associated antigen p97
RT (melanotransferrin) deduced from the mRNA sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:1261-1265(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skin, and Uterus;
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 [4]
RP PROTEIN SEQUENCE OF 20-30.
RX PubMed=2463331; DOI=10.1084/jem.169.2.585;
RA Furukawa K.S., Furukawa K., Real F.X., Old L.J., Lloyd K.O.;
RT "A unique antigenic epitope of human melanoma is carried on the common
RT melanoma glycoprotein gp95/p97.";
RL J. Exp. Med. 169:585-590(1989).
RN [5]
RP GPI-ANCHOR.
RX PubMed=8300636; DOI=10.1016/s0021-9258(17)42043-6;
RA Food M.R., Rothenberger S., Gabathuler R., Haidl I.D., Reid G.,
RA Jefferies W.A.;
RT "Transport and expression in human melanomas of a transferrin-like
RT glycosylphosphatidylinositol-anchored protein.";
RL J. Biol. Chem. 269:3034-3040(1994).
RN [6]
RP FUNCTION.
RX PubMed=7556058; DOI=10.1002/j.1460-2075.1995.tb00091.x;
RA Kennard M.L., Richardson D.R., Gabathuler R., Ponka P., Jefferies W.A.;
RT "A novel iron uptake mechanism mediated by GPI-anchored human p97.";
RL EMBO J. 14:4178-4186(1995).
RN [7]
RP IRON-BINDING.
RX PubMed=1544447; DOI=10.1016/0014-5793(92)80060-t;
RA Baker E.N., Baker H.M., Smith C.A., Stebbins M.R., Kahn M.,
RA Hellstroem K.E., Hellstroem I.;
RT "Human melanotransferrin (p97) has only one functional iron-binding site.";
RL FEBS Lett. 298:215-218(1992).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP PHOSPHORYLATION AT SER-462.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [10]
RP 3D-STRUCTURE MODELING.
RX PubMed=1633859; DOI=10.1016/0014-5793(92)80654-y;
RA Garrat R.C., Jhoti H.;
RT "A molecular model for the tumour-associated antigen, p97, suggests a Zn-
RT binding function.";
RL FEBS Lett. 305:55-61(1992).
CC -!- FUNCTION: Involved in iron cellular uptake. Seems to be internalized
CC and then recycled back to the cell membrane. Binds a single atom of
CC iron per subunit. Could also bind zinc. {ECO:0000269|PubMed:7556058}.
CC -!- INTERACTION:
CC P08582-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10195914, EBI-3867333;
CC P08582-2; O60760: HPGDS; NbExp=3; IntAct=EBI-10195914, EBI-10187349;
CC P08582-2; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-10195914, EBI-11959885;
CC P08582-2; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-10195914, EBI-10171774;
CC P08582-2; Q14696: MESD; NbExp=3; IntAct=EBI-10195914, EBI-6165891;
CC P08582-2; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-10195914, EBI-945833;
CC P08582-2; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-10195914, EBI-22310682;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Lipid-anchor, GPI-
CC anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P08582-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P08582-2; Sequence=VSP_006557, VSP_006558;
CC -!- TISSUE SPECIFICITY: Found predominantly in human melanomas and in
CC certain fetal tissues; also found in liver, epithelium, umbilical
CC chord, placenta and sweat gland ducts.
CC -!- SIMILARITY: Belongs to the transferrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00741}.
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DR EMBL; M12154; AAA59992.1; -; mRNA.
DR EMBL; AC068302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001875; AAH01875.1; -; mRNA.
DR EMBL; BC002623; AAH02623.1; -; mRNA.
DR EMBL; BC007550; AAH07550.1; -; mRNA.
DR EMBL; BC071910; AAH71910.1; -; mRNA.
DR CCDS; CCDS3325.1; -. [P08582-1]
DR CCDS; CCDS3326.1; -. [P08582-2]
DR PIR; A23814; TFHUM.
DR RefSeq; NP_005920.2; NM_005929.5. [P08582-1]
DR RefSeq; NP_201573.1; NM_033316.3. [P08582-2]
DR PDB; 6XR0; X-ray; 3.06 A; M=1-738.
DR PDBsum; 6XR0; -.
DR AlphaFoldDB; P08582; -.
DR SMR; P08582; -.
DR BioGRID; 110399; 120.
DR IntAct; P08582; 11.
