ID COL12_HUMAN Reviewed; 742 AA.
AC Q5KU26; Q6P9F2; Q8TCR2; Q8WZA4; Q9BY85; Q9BYH7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 27-MAR-2024, entry version 156.
DE RecName: Full=Collectin-12;
DE AltName: Full=Collectin placenta protein 1;
DE Short=CL-P1;
DE Short=hCL-P1;
DE AltName: Full=Nurse cell scavenger receptor 2;
DE AltName: Full=Scavenger receptor class A member 4;
DE AltName: Full=Scavenger receptor with C-type lectin;
GN Name=COLEC12; Synonyms=CLP1, NSR2, SCARA4, SRCL;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND VARIANTS PRO-522 AND SER-606.
RC TISSUE=Placenta;
RX PubMed=11162630; DOI=10.1006/bbrc.2000.4210;
RA Nakamura K., Funakoshi H., Miyamoto K., Tokunaga F., Nakamura T.;
RT "Molecular cloning and functional characterization of a human scavenger
RT receptor with C-type lectin (SRCL), a novel member of a scavenger receptor
RT family.";
RL Biochem. Biophys. Res. Commun. 280:1028-1035(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANT
RP PRO-522.
RC TISSUE=Lung, and Placenta;
RX PubMed=11564734; DOI=10.1074/jbc.m103942200;
RA Ohtani K., Suzuki Y., Eda S., Kawai T., Kase T., Keshi H., Sakai Y.,
RA Fukuoh A., Sakamoto T., Itabe H., Suzutani T., Ogasawara M., Yoshida I.,
RA Wakamiya N.;
RT "The membrane-type collectin CL-P1 is a scavenger receptor on vascular
RT endothelial cells.";
RL J. Biol. Chem. 276:44222-44228(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANT
RP PRO-522.
RX PubMed=12761161; DOI=10.1093/jb/mvg037;
RA Yoshida T., Tsuruta Y., Iwasaki M., Yamane S., Ochi T., Suzuki R.;
RT "SRCL/CL-P1 recognizes GalNAc and a carcinoma-associated antigen, Tn
RT antigen.";
RL J. Biochem. 133:271-277(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-91; PRO-522 AND
RP SER-606.
RC TISSUE=Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 326-742.
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP VARIANTS PRO-522 AND SER-606.
RX PubMed=12601552; DOI=10.1007/s100380300011;
RA Ohmori H., Makita Y., Funamizu M., Chiba S., Ohtani K., Suzuki Y.,
RA Wakamiya N., Hata A.;
RT "Haplotype analysis of the human collectin placenta 1 (hCL-P1) gene.";
RL J. Hum. Genet. 48:82-85(2003).
RN [8]
RP FUNCTION, AND SUBUNIT.
RX PubMed=15845541; DOI=10.1074/jbc.m504197200;
RA Coombs P.J., Graham S.A., Drickamer K., Taylor M.E.;
RT "Selective binding of the scavenger receptor C-type lectin to Lewis X
RT trisaccharide and related glycan ligands.";
RL J. Biol. Chem. 280:22993-22999(2005).
RN [9]
RP INTERACTION WITH FIBRILLAR AMYLOID-BETA PEPTIDE, FUNCTION IN CLEARANCE OF
RP AMYLOID-BETA, AND TISSUE SPECIFICITY.
RX PubMed=16868960; DOI=10.1002/jnr.20992;
RA Nakamura K., Ohya W., Funakoshi H., Sakaguchi G., Kato A., Takeda M.,
RA Kudo T., Nakamura T.;
RT "Possible role of scavenger receptor SRCL in the clearance of amyloid-beta
RT in Alzheimer's disease.";
RL J. Neurosci. Res. 84:874-890(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 603-742 IN COMPLEX WITH CALCIUM
RP IONS, AND DISULFIDE BONDS.
RX PubMed=17420244; DOI=10.1074/jbc.m701624200;
RA Feinberg H., Taylor M.E., Weis W.I.;
RT "Scavenger receptor C-type lectin binds to the leukocyte cell surface
RT glycan Lewis X by a novel mechanism.";
RL J. Biol. Chem. 282:17250-17258(2007).
