CD166_MOUSE
ID CD166_MOUSE Reviewed; 583 AA.
AC Q61490; O70136; Q8CDA5; Q8R2T0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=CD166 antigen;
DE AltName: Full=Activated leukocyte cell adhesion molecule {ECO:0000303|PubMed:9209500};
DE AltName: Full=BEN {ECO:0000303|PubMed:15345243};
DE AltName: Full=Protein DM-GRASP {ECO:0000303|PubMed:8089660};
DE AltName: CD_antigen=CD166;
DE Flags: Precursor;
GN Name=Alcam;
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], INTERACTION WITH CD6, SUBCELLULAR LOCATION,
RP DOMAIN, AND TISSUE SPECIFICITY.
RC STRAIN=NFS;
RX PubMed=9209500; DOI=10.1002/eji.1830270625;
RA Bowen M.A., Bajorath J., D'Egidio M., Whitney G.S., Palmer D., Kobarg J.,
RA Starling G.C., Siadak A.W., Aruffo A.;
RT "Characterization of mouse ALCAM (CD166): the CD6 binding domain is
RT conserved in different homologs and mediates cross-species binding.";
RL Eur. J. Immunol. 27:1469-1478(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 227-583.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8089660; DOI=10.1002/neu.480250708;
RA Kanki J.P., Chang S., Kuwada J.Y.;
RT "The molecular cloning and characterization of potential chick DM-GRASP
RT homologs in zebrafish and mouse.";
RL J. Neurobiol. 25:831-845(1994).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=15345243; DOI=10.1016/j.mcn.2004.06.005;
RA Weiner J.A., Koo S.J., Nicolas S., Fraboulet S., Pfaff S.L., Pourquie O.,
RA Sanes J.R.;
RT "Axon fasciculation defects and retinal dysplasias in mice lacking the
RT immunoglobulin superfamily adhesion molecule BEN/ALCAM/SC1.";
RL Mol. Cell. Neurosci. 27:59-69(2004).
RN [6]
RP INTERACTION WITH CD6, AND SUBCELLULAR LOCATION.
RX PubMed=16914752; DOI=10.1128/mcb.00688-06;
RA Hassan N.J., Simmonds S.J., Clarkson N.G., Hanrahan S., Puklavec M.J.,
RA Bomb M., Barclay A.N., Brown M.H.;
RT "CD6 regulates T-cell responses through activation-dependent recruitment of
RT the positive regulator SLP-76.";
RL Mol. Cell. Biol. 26:6727-6738(2006).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-95; ASN-167; ASN-457 AND
RP ASN-499.
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=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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 FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=23169771; DOI=10.1096/fj.12-217844;
RA Iolyeva M., Karaman S., Willrodt A.H., Weingartner S., Vigl B., Halin C.;
RT "Novel role for ALCAM in lymphatic network formation and function.";
RL FASEB J. 27:978-990(2013).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=24740813; DOI=10.1182/blood-2014-03-565721;
RA Chitteti B.R., Kobayashi M., Cheng Y., Zhang H., Poteat B.A.,
RA Broxmeyer H.E., Pelus L.M., Hanenberg H., Zollman A., Kamocka M.M.,
RA Carlesso N., Cardoso A.A., Kacena M.A., Srour E.F.;
RT "CD166 regulates human and murine hematopoietic stem cells and the
RT hematopoietic niche.";
RL Blood 124:519-529(2014).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25730656;
RA Hooker R.A., Chitteti B.R., Egan P.H., Cheng Y.H., Himes E.R., Meijome T.,
RA Srour E.F., Fuchs R.K., Kacena M.A.;
RT "Activated leukocyte cell adhesion molecule (ALCAM or CD166) modulates bone
RT phenotype and hematopoiesis.";
RL J. Musculoskelet. Neuronal Interact. 15:83-94(2015).
CC -!- FUNCTION: Cell adhesion molecule that mediates both heterotypic cell-
CC cell contacts via its interaction with CD6, as well as homotypic cell-
CC cell contacts. Promotes T-cell activation and proliferation via its
CC interactions with CD6 (By similarity). Contributes to the formation and
CC maturation of the immunological synapse via its interactions with CD6
CC (By similarity). Mediates homotypic interactions with cells that
CC express ALCAM (PubMed:24740813). Mediates attachment of dendritic cells
CC onto endothelial cells via homotypic interaction. Inhibits endothelial
CC cell migration and promotes endothelial tube formation via homotypic
CC interactions (PubMed:23169771). Required for normal organization of the
CC lymph vessel network (PubMed:23169771). Required for normal
CC hematopoietic stem cell engraftment in the bone marrow
CC (PubMed:24740813). Plays a role in hematopoiesis; required for normal
CC numbers of hematopoietic stem cells in bone marrow (PubMed:25730656).