DR MINT; P08582; -.
DR STRING; 9606.ENSP00000296350; -.
DR MEROPS; S60.973; -.
DR MEROPS; S60.976; -.
DR GlyConnect; 1499; 2 N-Linked glycans (2 sites).
DR GlyGen; P08582; 3 sites, 2 N-linked glycans (2 sites).
DR iPTMnet; P08582; -.
DR PhosphoSitePlus; P08582; -.
DR BioMuta; MELTF; -.
DR DMDM; 338817914; -.
DR EPD; P08582; -.
DR jPOST; P08582; -.
DR MassIVE; P08582; -.
DR MaxQB; P08582; -.
DR PaxDb; P08582; -.
DR PeptideAtlas; P08582; -.
DR PRIDE; P08582; -.
DR ProteomicsDB; 52131; -. [P08582-1]
DR ProteomicsDB; 52132; -. [P08582-2]
DR Antibodypedia; 1405; 337 antibodies from 33 providers.
DR DNASU; 4241; -.
DR Ensembl; ENST00000296350.10; ENSP00000296350.5; ENSG00000163975.13. [P08582-1]
DR Ensembl; ENST00000296351.8; ENSP00000296351.4; ENSG00000163975.13. [P08582-2]
DR GeneID; 4241; -.
DR KEGG; hsa:4241; -.
DR MANE-Select; ENST00000296350.10; ENSP00000296350.5; NM_005929.6; NP_005920.2.
DR UCSC; uc003fxk.5; human. [P08582-1]
DR CTD; 4241; -.
DR DisGeNET; 4241; -.
DR GeneCards; MELTF; -.
DR HGNC; HGNC:7037; MELTF.
DR HPA; ENSG00000163975; Tissue enhanced (salivary).
DR MIM; 155750; gene.
DR neXtProt; NX_P08582; -.
DR OpenTargets; ENSG00000163975; -.
DR PharmGKB; PA30774; -.
DR VEuPathDB; HostDB:ENSG00000163975; -.
DR eggNOG; ENOG502QSZB; Eukaryota.
DR GeneTree; ENSGT00940000159265; -.
DR HOGENOM; CLU_011309_3_0_1; -.
DR InParanoid; P08582; -.
DR OMA; WNVPVGF; -.
DR PhylomeDB; P08582; -.
DR TreeFam; TF324013; -.
DR PathwayCommons; P08582; -.
DR Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; P08582; -.
DR BioGRID-ORCS; 4241; 12 hits in 1067 CRISPR screens.
DR ChiTaRS; MELTF; human.
DR GeneWiki; Melanotransferrin; -.
DR GenomeRNAi; 4241; -.
DR Pharos; P08582; Tbio.
DR PRO; PR:P08582; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P08582; protein.
DR Bgee; ENSG00000163975; Expressed in tibia and 148 other tissues.
DR ExpressionAtlas; P08582; baseline and differential.
DR Genevisible; P08582; HS.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IMP:UniProtKB.
DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR GO; GO:0006826; P:iron ion transport; IMP:UniProtKB.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR GO; GO:0090091; P:positive regulation of extracellular matrix disassembly; IDA:UniProtKB.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; IDA:UniProtKB.
DR InterPro; IPR029773; MTF.
DR InterPro; IPR016357; Transferrin.
DR InterPro; IPR001156; Transferrin-like_dom.
DR InterPro; IPR018195; Transferrin_Fe_BS.
DR PANTHER; PTHR11485:SF21; PTHR11485:SF21; 1.
DR Pfam; PF00405; Transferrin; 2.
DR PIRSF; PIRSF002549; Transferrin; 1.
DR PRINTS; PR00422; TRANSFERRIN.
DR SMART; SM00094; TR_FER; 2.
DR PROSITE; PS00205; TRANSFERRIN_LIKE_1; 2.
DR PROSITE; PS00206; TRANSFERRIN_LIKE_2; 2.
DR PROSITE; PS00207; TRANSFERRIN_LIKE_3; 2.