CC -!- FUNCTION: Scavenger receptor that displays several functions associated
CC with host defense. Promotes binding and phagocytosis of Gram-positive,
CC Gram-negative bacteria and yeast. Mediates the recognition,
CC internalization and degradation of oxidatively modified low density
CC lipoprotein (oxLDL) by vascular endothelial cells. Binds to several
CC carbohydrates including Gal-type ligands, D-galactose, L- and D-fucose,
CC GalNAc, T and Tn antigens in a calcium-dependent manner and
CC internalizes specifically GalNAc in nurse-like cells. Binds also to
CC sialyl Lewis X or a trisaccharide and asialo-orosomucoid (ASOR). May
CC also play a role in the clearance of amyloid-beta in Alzheimer disease.
CC {ECO:0000269|PubMed:11162630, ECO:0000269|PubMed:11564734,
CC ECO:0000269|PubMed:12761161, ECO:0000269|PubMed:15845541,
CC ECO:0000269|PubMed:16868960}.
CC -!- SUBUNIT: The extracellular domain forms a stable trimer. The
CC extracellular domain interacts with fibrillar amyloid-beta peptide.
CC {ECO:0000269|PubMed:15845541, ECO:0000269|PubMed:16868960,
CC ECO:0000269|PubMed:17420244}.
CC -!- INTERACTION:
CC Q5KU26; P02741: CRP; NbExp=3; IntAct=EBI-1104680, EBI-1395983;
CC Q5KU26; Q9UKJ1: PILRA; NbExp=2; IntAct=EBI-1104680, EBI-965833;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11162630}; Single-
CC pass type II membrane protein {ECO:0000269|PubMed:11162630}. Note=Forms
CC clusters on the cell surface.
CC -!- TISSUE SPECIFICITY: Expressed in perivascular macrophages. Expressed in
CC plaques-surrounding reactive astrocytes and in perivascular astrocytes
CC associated with cerebral amyloid angiopathy (CAA) in the temporal
CC cortex of Alzheimer patient (at protein level). Strongly expressed in
CC placenta. Moderately expressed in heart, skeletal muscle, small
CC intestine and lung. Weakly expressed in brain, colon, thymus and
CC kidney. Expressed in nurse-like cells. Expressed in reactive astrocytes
CC and vascular/perivascular cells in the brain of Alzheimer patient.
CC {ECO:0000269|PubMed:11162630, ECO:0000269|PubMed:11564734,
CC ECO:0000269|PubMed:12761161, ECO:0000269|PubMed:16868960}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB39148.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AB038518; BAB39147.1; -; mRNA.
DR EMBL; AB052103; BAB39148.1; ALT_SEQ; mRNA.
DR EMBL; AB005145; BAB72147.1; -; mRNA.
DR EMBL; AB034251; BAD83592.1; -; mRNA.
DR EMBL; AP000915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP005240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060789; AAH60789.1; -; mRNA.
DR EMBL; AL713657; CAD28466.1; -; mRNA.
DR CCDS; CCDS32782.1; -.
DR PIR; JC7595; JC7595.
DR RefSeq; NP_569057.1; NM_130386.2.
DR PDB; 2OX8; X-ray; 2.50 A; A/B/C/D=607-742.
DR PDBsum; 2OX8; -.
DR AlphaFoldDB; Q5KU26; -.
DR SMR; Q5KU26; -.
DR BioGRID; 123353; 67.
DR IntAct; Q5KU26; 34.
DR STRING; 9606.ENSP00000383115; -.
DR UniLectin; Q5KU26; -.
DR GlyConnect; 1141; 1 N-Linked glycan (1 site).
DR GlyCosmos; Q5KU26; 5 sites, 1 glycan.
DR GlyGen; Q5KU26; 5 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q5KU26; -.
DR PhosphoSitePlus; Q5KU26; -.
DR SwissPalm; Q5KU26; -.
DR BioMuta; COLEC12; -.
DR DMDM; 296439391; -.
DR jPOST; Q5KU26; -.
DR MassIVE; Q5KU26; -.
