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}; 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; 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 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. DR Genevisible; Q5KU26; HS. 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 //