CC Promotes in vitro osteoblast proliferation and differentiation
CC (PubMed:25730656). Promotes neurite extension, axon growth and axon
CC guidance; axons grow preferentially on surfaces that contain ALCAM (By
CC similarity). Mediates outgrowth and pathfinding for retinal ganglion
CC cell axons (PubMed:15345243). {ECO:0000250|UniProtKB:P42292,
CC ECO:0000250|UniProtKB:Q13740, ECO:0000269|PubMed:15345243,
CC ECO:0000269|PubMed:23169771}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts (via extracellular
CC domain) with CD6 (via extracellular domain) (PubMed:9209500,
CC PubMed:16914752). Homodimerization and interaction with CD6 involve the
CC same region and cannot occur simultaneously. The affinity for CD6 is
CC much higher than the affinity for self-association. Interacts (via
CC glycosylated extracellular domain) with LGALS1 and LGALS3. Interaction
CC with LGALS1 or LGALS3 inhibits interaction with CD6.
CC {ECO:0000250|UniProtKB:Q13740, ECO:0000269|PubMed:16914752,
CC ECO:0000269|PubMed:9209500}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15345243,
CC ECO:0000269|PubMed:16914752, ECO:0000269|PubMed:23169771,
CC ECO:0000269|PubMed:9209500}; Single-pass type I membrane protein
CC {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:15345243}.
CC Cell projection, dendrite {ECO:0000269|PubMed:15345243}. Note=Detected
CC at the immunological synapse, i.e, at the contact zone between antigen-
CC presenting dendritic cells and T-cells. Colocalizes with CD6 and the
CC TCR/CD3 complex at the immunological synapse.
CC {ECO:0000250|UniProtKB:Q13740}.
CC -!- TISSUE SPECIFICITY: Detected on brain motor neurons, in differentiating
CC retinal ganglion cells and in adult retina (PubMed:15345243). Detected
CC on leukocytes and on lymphatic endothelial cells (PubMed:23169771).
CC Detected in spleen B cells and T-cells (at protein level)
CC (PubMed:9209500). Detected in adult brain and embryonic spinal cord
CC (PubMed:15345243). Expressed at high levels in the brain, and lung, and
CC at lower levels in the liver, and the kidney, as well as by activated
CC leukocytes (PubMed:9209500). {ECO:0000269|PubMed:15345243,
CC ECO:0000269|PubMed:23169771, ECO:0000269|PubMed:9209500}.
CC -!- DOMAIN: The CD6 binding site is located in the N-terminal Ig-like
CC domain. {ECO:0000269|PubMed:9209500}.
CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q13740}.
CC -!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian rate, are
CC viable and fertile and display no obvious external phenotype. Unlike
CC wild-type mice, that have tightly fasciculated and smooth nerve
CC bundles, mutant mice have more loosely bundled nerves with many single
CC axons extending out of the main nerve. Eyes from mutant mice display a
CC variable degree of retinal displasia (PubMed:15345243). Besides, lymph
CC nodes from mutant mice display reduced weight and cellularity, but
CC appear otherwise normal (PubMed:23169771). Mutant mice have only half
CC of the normal number of hematopoietic stem cells in their bone marrow
CC (PubMed:24740813, PubMed:25730656). Survival of lethally irradiated
CC mice that receive bone marrow from mutant mice is impaired, due to
CC impaired homotypic cell-cell attachment, impaired engraftment and
CC proliferation of mutant hematopoietic stem cells (PubMed:24740813).
CC Mutant mice are larger and heavier than wild-type and have increased
CC bone mineral density (PubMed:25730656). Mutant spleen has an altered
CC leukocyte composition, with reduced numbers of CD4(+) and CD8(+) T-
CC cells, B-cells, dendritic cells, neutrophils and macrophages, but no
CC change in the total leukocyte number. Their lungs display reduced
CC numbers of lymph vessel and blood vessel endothelial cells, but no
CC difference in lung weight. Lymph vessels in mesentery and diaphragm are
CC more densely interconnected and show a decreased level of hierarchical
CC vascular organization in mutant mice (PubMed:23169771).
CC {ECO:0000269|PubMed:15345243, ECO:0000269|PubMed:23169771,
CC ECO:0000269|PubMed:25730656}.
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DR EMBL; U95030; AAC06342.1; -; mRNA.
DR EMBL; AK030851; BAC27159.1; -; mRNA.
DR EMBL; AK031391; BAC27382.1; -; mRNA.
DR EMBL; BC027280; AAH27280.1; -; mRNA.
DR EMBL; L25274; AAA37528.1; -; mRNA.
DR CCDS; CCDS37356.1; -.
DR RefSeq; NP_033785.1; NM_009655.3.
DR AlphaFoldDB; Q61490; -.
DR SMR; Q61490; -.
DR BioGRID; 198061; 3.
DR STRING; 10090.ENSMUSP00000023312; -.
DR GlyConnect; 2196; 15 N-Linked glycans (4 sites).
DR GlyGen; Q61490; 8 sites, 15 N-linked glycans (4 sites).
