ID TCO2_HUMAN Reviewed; 427 AA. AC P20062; Q96FD4; Q9BVI8; Q9UCI5; Q9UCI6; Q9UDM0; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 3. DT 27-MAR-2024, entry version 213. DE RecName: Full=Transcobalamin-2; DE Short=TC-2; DE AltName: Full=Transcobalamin II; DE Short=TC II; DE Short=TCII; DE Flags: Precursor; GN Name=TCN2; Synonyms=TC2; 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), AND VARIANTS THR-198; LEU-219; RP PRO-259 AND SER-376. RX PubMed=1708393; DOI=10.1016/s0021-9258(20)89528-3; RA Platica O., Janeczko R., Quadros E.V., Regec A., Romain R., RA Rothenberg S.P.; RT "The cDNA sequence and the deduced amino acid sequence of human RT transcobalamin II show homology with rat intrinsic factor and human RT transcobalamin I."; RL J. Biol. Chem. 266:7860-7863(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8439564; DOI=10.1016/0167-4781(93)90264-e; RA Li N., Seetharam S., Lindemans J., Alpers D.H., Arwert F., Seetharam B.; RT "Isolation and sequence analysis of variant forms of human transcobalamin RT II."; RL Biochim. Biophys. Acta 1172:21-30(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7742531; RA Regec A., Quadros E.V., Platica O., Rothenberg S.P.; RT "The cloning and characterization of the human transcobalamin II gene."; RL Blood 85:2711-2719(1995). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-259. RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP GLN-227. RC TISSUE=Brain, and Eye; 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 [7] RP PROTEIN SEQUENCE OF 19-37, AND SUBCELLULAR LOCATION. RX PubMed=3782074; DOI=10.1016/s0021-9258(18)66733-x; RA Quadros E.V., Rothenberg S.P., Pan Y.C.E., Stein S.; RT "Purification and molecular characterization of human transcobalamin II."; RL J. Biol. Chem. 261:15455-15460(1986). RN [8] RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=8443384; RA Quadros E.V., Sai P., Rothenberg S.P.; RT "Functional human transcobalamin II isoproteins are secreted by insect RT cells using the baculovirus expression system."; RL Blood 81:1239-1245(1993). RN [9] {ECO:0007744|PDB:2BB5} RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 19-427 IN COMPLEX WITH COBALAMIN, RP AND DISULFIDE BONDS. RX PubMed=16537422; DOI=10.1073/pnas.0509099103; RA Wuerges J., Garau G., Geremia S., Fedosov S.N., Petersen T.E., RA Randaccio L.; RT "Structural basis for mammalian vitamin B12 transport by transcobalamin."; RL Proc. Natl. Acad. Sci. U.S.A. 103:4386-4391(2006). RN [10] {ECO:0007744|PDB:4ZRP, ECO:0007744|PDB:4ZRQ} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 19-427 IN COMPLEX WITH COBALAMIN RP AND CD320, INTERACTION WITH CD320, AND DISULFIDE BONDS. RX PubMed=27411955; DOI=10.1038/ncomms12100; RA Alam A., Woo J.S., Schmitz J., Prinz B., Root K., Chen F., Bloch J.S., RA Zenobi R., Locher K.P.; RT "Structural basis of transcobalamin recognition by human CD320 receptor."; RL Nat. Commun. 7:12100-12100(2016). RN [11] RP VARIANT PRO-259, AND POLYMORPHISM. RX PubMed=11159542; DOI=10.1182/blood.v97.4.1092; RA Namour F., Olivier J., Abdelmouttaleb I., Adjalla C., Debard R., Salvat C., RA Gueant J.; RT "Transcobalamin codon 259 polymorphism in HT-29 and Caco-2 cells and in RT Caucasians: relation to transcobalamin and homocysteine concentration in RT blood."; RL Blood 97:1092-1098(2001). CC -!- FUNCTION: Primary vitamin B12-binding and transport protein. Delivers CC cobalamin to cells. {ECO:0000269|PubMed:8443384}. CC -!- SUBUNIT: Interacts with CD320 (via LDL-receptor class A domains). CC {ECO:0000269|PubMed:27411955}. CC -!