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 27-MAR-2024, entry version 213. 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; P13569: CFTR; NbExp=7; IntAct=EBI-7172128, EBI-349854; 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}. 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; 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; 123. DR IntAct; P08582; 13. 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 GlyCosmos; P08582; 3 sites, 2 glycans. 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; 9606-ENSP00000296350; -. DR PeptideAtlas; P08582; -. DR ProteomicsDB; 52131; -. [P08582-1] DR ProteomicsDB; 52132; -. [P08582-2] DR Pumba; P08582; -. DR Antibodypedia; 1405; 407 antibodies from 33 providers. DR DNASU; 4241; -. DR Ensembl; ENST00000296350.10; ENSP00000296350.5; ENSG00000163975.14. [P08582-1] DR Ensembl; ENST00000296351.8; ENSP00000296351.4; ENSG00000163975.14. [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 AGR; HGNC:7037; -. DR CTD; 4241; -. DR DisGeNET; 4241; -. DR GeneCards; MELTF; -. DR HGNC; HGNC:7037; MELTF. DR HPA; ENSG00000163975; Tissue enhanced (kidney, salivary gland). 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; VNEMLQT; -. DR OrthoDB; 2906687at2759; -. 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 1138 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 149 other cell types or tissues. DR ExpressionAtlas; P08582; baseline and differential. 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; IDA:UniProtKB. DR GO; GO:0055037; C:recycling endosome; IBA:GO_Central. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IMP:UniProtKB. 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 CDD; cd13529; PBP2_transferrin; 2. DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 4. DR InterPro; IPR016357; Transferrin. DR InterPro; IPR001156; Transferrin-like_dom. DR InterPro; IPR018195; Transferrin_Fe_BS. DR PANTHER; PTHR11485:SF21; MELANOTRANSFERRIN; 1. DR PANTHER; PTHR11485; TRANSFERRIN; 1. DR Pfam; PF00405; Transferrin; 2. DR PIRSF; PIRSF002549; Transferrin; 1. DR PRINTS; PR00422; TRANSFERRIN. DR SMART; SM00094; TR_FER; 2. DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 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. DR Genevisible; P08582; HS. 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 //