COL12_MOUSE
ID COL12_MOUSE Reviewed; 742 AA.
AC Q8K4Q8; Q3TYT8; Q8C979; Q8VIF6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Collectin-12;
DE AltName: Full=Collectin placenta protein 1;
DE Short=CL-P1;
DE AltName: Full=Scavenger receptor with C-type lectin;
GN Name=Colec12; Synonyms=Clp1, Srcl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=11718900; DOI=10.1016/s0167-4781(01)00284-6;
RA Nakamura K., Funakoshi H., Tokunaga F., Nakamura T.;
RT "Molecular cloning of a mouse scavenger receptor with C-type lectin (SRCL),
RT a novel member of the scavenger receptor family.";
RL Biochim. Biophys. Acta 1522:53-58(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 "cDNA cloning of mouse CL-P1 gene.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Inner ear;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary tumor;
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 [5]
RP TISSUE SPECIFICITY.
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 [6]
RP INTERACTION WITH FIBRILLAR AMYLOID-BETA PEPTIDE, INDUCTION, AND TISSUE
RP 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 [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-67; ASN-159; ASN-168 AND
RP ASN-271.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 603-742 IN COMPLEX WITH GLYCAN
RP LEWIS X AND CALCIUM 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. Binds also to sialyl Lewis X or a
CC trisaccharide and asialo-orosomucoid (ASOR). Mediates the recognition,
CC internalization and degradation of oxidatively modified low density
CC lipoprotein (oxLDL) by vascular endothelial cells (By similarity).
CC Binds to several carbohydrates including Gal-type ligands, D-galactose,
CC L- and D-fucose, GalNAc, T and Tn antigens in a calcium-dependent
CC manner and internalizes specifically GalNAc in nurse-like cells (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:11718900}.
CC -!- SUBUNIT: The extracellular domain forms a stable trimer (By
CC similarity). The extracellular domain interacts with fibrillar amyloid-
CC beta peptide. {ECO:0000250, ECO:0000269|PubMed:16868960,
CC ECO:0000269|PubMed:17420244}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}. Note=Forms clusters on the cell
CC surface. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in vascular endothelial cells in the
CC heart, in perivascular macrophage and smooth muscle cells. Expressed in
CC plaques-surrounding reactive astrocytes located in cerebral cortex and
CC hippocampus and in leptomeningeal vessels showing characteristics of
CC cerebral amyloid angiopathy (CAA) in a double transgenic mouse model of
CC Alzheimer disease (at protein level). Strongly expressed in lung.
CC Moderately expressed in heart, skeletal muscle, spleen, liver, brain,
CC colon, testis, stomach and kidney. Expressed in neonatal astrocytes.
CC Expressed in reactive astrocytes and vascular/perivascular cells in the
CC brain of a double transgenic mouse model of Alzheimer disease.
CC {ECO:0000269|PubMed:11564734, ECO:0000269|PubMed:11718900,
CC ECO:0000269|PubMed:16868960}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 9 dpc, increases
CC progressively to a peak at 14 dpc and gradually decreases until 19 dpc.
CC {ECO:0000269|PubMed:11718900}.
CC -!- INDUCTION: Up-regulated in activated microglia and by fibrillar
CC amyloid-beta peptide in activated astrocytes.
CC {ECO:0000269|PubMed:16868960}.
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DR EMBL; AB038519; BAB82497.1; -; mRNA.
DR EMBL; AB078434; BAC05523.1; -; mRNA.
DR EMBL; AK042772; BAC31361.1; -; mRNA.
DR EMBL; AK158366; BAE34474.1; -; mRNA.
DR EMBL; BC057936; AAH57936.1; -; mRNA.
DR CCDS; CCDS37732.1; -.
DR RefSeq; NP_569716.2; NM_130449.2.
DR PDB; 2OX9; X-ray; 1.95 A; A/B/C/D=603-742.
DR PDBsum; 2OX9; -.
DR AlphaFoldDB; Q8K4Q8; -.
DR SMR; Q8K4Q8; -.
DR STRING; 10090.ENSMUSP00000043220; -.
DR UniLectin; Q8K4Q8; -.
DR GlyConnect; 2222; 1 N-Linked glycan (1 site).
DR GlyGen; Q8K4Q8; 5 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q8K4Q8; -.
DR PhosphoSitePlus; Q8K4Q8; -.
DR MaxQB; Q8K4Q8; -.
DR PaxDb; Q8K4Q8; -.
DR PeptideAtlas; Q8K4Q8; -.
DR PRIDE; Q8K4Q8; -.
DR ProteomicsDB; 283425; -.
DR Antibodypedia; 21901; 239 antibodies from 26 providers.
DR DNASU; 140792; -.
DR Ensembl; ENSMUST00000234965; ENSMUSP00000157132; ENSMUSG00000036103.
DR GeneID; 140792; -.
DR KEGG; mmu:140792; -.
DR UCSC; uc008eak.2; mouse.
DR CTD; 81035; -.
DR MGI; MGI:2152907; Colec12.
DR VEuPathDB; HostDB:ENSMUSG00000036103; -.
DR eggNOG; ENOG502QQKQ; Eukaryota.
DR GeneTree; ENSGT00950000183074; -.
DR HOGENOM; CLU_022132_0_0_1; -.
DR InParanoid; Q8K4Q8; -.