- INTERACTION: CC P20062; Q9NPF0: CD320; NbExp=11; IntAct=EBI-2853005, EBI-1054562; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3782074, CC ECO:0000269|PubMed:8443384}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P20062-1; Sequence=Displayed; CC Name=2; CC IsoId=P20062-2; Sequence=VSP_043711; CC -!- POLYMORPHISM: Pro/Arg-259 polymorphism affects TCN2 plasma CC concentration and may interfere in vitamin B(12) cellular availability CC and homocysteine metabolism (PubMed:11159542). CC {ECO:0000269|PubMed:11159542}. CC -!- DISEASE: Transcobalamin II deficiency (TCN2 deficiency) [MIM:275350]: CC Results in various forms of anemia. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the eukaryotic cobalamin transport proteins CC family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=TCN2base; Note=TCN2 mutation db; CC URL="http://structure.bmc.lu.se/idbase/TCN2base/"; 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; M60396; AAA61054.1; -; mRNA. DR EMBL; L02647; AAA61056.1; -; mRNA. DR EMBL; L02648; AAA61057.1; -; mRNA. DR EMBL; AF047576; AAC05491.1; -; Genomic_DNA. DR EMBL; CR456591; CAG30477.1; -; mRNA. DR EMBL; AC005006; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC001176; AAH01176.1; -; mRNA. DR EMBL; BC011239; AAH11239.1; -; mRNA. DR CCDS; CCDS13881.1; -. [P20062-1] DR CCDS; CCDS54519.1; -. [P20062-2] DR PIR; A39744; A39744. DR RefSeq; NP_000346.2; NM_000355.3. [P20062-1] DR RefSeq; NP_001171655.1; NM_001184726.1. [P20062-2] DR PDB; 2BB5; X-ray; 3.20 A; A/B=19-427. DR PDB; 4ZRP; X-ray; 2.10 A; A/B=19-427. DR PDB; 4ZRQ; X-ray; 2.60 A; A/B=19-427. DR PDB; 5NO0; X-ray; 1.57 A; A=325-427. DR PDB; 5NP4; X-ray; 1.43 A; A=325-427. DR PDB; 5NRP; X-ray; 1.57 A; A=325-427. DR PDB; 5NSA; X-ray; 1.27 A; A=325-427. DR PDB; 7QBD; X-ray; 4.18 A; A/B=19-427. DR PDB; 7QBE; X-ray; 3.00 A; A/C=19-427. DR PDB; 7QBF; X-ray; 1.85 A; A=19-427. DR PDB; 7QBG; X-ray; 2.69 A; A/C=19-427. DR PDBsum; 2BB5; -. DR PDBsum; 4ZRP; -. DR PDBsum; 4ZRQ; -. DR PDBsum; 5NO0; -. DR PDBsum; 5NP4; -. DR PDBsum; 5NRP; -. DR PDBsum; 5NSA; -. DR PDBsum; 7QBD; -. DR PDBsum; 7QBE; -. DR PDBsum; 7QBF; -. DR PDBsum; 7QBG; -. DR AlphaFoldDB; P20062; -. DR SMR; P20062; -. DR BioGRID; 112808; 12. DR IntAct; P20062; 3. DR STRING; 9606.ENSP00000215838; -. DR DrugBank; DB00115; Cyanocobalamin. DR DrugBank; DB00200; Hydroxocobalamin. DR DrugCentral; P20062; -. DR BioMuta; TCN2; -. DR DMDM; 224471876; -. DR EPD; P20062; -. DR jPOST; P20062; -. DR MassIVE; P20062; -. DR PaxDb; 9606-ENSP00000215838; -. DR PeptideAtlas; P20062; -. DR ProteomicsDB; 53720; -. [P20062-1] DR ProteomicsDB; 53721; -. [P20062-2] DR ABCD; P20062; 4 sequenced antibodies. DR Antibodypedia; 206; 265 antibodies from 27 providers. DR DNASU; 6948; -. DR Ensembl; ENST00000215838.8; ENSP00000215838.3; ENSG00000185339.10. [P20062-1] DR Ensembl; ENST00000407817.3; ENSP00000384914.3; ENSG00000185339.10. [P20062-2] DR GeneID; 6948; -. DR KEGG; hsa:6948; -. DR MANE-Select; ENST00000215838.8; ENSP00000215838.3; NM_000355.4; NP_000346.2. DR UCSC; uc003aip.3; human. [P20062-1] DR AGR; HGNC:11653; -. DR CTD; 6948; -. DR DisGeNET; 6948; -. DR GeneCards; TCN2; -. DR HGNC; HGNC:11653; TCN2. DR HPA; ENSG00000185339; Tissue enhanced (kidney). DR MalaCards; TCN2; -. DR MIM; 275350; phenotype. DR MIM; 613441; gene. DR neXtProt; NX_P20062; -. DR OpenTargets; ENSG00000185339; -. DR Orphanet; 859; Transcobalamin deficiency. DR PharmGKB; PA36404; -. DR VEuPathDB; HostDB:ENSG00000185339; -. DR eggNOG; ENOG502QSED; Eukaryota. DR GeneTree; ENSGT00530000063370; -. DR