DR iPTMnet; Q61490; -.
DR PhosphoSitePlus; Q61490; -.
DR CPTAC; non-CPTAC-3640; -.
DR EPD; Q61490; -.
DR jPOST; Q61490; -.
DR MaxQB; Q61490; -.
DR PaxDb; Q61490; -.
DR PeptideAtlas; Q61490; -.
DR PRIDE; Q61490; -.
DR ProteomicsDB; 281133; -.
DR Antibodypedia; 2625; 844 antibodies from 40 providers.
DR DNASU; 11658; -.
DR Ensembl; ENSMUST00000023312; ENSMUSP00000023312; ENSMUSG00000022636.
DR GeneID; 11658; -.
DR KEGG; mmu:11658; -.
DR UCSC; uc007zli.2; mouse.
DR CTD; 214; -.
DR MGI; MGI:1313266; Alcam.
DR VEuPathDB; HostDB:ENSMUSG00000022636; -.
DR eggNOG; ENOG502RMQM; Eukaryota.
DR GeneTree; ENSGT00940000156881; -.
DR HOGENOM; CLU_028888_2_0_1; -.
DR InParanoid; Q61490; -.
DR OMA; GIVYWLY; -.
DR OrthoDB; 536204at2759; -.
DR PhylomeDB; Q61490; -.
DR TreeFam; TF321859; -.
DR BioGRID-ORCS; 11658; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Alcam; mouse.
DR PRO; PR:Q61490; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q61490; protein.
DR Bgee; ENSMUSG00000022636; Expressed in olfactory tubercle and 296 other tissues.
DR ExpressionAtlas; Q61490; baseline and differential.
DR Genevisible; Q61490; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0001772; C:immunological synapse; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042101; C:T cell receptor complex; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0048846; P:axon extension involved in axon guidance; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:UniProtKB.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:MGI.
DR GO; GO:1990138; P:neuron projection extension; ISS:UniProtKB.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR039810; CD166_antigen.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR PANTHER; PTHR11973:SF2; PTHR11973:SF2; 1.
DR Pfam; PF08205; C2-set_2; 1.
DR SMART; SM00409; IG; 3.
DR SUPFAM; SSF48726; SSF48726; 4.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW Adaptive immunity; Cell adhesion; Cell membrane; Cell projection;
KW Disulfide bond; Glycoprotein; Immunity; Immunoglobulin domain; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..583
FT /note="CD166 antigen"
FT /id="PRO_0000014660"
FT TOPO_DOM 28..527
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..549
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..583
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..120
FT /note="Ig-like V-type 1"
FT DOMAIN 125..234
FT /note="Ig-like V-type 2"
FT DOMAIN 245..328
FT /note="Ig-like C2-type 1"
FT DOMAIN 333..409
FT /note="Ig-like C2-type 2"
FT DOMAIN 416..501
FT /note="Ig-like C2-type 3"
FT REGION 562..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 361
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT CARBOHYD 480
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19656770"
FT DISULFID 43..113
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 157..220
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 270..313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 354..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 435..485
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT CONFLICT 8
FT /note="S -> C (in Ref. 2; BAC27159)"
FT /evidence="ECO:0000305"
FT CONFLICT 227..232
FT /note="PSGQKT -> AAGIPA (in Ref. 4; AAA37528)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="S -> R (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="G -> S (in Ref. 2; BAC27159)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="S -> F (in Ref. 4; AAA37528)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 583 AA; 65092 MW; 570AFA8FCAF888F8 CRC64;
MASKVSPSCR LVFCLLISAA VLRPGLGWYT VNSAYGDTIV MPCRLDVPQN LMFGKWKYEK
PDGSPVFIAF RSSTKKSVQY DDVPEYKDRL SLSENYTLSI ANAKISDEKR FVCMLVTEDN
VFEAPTLVKV FKQPSKPEIV NKAPFLETDQ LKKLGDCISR DSYPDGNITW YRNGKVLQPV
EGEVAILFKK EIDPGTQLYT VTSSLEYKTT RSDIQMPFTC SVTYYGPSGQ KTIYSEQEIF
DIYYPTEQVT IQVLPPKNAI KEGDNITLQC LGNGNPPPEE FMFYLPGQPE GIRSSNTYTL
TDVRRNATGD YKCSLIDKRN MAASTTITVH YLDLSLNPSG EVTKQIGDTL PVSCTISASR
NATVVWMKDN IRLRSSPSFS SLHYQDAGNY VCETALQEVE GLKKRESLTL IVEGKPQIKM
TKKTDPSGLS KTIICHVEGF PKPAIHWTIT GSGSVINQTE ESPYINGRYY SKIIISPEEN
VTLTCTAENQ LERTVNSLNV SAISIPEHDE ADDISDENRE KVNDQAKLIV GIVVGLLLAA
LVAGVVYWLY MKKSKTASKH VNKDLGNMEE NKKLEENNHK TEA
