CD248_HUMAN
ID CD248_HUMAN Reviewed; 757 AA.
AC Q9HCU0; Q2M2V5; Q3SX55; Q96KB6;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Endosialin;
DE AltName: Full=Tumor endothelial marker 1;
DE AltName: CD_antigen=CD248;
DE Flags: Precursor;
GN Name=CD248; Synonyms=CD164L1, TEM1;
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 TISSUE SPECIFICITY.
RX PubMed=10947988; DOI=10.1126/science.289.5482.1197;
RA St Croix B., Rago C., Velculescu V.E., Traverso G., Romans K.E.,
RA Montgomery E., Lal A., Riggins G.J., Lengauer C., Vogelstein B.,
RA Kinzler K.W.;
RT "Genes expressed in human tumor endothelium.";
RL Science 289:1197-1202(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=11084048; DOI=10.1074/jbc.m009604200;
RA Christian S., Ahorn H., Koehler A., Eisenhaber F., Rodi H.P.,
RA Garin-Chesa P., Park J.E., Rettig W.J., Lenter M.C.;
RT "Molecular cloning and characterization of endosialin, a C-type lectin-like
RT cell surface receptor of tumor endothelium.";
RL J. Biol. Chem. 276:7408-7414(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ARG-457.
RC TISSUE=Brain;
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, AND GLYCOSYLATION.
RX PubMed=1438285; DOI=10.1073/pnas.89.22.10832;
RA Rettig W.J., Garin-Chesa P., Healey J.H., Su S.L., Jaffe E.A., Old L.J.;
RT "Identification of endosialin, a cell surface glycoprotein of vascular
RT endothelial cells in human cancer.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:10832-10836(1992).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=16076089;
RA Dolznig H., Schweifer N., Puri C., Kraut N., Rettig W.J., Kerjaschki D.,
RA Garin-Chesa P.;
RT "Characterization of cancer stroma markers: in silico analysis of an mRNA
RT expression database for fibroblast activation protein and endosialin.";
RL Cancer Immun. 5:10-10(2005).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15862292; DOI=10.1016/j.febslet.2005.03.071;
RA MacFadyen J.R., Haworth O., Roberston D., Hardie D., Webster M.T.,
RA Morris H.R., Panico M., Sutton-Smith M., Dell A., van der Geer P.,
RA Wienke D., Buckley C.D., Isacke C.M.;
RT "Endosialin (TEM1, CD248) is a marker of stromal fibroblasts and is not
RT selectively expressed on tumour endothelium.";
RL FEBS Lett. 579:2569-2575(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] PHE-6.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May play a role in tumor angiogenesis.
CC {ECO:0000269|PubMed:15862292}.
CC -!- INTERACTION:
CC Q9HCU0; P46379-2: BAG6; NbExp=3; IntAct=EBI-9680942, EBI-10988864;
CC Q9HCU0; Q9UMF0: ICAM5; NbExp=3; IntAct=EBI-9680942, EBI-6398041;
CC Q9HCU0; O14901: KLF11; NbExp=3; IntAct=EBI-9680942, EBI-948266;
CC Q9HCU0; Q13449: LSAMP; NbExp=3; IntAct=EBI-9680942, EBI-4314821;
CC Q9HCU0; P27361: MAPK3; NbExp=3; IntAct=EBI-9680942, EBI-73995;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HCU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HCU0-2; Sequence=VSP_017087;
CC -!- TISSUE SPECIFICITY: Expressed in tumor endothelial cells but absent or
CC barely detectable in normal endothelial cells. Expressed in metastatic
CC lesions of the liver and during angiogenesis of corpus luteum formation
CC and wound healing. Expressed in vascular endothelial cells of malignant
CC tumors but not in normal blood vessels. Expressed in stromal
CC fibroblasts. {ECO:0000269|PubMed:10947988, ECO:0000269|PubMed:11084048,
CC ECO:0000269|PubMed:1438285, ECO:0000269|PubMed:15862292,
CC ECO:0000269|PubMed:16076089}.
CC -!- PTM: O-glycosylated with sialylated oligosaccharides.
CC {ECO:0000269|PubMed:1438285}.
CC -!- PTM: May be N-glycosylated. {ECO:0000269|PubMed:1438285}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CD248ID968ch11q13.html";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Endosialin;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_210";
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DR EMBL; AF279142; AAG00867.1; -; mRNA.
DR EMBL; AJ295846; CAC34381.1; -; mRNA.
DR EMBL; AK027290; BAB55018.1; -; mRNA.
DR EMBL; BC051340; AAH51340.1; -; mRNA.
DR EMBL; BC104484; AAI04485.1; -; mRNA.
DR EMBL; BC105633; AAI05634.1; -; mRNA.
DR CCDS; CCDS8134.1; -. [Q9HCU0-1]
DR RefSeq; NP_065137.1; NM_020404.2. [Q9HCU0-1]
DR AlphaFoldDB; Q9HCU0; -.
DR SMR; Q9HCU0; -.
DR BioGRID; 121387; 3.
DR IntAct; Q9HCU0; 7.
DR MINT; Q9HCU0; -.
DR STRING; 9606.ENSP00000308117; -.
DR ChEMBL; CHEMBL3712975; -.
DR GlyGen; Q9HCU0; 34 sites, 4 O-linked glycans (16 sites).
DR iPTMnet; Q9HCU0; -.
DR PhosphoSitePlus; Q9HCU0; -.
DR BioMuta; CD248; -.
DR DMDM; 74752810; -.
DR jPOST; Q9HCU0; -.
DR MassIVE; Q9HCU0; -.