InParanoid; P20062; -. DR OMA; QCVKDSG; -. DR OrthoDB; 5354110at2759; -. DR PhylomeDB; P20062; -. DR TreeFam; TF333092; -. DR PathwayCommons; P20062; -. DR Reactome; R-HSA-3359454; Defective TCN2 causes TCN2 deficiency. DR Reactome; R-HSA-3359485; Defective CD320 causes MMATC. DR Reactome; R-HSA-9758890; Transport of RCbl within the body. DR SABIO-RK; P20062; -. DR SignaLink; P20062; -. DR BioGRID-ORCS; 6948; 11 hits in 1166 CRISPR screens. DR ChiTaRS; TCN2; human. DR EvolutionaryTrace; P20062; -. DR GenomeRNAi; 6948; -. DR Pharos; P20062; Tbio. DR PRO; PR:P20062; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; P20062; Protein. DR Bgee; ENSG00000185339; Expressed in gall bladder and 122 other cell types or tissues. DR ExpressionAtlas; P20062; baseline and differential. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0140355; F:cargo receptor ligand activity; EXP:Reactome. DR GO; GO:0031419; F:cobalamin binding; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015889; P:cobalamin transport; IDA:UniProtKB. DR GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW. DR Gene3D; 1.50.10.20; -; 1. DR Gene3D; 2.170.130.30; -; 1. DR InterPro; IPR002157; Cbl-bd_prot. DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase. DR InterPro; IPR027954; Transcobalamin-like_C. DR PANTHER; PTHR10559; TRANSCOBALAMIN-1/GASTRIC INTRINSIC FACTOR; 1. DR PANTHER; PTHR10559:SF14; TRANSCOBALAMIN-2; 1. DR Pfam; PF01122; Cobalamin_bind; 1. DR Pfam; PF14478; DUF4430; 1. DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1. DR PROSITE; PS00468; COBALAMIN_BINDING; 1. DR Genevisible; P20062; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cobalt; Cobalt transport; KW Direct protein sequencing; Disulfide bond; Ion transport; Metal-binding; KW Reference proteome; Secreted; Signal; Transport. FT SIGNAL 1..18 FT /evidence="ECO:0000269|PubMed:3782074" FT CHAIN 19..427 FT /note="Transcobalamin-2" FT /id="PRO_0000005564" FT BINDING 104 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /evidence="ECO:0000269|PubMed:16537422, FT ECO:0000269|PubMed:27411955, ECO:0007744|PDB:2BB5" FT BINDING 152..156 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /evidence="ECO:0000269|PubMed:16537422, FT ECO:0007744|PDB:2BB5" FT BINDING 190..194 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /evidence="ECO:0000269|PubMed:16537422, FT ECO:0007744|PDB:2BB5" FT BINDING 190 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /ligand_part="Co" FT /ligand_part_id="ChEBI:CHEBI:27638" FT /note="axial binding residue" FT BINDING 242 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /evidence="ECO:0000269|PubMed:16537422, FT ECO:0007744|PDB:2BB5" FT BINDING 245 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /evidence="ECO:0000269|PubMed:16537422, FT ECO:0000269|PubMed:27411955, ECO:0007744|PDB:2BB5" FT BINDING 291 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /evidence="ECO:0000269|PubMed:16537422" FT BINDING 395..397 FT /ligand="cob(II)alamin" FT /ligand_id="ChEBI:CHEBI:16304" FT /evidence="ECO:0000269|PubMed:16537422, FT ECO:0007744|PDB:2BB5" FT DISULFID 21..267 FT /evidence="ECO:0000269|PubMed:16537422, FT ECO:0000269|PubMed:27411955, ECO:0007744|PDB:2BB5, FT ECO:0007744|PDB:4ZRP, ECO:0007744|PDB:4ZRQ" FT DISULFID 83..96 FT /evidence="ECO:0000269|PubMed:27411955, FT ECO:0007744|PDB:4ZRP, ECO:0007744|PDB:4ZRQ" FT DISULFID 116..309 FT /evidence="ECO:0000269|PubMed:16537422, FT ECO:0000269|PubMed:27411955, ECO:0007744|PDB:2BB5, FT ECO:0007744|PDB:4ZRP, ECO:0007744|PDB:4ZRQ" FT DISULFID 165..205 