DR PROSITE; PS51408; TRANSFERRIN_LIKE_4; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW Ion transport; Iron; Iron transport; Lipoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transport; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:2463331"
FT CHAIN 20..709
FT /note="Melanotransferrin"
FT /evidence="ECO:0000255"
FT /id="PRO_0000035739"
FT PROPEP 710..738
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000035740"
FT DOMAIN 23..357
FT /note="Transferrin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DOMAIN 366..706
FT /note="Transferrin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT REGION 20..30
FT /note="Antigenic epitope"
FT BINDING 78
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 107
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 132
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 136
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 138
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 139
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 210
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 279
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 421
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 451
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 556
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT BINDING 625
FT /ligand="Fe(3+)"
FT /ligand_id="ChEBI:CHEBI:29034"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT MOD_RES 462
FT /note="Phosphoserine; by FAM20C"
FT /evidence="ECO:0000269|PubMed:26091039"
FT LIPID 709
FT /note="GPI-anchor amidated cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..63
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 36..54
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 130..216
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 172..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 186..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT DISULFID 257..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00741"
FT VAR_SEQ 238..302
FT /note="GKTLPSWGQALLSQDFELLCRDGSRADVTEWRQCHLARVPAHAVVVRADTDG
FT GLIFRLLNEGQRL -> ESPSRRQTWTRSEEEEGECPAHEEARRTMRSSAGQAWKWAPV
FT HRPQDESDKGEFGKRAKSRDMLG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006557"
FT VAR_SEQ 303..738
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_006558"
FT VARIANT 294
FT /note="R -> W (in dbSNP:rs2276790)"
FT /id="VAR_020413"
FT VARIANT 559
FT /note="A -> T (in dbSNP:rs17129219)"
FT /id="VAR_057304"
FT CONFLICT 431
FT /note="T -> K (in Ref. 1; AAA59992)"
FT /evidence="ECO:0000305"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 30..45
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 60..68
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 79..87
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:6XR0"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 105..116
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:6XR0"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 141..150
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 160..167
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 209..218
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:6XR0"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:6XR0"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 273..277
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 280..287
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 290..302
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 346..355
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 373..388
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 392..399
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 403..411
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 422..431
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 435..442
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 452..458
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:6XR0"
FT TURN 483..486
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 487..495
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 506..513
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 514..518
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 529..532
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 555..564
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 569..574
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 577..580
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 589..592
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 596..598
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 599..602
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 608..610
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 611..616
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 626..629
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 635..649
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:6XR0"
FT TURN 664..667
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 668..670
FT /evidence="ECO:0007829|PDB:6XR0"
FT STRAND 677..681
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 689..693
FT /evidence="ECO:0007829|PDB:6XR0"
FT HELIX 695..705
FT /evidence="ECO:0007829|PDB:6XR0"
SQ SEQUENCE 738 AA; 80215 MW; B0F08B708D2A0A0F CRC64;
MRGPSGALWL LLALRTVLGG MEVRWCATSD PEQHKCGNMS EAFREAGIQP SLLCVRGTSA
DHCVQLIAAQ EADAITLDGG AIYEAGKEHG LKPVVGEVYD QEVGTSYYAV AVVRRSSHVT
IDTLKGVKSC HTGINRTVGW NVPVGYLVES GRLSVMGCDV LKAVSDYFGG SCVPGAGETS
YSESLCRLCR GDSSGEGVCD KSPLERYYDY SGAFRCLAEG AGDVAFVKHS TVLENTDGKT
LPSWGQALLS QDFELLCRDG SRADVTEWRQ CHLARVPAHA VVVRADTDGG LIFRLLNEGQ
RLFSHEGSSF QMFSSEAYGQ KDLLFKDSTS ELVPIATQTY EAWLGHEYLH AMKGLLCDPN
RLPPYLRWCV LSTPEIQKCG DMAVAFRRQR LKPEIQCVSA KSPQHCMERI QAEQVDAVTL
SGEDIYTAGK TYGLVPAAGE HYAPEDSSNS YYVVAVVRRD SSHAFTLDEL RGKRSCHAGF
GSPAGWDVPV GALIQRGFIR PKDCDVLTAV SEFFNASCVP VNNPKNYPSS LCALCVGDEQ
GRNKCVGNSQ ERYYGYRGAF RCLVENAGDV AFVRHTTVFD NTNGHNSEPW AAELRSEDYE
LLCPNGARAE VSQFAACNLA QIPPHAVMVR PDTNIFTVYG LLDKAQDLFG DDHNKNGFKM
FDSSNYHGQD LLFKDATVRA VPVGEKTTYR GWLGLDYVAA LEGMSSQQCS GAAAPAPGAP
LLPLLLPALA ARLLPPAL