DR OMA; KDMDKGQ; -.
DR OrthoDB; 565046at2759; -.
DR PhylomeDB; Q8K4Q8; -.
DR TreeFam; TF332426; -.
DR BioGRID-ORCS; 140792; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Colec12; mouse.
DR EvolutionaryTrace; Q8K4Q8; -.
DR PRO; PR:Q8K4Q8; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q8K4Q8; protein.
DR Bgee; ENSMUSG00000036103; Expressed in humerus cartilage element and 211 other tissues.
DR ExpressionAtlas; Q8K4Q8; baseline and differential.
DR Genevisible; Q8K4Q8; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0016021; C:integral component of membrane; ISS:MGI.
DR GO; GO:0030246; F:carbohydrate binding; ISS:MGI.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038187; F:pattern recognition receptor activity; ISS:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0071360; P:cellular response to exogenous dsRNA; IEA:Ensembl.
DR GO; GO:0042742; P:defense response to bacterium; ISO:MGI.
DR GO; GO:0006955; P:immune response; IDA:MGI.
DR GO; GO:0006910; P:phagocytosis, recognition; ISS:UniProtKB.
DR GO; GO:0044857; P:plasma membrane raft organization; ISO:MGI.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; ISO:MGI.
DR CDD; cd03590; CLECT_DC-SIGN_like; 1.
DR Gene3D; 3.10.100.10; -; 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 Pfam; PF01391; Collagen; 3.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 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_0000318682"
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 452..511
FT /note="Collagen-like 1"
FT DOMAIN 527..586
FT /note="Collagen-like 2"
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..142
FT /evidence="ECO:0000255"
FT COILED 205..254
FT /evidence="ECO:0000255"
FT COMPBIAS 519..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 BINDING 694
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
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 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 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 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 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:0000269|PubMed:19656770"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
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 CONFLICT 22
FT /note="Q -> H (in Ref. 1; BAB82497)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="K -> I (in Ref. 1; BAB82497)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="T -> S (in Ref. 1; BAB82497)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="Q -> L (in Ref. 3; BAC31361)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="S -> N (in Ref. 1; BAB82497)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="R -> W (in Ref. 1; BAB82497)"
FT /evidence="ECO:0000305"
FT CONFLICT 628
FT /note="F -> L (in Ref. 1; BAB82497)"
FT /evidence="ECO:0000305"
FT STRAND 612..614
FT /evidence="ECO:0007829|PDB:2OX9"
FT STRAND 617..621
FT /evidence="ECO:0007829|PDB:2OX9"
FT HELIX 628..637
FT /evidence="ECO:0007829|PDB:2OX9"
FT HELIX 648..656
FT /evidence="ECO:0007829|PDB:2OX9"
FT STRAND 660..662
FT /evidence="ECO:0007829|PDB:2OX9"
FT STRAND 664..669
FT /evidence="ECO:0007829|PDB:2OX9"
FT STRAND 671..673
FT /evidence="ECO:0007829|PDB:2OX9"
FT TURN 698..702
FT /evidence="ECO:0007829|PDB:2OX9"
FT STRAND 708..711
FT /evidence="ECO:0007829|PDB:2OX9"
FT HELIX 713..715
FT /evidence="ECO:0007829|PDB:2OX9"
FT STRAND 717..720
FT /evidence="ECO:0007829|PDB:2OX9"
FT STRAND 726..733
FT /evidence="ECO:0007829|PDB:2OX9"
SQ SEQUENCE 742 AA; 81304 MW; 1537C490E5911C45 CRC64;
MKDDFAEEEE VQSFGYKRFG IQEGTQCTKC KNNWALKFSI VLLYILCALL TITVAILGYK
VVEKMDNVTD GMETSHQTYD NKLTAVESDL KKLGDQAGKK ALSTNSELST FRSDILDLRQ
QLQEITEKTS KNKDTLEKLQ ANGDSLVDRQ SQLKETLQNN SFLITTVNKT LQAYNGYVTN
LQQDTSVLQG NLQSQMYSQS VVIMNLNNLN LTQVQQRNLI SNLQQSVDDT SLAIQRIKND
FQNLQQVFLQ AKKDTDWLKE KVQSLQTLAA NNSALAKANN DTLEDMNSQL SSFTGQMDNI
TTISQANEQS LKDLQDLHKD TENRTAVKFS QLEERFQVFE TDIVNIISNI SYTAHHLRTL
TSNLNDVRTT CTDTLTRHTD DLTSLNNTLV NIRLDSISLR MQQDMMRSKL DTEVANLSVV
MEEMKLVDSK HGQLIKNFTI LQGPPGPRGP KGDRGSQGPP GPTGNKGQKG EKGEPGPPGP
AGERGTIGPV GPPGERGSKG SKGSQGPKGS RGSPGKPGPQ GPSGDPGPPG PPGKDGLPGP
QGPPGFQGLQ GTVGEPGVPG PRGLPGLPGV PGMPGPKGPP GPPGPSGAME PLALQNEPTP
ASEVNGCPPH WKNFTDKCYY FSLEKEIFED AKLFCEDKSS HLVFINSREE QQWIKKHTVG
RESHWIGLTD SEQESEWKWL DGSPVDYKNW KAGQPDNWGS GHGPGEDCAG LIYAGQWNDF
QCDEINNFIC EKEREAVPSS IL