DR PaxDb; Q9HCU0; -.
DR PeptideAtlas; Q9HCU0; -.
DR PRIDE; Q9HCU0; -.
DR ProteomicsDB; 81798; -. [Q9HCU0-1]
DR ProteomicsDB; 81799; -. [Q9HCU0-2]
DR ABCD; Q9HCU0; 1 sequenced antibody.
DR Antibodypedia; 30126; 380 antibodies from 38 providers.
DR DNASU; 57124; -.
DR Ensembl; ENST00000311330.4; ENSP00000308117.3; ENSG00000174807.4. [Q9HCU0-1]
DR GeneID; 57124; -.
DR KEGG; hsa:57124; -.
DR MANE-Select; ENST00000311330.4; ENSP00000308117.3; NM_020404.3; NP_065137.1.
DR UCSC; uc001ohm.1; human. [Q9HCU0-1]
DR CTD; 57124; -.
DR DisGeNET; 57124; -.
DR GeneCards; CD248; -.
DR HGNC; HGNC:18219; CD248.
DR HPA; ENSG00000174807; Tissue enhanced (adipose tissue, breast).
DR MIM; 606064; gene.
DR neXtProt; NX_Q9HCU0; -.
DR OpenTargets; ENSG00000174807; -.
DR PharmGKB; PA134864533; -.
DR VEuPathDB; HostDB:ENSG00000174807; -.
DR eggNOG; ENOG502QQKI; Eukaryota.
DR GeneTree; ENSGT00940000162405; -.
DR HOGENOM; CLU_027075_0_0_1; -.
DR InParanoid; Q9HCU0; -.
DR OMA; NWAQPAT; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; Q9HCU0; -.
DR TreeFam; TF330714; -.
DR PathwayCommons; Q9HCU0; -.
DR SignaLink; Q9HCU0; -.
DR BioGRID-ORCS; 57124; 10 hits in 1062 CRISPR screens.
DR ChiTaRS; CD248; human.
DR GeneWiki; CD248; -.
DR GenomeRNAi; 57124; -.
DR Pharos; Q9HCU0; Tbio.
DR PRO; PR:Q9HCU0; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9HCU0; protein.
DR Bgee; ENSG00000174807; Expressed in decidua and 168 other tissues.
DR Genevisible; Q9HCU0; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; TAS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:1990430; F:extracellular matrix protein binding; IBA:GO_Central.
DR GO; GO:0060033; P:anatomical structure regression; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0072577; P:endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0010761; P:fibroblast migration; IEA:Ensembl.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0048535; P:lymph node development; IEA:Ensembl.
DR GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
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; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00179; EGF_CA; 2.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF57184; SSF57184; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01187; EGF_CA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Disulfide bond; EGF-like domain;
KW Glycoprotein; Lectin; Membrane; Phosphoprotein; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..757
FT /note="Endosialin"
FT /id="PRO_0000045799"
FT TOPO_DOM 18..687
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..757
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..156
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 162..232
FT /note="Sushi"
FT DOMAIN 312..351
FT /note="EGF-like; calcium-binding"
FT /evidence="ECO:0000255"
FT REGION 618..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 60
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 472
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 541
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 543
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 587
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 593
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 595
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 598
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 601
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 612
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 619
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 623
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 625
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 627
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 630
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 636
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT DISULFID 131..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 316..326
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 322..335
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 337..350
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 1..324
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_017087"
FT VARIANT 6
FT /note="L -> F (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036399"
FT VARIANT 457
FT /note="H -> R (in dbSNP:rs3741367)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025013"
FT CONFLICT 486
FT /note="A -> V (in Ref. 3; BAB55018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 757 AA; 80859 MW; C96363EA1FD8FFA0 CRC64;
MLLRLLLAWA AAGPTLGQDP WAAEPRAACG PSSCYALFPR RRTFLEAWRA CRELGGDLAT
PRTPEEAQRV DSLVGAGPAS RLLWIGLQRQ ARQCQLQRPL RGFTWTTGDQ DTAFTNWAQP
ASGGPCPAQR CVALEASGEH RWLEGSCTLA VDGYLCQFGF EGACPALQDE AGQAGPAVYT
TPFHLVSTEF EWLPFGSVAA VQCQAGRGAS LLCVKQPEGG VGWSRAGPLC LGTGCSPDNG
GCEHECVEEV DGHVSCRCTE GFRLAADGRS CEDPCAQAPC EQQCEPGGPQ GYSCHCRLGF
RPAEDDPHRC VDTDECQIAG VCQQMCVNYV GGFECYCSEG HELEADGISC SPAGAMGAQA
SQDLGDELLD DGEDEEDEDE AWKAFNGGWT EMPGILWMEP TQPPDFALAY RPSFPEDREP
QIPYPEPTWP PPLSAPRVPY HSSVLSVTRP VVVSATHPTL PSAHQPPVIP ATHPALSRDH
QIPVIAANYP DLPSAYQPGI LSVSHSAQPP AHQPPMISTK YPELFPAHQS PMFPDTRVAG
TQTTTHLPGI PPNHAPLVTT LGAQLPPQAP DALVLRTQAT QLPIIPTAQP SLTTTSRSPV
SPAHQISVPA ATQPAALPTL LPSQSPTNQT SPISPTHPHS KAPQIPREDG PSPKLALWLP
SPAPTAAPTA LGEAGLAEHS QRDDRWLLVA LLVPTCVFLV VLLALGIVYC TRCGPHAPNK
RITDCYRWVI HAGSKSPTEP MPPRGSLTGV QTCRTSV