DR MaxQB; Q5KU26; -.
DR PaxDb; 9606-ENSP00000383115; -.
DR PeptideAtlas; Q5KU26; -.
DR ProteomicsDB; 63550; -.
DR Pumba; Q5KU26; -.
DR Antibodypedia; 21901; 253 antibodies from 26 providers.
DR DNASU; 81035; -.
DR Ensembl; ENST00000400256.5; ENSP00000383115.3; ENSG00000158270.12.
DR GeneID; 81035; -.
DR KEGG; hsa:81035; -.
DR MANE-Select; ENST00000400256.5; ENSP00000383115.3; NM_130386.3; NP_569057.2.
DR UCSC; uc002kkm.4; human.
DR AGR; HGNC:16016; -.
DR CTD; 81035; -.
DR DisGeNET; 81035; -.
DR GeneCards; COLEC12; -.
DR HGNC; HGNC:16016; COLEC12.
DR HPA; ENSG00000158270; Tissue enhanced (cervix).
DR MIM; 607621; gene.
DR neXtProt; NX_Q5KU26; -.
DR OpenTargets; ENSG00000158270; -.
DR PharmGKB; PA26738; -.
DR VEuPathDB; HostDB:ENSG00000158270; -.
DR eggNOG; ENOG502QQKQ; Eukaryota.
DR GeneTree; ENSGT00950000183074; -.
DR HOGENOM; CLU_022132_0_0_1; -.
DR InParanoid; Q5KU26; -.
DR OMA; KMQQDLM; -.
DR OrthoDB; 4613106at2759; -.
DR PhylomeDB; Q5KU26; -.
DR TreeFam; TF332426; -.
DR PathwayCommons; Q5KU26; -.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
DR SignaLink; Q5KU26; -.
DR BioGRID-ORCS; 81035; 14 hits in 1148 CRISPR screens.
DR ChiTaRS; COLEC12; human.
DR EvolutionaryTrace; Q5KU26; -.
DR GenomeRNAi; 81035; -.
DR Pharos; Q5KU26; Tbio.
DR PRO; PR:Q5KU26; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q5KU26; Protein.
DR Bgee; ENSG00000158270; Expressed in synovial joint and 201 other cell types or tissues.
DR Genevisible; Q5KU26; HS.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; TAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005534; F:galactose binding; NAS:UniProtKB.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038187; F:pattern recognition receptor activity; IDA:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IDA:UniProtKB.
DR GO; GO:0009756; P:carbohydrate mediated signaling; NAS:UniProtKB.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; IMP:UniProtKB.
DR GO; GO:0006952; P:defense response; TAS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
DR GO; GO:0006910; P:phagocytosis, recognition; IDA:UniProtKB.
DR GO; GO:0044857; P:plasma membrane raft organization; IMP:GO_Central.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IMP:UniProtKB.
DR CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR033989; CD209-like_CTLD.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR016187; CTDL_fold.
DR PANTHER; PTHR22803:SF146; COLLECTIN-12; 1.
DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Coiled coil; Collagen; Disulfide bond; Glycoprotein;
KW Lectin; Membrane; Metal-binding; Receptor; Reference proteome; Repeat;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..742
FT /note="Collectin-12"
FT /id="PRO_0000318681"
FT TOPO_DOM 1..37
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..742
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 443..472
FT /note="Collagen-like 1"
FT DOMAIN 473..529
FT /note="Collagen-like 2"
FT DOMAIN 530..589
FT /note="Collagen-like 3"
FT DOMAIN 614..731
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 439..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 73..141
FT /evidence="ECO:0000255"
FT COILED 215..328
FT /evidence="ECO:0000255"
FT COMPBIAS 521..539
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..587
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 644
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 646
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 650
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT BINDING 670
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 674
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 691
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 694
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 694
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 696
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 696
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 697
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 706
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 706
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 706
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 707
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT BINDING 718
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 718
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 719
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250"
FT BINDING 719
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT BINDING 731
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 607..618
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:17420244"
FT DISULFID 635..730
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:17420244"
FT DISULFID 708..722
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:17420244"
FT VARIANT 91
FT /note="K -> E (in dbSNP:rs17855029)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_038853"
FT VARIANT 487
FT /note="I -> V (in dbSNP:rs8098850)"
FT /id="VAR_038854"
FT VARIANT 522
FT /note="S -> P (in dbSNP:rs2305025)"
FT /evidence="ECO:0000269|PubMed:11162630,
FT ECO:0000269|PubMed:11564734, ECO:0000269|PubMed:12601552,
FT ECO:0000269|PubMed:12761161, ECO:0000269|PubMed:15489334"
FT /id="VAR_038855"
FT VARIANT 606
FT /note="G -> S (in dbSNP:rs2305027)"
FT /evidence="ECO:0000269|PubMed:11162630,
FT ECO:0000269|PubMed:12601552, ECO:0000269|PubMed:15489334"
FT /id="VAR_038856"
FT CONFLICT 12
FT /note="Q -> P (in Ref. 1; BAB39148)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="Y -> F (in Ref. 1; BAB39148)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="Q -> H (in Ref. 1; BAB39148)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="T -> P (in Ref. 1; BAB39148)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="K -> H (in Ref. 1; BAB39148)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="M -> V (in Ref. 3; BAD83592)"
FT /evidence="ECO:0000305"
FT STRAND 612..614
FT /evidence="ECO:0007829|PDB:2OX8"
FT STRAND 617..621
FT /evidence="ECO:0007829|PDB:2OX8"
FT HELIX 628..637
FT /evidence="ECO:0007829|PDB:2OX8"
FT HELIX 648..657
FT /evidence="ECO:0007829|PDB:2OX8"
FT STRAND 664..669
FT /evidence="ECO:0007829|PDB:2OX8"
FT STRAND 671..673
FT /evidence="ECO:0007829|PDB:2OX8"
FT TURN 692..700
FT /evidence="ECO:0007829|PDB:2OX8"
FT STRAND 708..711
FT /evidence="ECO:0007829|PDB:2OX8"
FT STRAND 717..720
FT /evidence="ECO:0007829|PDB:2OX8"
FT STRAND 726..733
FT /evidence="ECO:0007829|PDB:2OX8"
SQ SEQUENCE 742 AA; 81515 MW; 85A003C1D6A83949 CRC64;
MKDDFAEEEE VQSFGYKRFG IQEGTQCTKC KNNWALKFSI ILLYILCALL TITVAILGYK
VVEKMDNVTG GMETSRQTYD DKLTAVESDL KKLGDQTGKK AISTNSELST FRSDILDLRQ
QLREITEKTS KNKDTLEKLQ ASGDALVDRQ SQLKETLENN SFLITTVNKT LQAYNGYVTN
LQQDTSVLQG NLQNQMYSHN VVIMNLNNLN LTQVQQRNLI TNLQRSVDDT SQAIQRIKND
FQNLQQVFLQ AKKDTDWLKE KVQSLQTLAA NNSALAKANN DTLEDMNSQL NSFTGQMENI
TTISQANEQN LKDLQDLHKD AENRTAIKFN QLEERFQLFE TDIVNIISNI SYTAHHLRTL
TSNLNEVRTT CTDTLTKHTD DLTSLNNTLA NIRLDSVSLR MQQDLMRSRL DTEVANLSVI
MEEMKLVDSK HGQLIKNFTI LQGPPGPRGP RGDRGSQGPP GPTGNKGQKG EKGEPGPPGP
AGERGPIGPA GPPGERGGKG SKGSQGPKGS RGSPGKPGPQ GSSGDPGPPG PPGKEGLPGP
QGPPGFQGLQ GTVGEPGVPG PRGLPGLPGV PGMPGPKGPP GPPGPSGAVV PLALQNEPTP
APEDNGCPPH WKNFTDKCYY FSVEKEIFED AKLFCEDKSS HLVFINTREE QQWIKKQMVG
RESHWIGLTD SERENEWKWL DGTSPDYKNW KAGQPDNWGH GHGPGEDCAG LIYAGQWNDF
QCEDVNNFIC EKDRETVLSS AL
//