FT /evidence="ECO:0000269|PubMed:16537422, FT ECO:0000269|PubMed:27411955, ECO:0007744|PDB:2BB5, FT ECO:0007744|PDB:4ZRP, ECO:0007744|PDB:4ZRQ" FT VAR_SEQ 116..143 FT /note="CEFVRGHKGDRLVSQLKWFLEDEKRAIG -> W (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_043711" FT VARIANT 23 FT /note="I -> V (in dbSNP:rs9606756)" FT /id="VAR_054539" FT VARIANT 89 FT /note="F -> L (in dbSNP:rs35915865)" FT /id="VAR_054540" FT VARIANT 198 FT /note="M -> T" FT /evidence="ECO:0000269|PubMed:1708393" FT /id="VAR_001638" FT VARIANT 215 FT /note="R -> W (in dbSNP:rs35838082)" FT /id="VAR_054541" FT VARIANT 219 FT /note="I -> L" FT /evidence="ECO:0000269|PubMed:1708393" FT /id="VAR_001639" FT VARIANT 227 FT /note="R -> Q (in dbSNP:rs17849434)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_054542" FT VARIANT 259 FT /note="R -> P (in dbSNP:rs1801198)" FT /evidence="ECO:0000269|PubMed:11159542, FT ECO:0000269|PubMed:15461802, ECO:0000269|PubMed:1708393" FT /id="VAR_001640" FT VARIANT 348 FT /note="S -> F (in dbSNP:rs9621049)" FT /id="VAR_054543" FT VARIANT 376 FT /note="L -> S (in dbSNP:rs1131603)" FT /evidence="ECO:0000269|PubMed:1708393" FT /id="VAR_001641" FT VARIANT 399 FT /note="R -> Q (in dbSNP:rs4820889)" FT /id="VAR_054544" FT HELIX 28..38 FT /evidence="ECO:0007829|PDB:7QBF" FT HELIX 39..43 FT /evidence="ECO:0007829|PDB:7QBF" FT TURN 47..49 FT /evidence="ECO:0007829|PDB:7QBF" FT HELIX 52..59 FT /evidence="ECO:0007829|PDB:7QBF" FT STRAND 61..64 FT /evidence="ECO:0007829|PDB:7QBF" FT HELIX 67..84 FT /evidence="ECO:0007829|PDB:7QBF" FT TURN 91..93 FT /evidence="ECO:0007829|PDB:7QBF" FT HELIX 102..114 FT /evidence="ECO:0007829|PDB:7QBF" FT HELIX 121..142 FT /evidence="ECO:0007829|PDB:7QBF" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:4ZRP" FT HELIX 154..166 FT /evidence="ECO:0007829|PDB:7QBF" FT HELIX 173..183 FT /evidence="ECO:0007829|PDB:7QBF" FT STRAND 184..186 FT /evidence="ECO:0007829|PDB:4ZRQ" FT HELIX 193..209 FT /evidence="ECO:0007829|PDB:7QBF" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:7QBF" FT HELIX 216..232 FT /evidence="ECO:0007829|PDB:7QBF" FT STRAND 240..242 FT /evidence="ECO:0007829|PDB:7QBF" FT TURN 243..245 FT /evidence="ECO:0007829|PDB:7QBF" FT HELIX 246..253 FT /evidence="ECO:0007829|PDB:7QBF" FT HELIX 263..279 FT /evidence="ECO:0007829|PDB:7QBF" FT HELIX 286..292 FT /evidence="ECO:0007829|PDB:7QBF" FT HELIX 295..297 FT /evidence="ECO:0007829|PDB:7QBF" FT HELIX 301..304 FT /evidence="ECO:0007829|PDB:7QBF" FT STRAND 328..336 FT /evidence="ECO:0007829|PDB:5NSA" FT STRAND 338..341 FT /evidence="ECO:0007829|PDB:5NSA" FT STRAND 343..350 FT /evidence="ECO:0007829|PDB:5NSA" FT HELIX 355..365 FT /evidence="ECO:0007829|PDB:5NSA" FT STRAND 370..373 FT /evidence="ECO:0007829|PDB:5NSA" FT STRAND 380..384 FT /evidence="ECO:0007829|PDB:5NSA" FT STRAND 393..399 FT /evidence="ECO:0007829|PDB:5NSA" FT TURN 400..402 FT /evidence="ECO:0007829|PDB:5NSA" FT TURN 409..411 FT /evidence="ECO:0007829|PDB:5NSA" FT STRAND 419..426 FT /evidence="ECO:0007829|PDB:5NSA" SQ SEQUENCE 427 AA; 47535 MW; FD04A110941989DB CRC64; MRHLGAFLFL LGVLGALTEM CEIPEMDSHL VEKLGQHLLP WMDRLSLEHL NPSIYVGLRL SSLQAGTKED LYLHSLKLGY QQCLLGSAFS EDDGDCQGKP SMGQLALYLL ALRANCEFVR GHKGDRLVSQ LKWFLEDEKR AIGHDHKGHP HTSYYQYGLG ILALCLHQKR VHDSVVDKLL YAVEPFHQGH HSVDTAAMAG LAFTCLKRSN FNPGRRQRIT MAIRTVREEI LKAQTPEGHF GNVYSTPLAL QFLMTSPMRG AELGTACLKA RVALLASLQD GAFQNALMIS QLLPVLNHKT YIDLIFPDCL APRVMLEPAA ETIPQTQEII SVTLQVLSLL PPYRQSISVL AGSTVEDVLK KAHELGGFTY ETQASLSGPY LTSVMGKAAG EREFWQLLRD PNTPLLQGIA DYRPKDGETI ELRLVSW //