TCO2_HUMAN
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 03-AUG-2022, entry version 204.
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 -!- 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/";
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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; 2.
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; P20062; -.
DR PeptideAtlas; P20062; -.
DR PRIDE; P20062; -.
DR ProteomicsDB; 53720; -. [P20062-1]
DR ProteomicsDB; 53721; -. [P20062-2]
DR Antibodypedia; 206; 236 antibodies from 27 providers.
DR DNASU; 6948; -.
DR Ensembl; ENST00000215838.8; ENSP00000215838.3; ENSG00000185339.9. [P20062-1]
DR Ensembl; ENST00000407817.3; ENSP00000384914.3; ENSG00000185339.9. [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 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; 1233171at2759; -.
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; 10 hits in 1088 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 120 other tissues.
DR ExpressionAtlas; P20062; baseline and differential.
DR Genevisible; P20062; HS.
DR GO; GO:0005768; C:endosome; TAS:Reactome.
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:0140355; F:cargo receptor ligand activity; IEA:Ensembl.
DR GO; GO:0031419; F:cobalamin binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009235; P:cobalamin metabolic process; IEA:Ensembl.
DR GO; GO:0015889; P:cobalamin transport; IDA:UniProtKB.
DR GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR002157; Cbl-bd_prot.
DR InterPro; IPR027954; DUF4430.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01122; Cobalamin_bind; 1.
DR Pfam; PF14478; DUF4430; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR PROSITE; PS00468; COBALAMIN_BINDING; 1.
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:4ZRP"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:4ZRP"
FT TURN 47..49
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:4ZRP"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 67..85
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 121..142
FT /evidence="ECO:0007829|PDB:4ZRP"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:4ZRP"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:4ZRQ"
FT HELIX 193..208
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 216..232
FT /evidence="ECO:0007829|PDB:4ZRP"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:4ZRP"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 246..253
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 263..279
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 286..296
FT /evidence="ECO:0007829|PDB:4ZRP"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:4ZRP"
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
