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   24-JAN-2024, entry version 172.
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="https://atlasgeneticsoncology.org/gene/968/CD248";
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   GlyCosmos; Q9HCU0; 34 sites, 4 glycans.
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; 9606-ENSP00000308117; -.
DR   PeptideAtlas; Q9HCU0; -.
DR   ProteomicsDB; 81798; -. [Q9HCU0-1]
DR   ProteomicsDB; 81799; -. [Q9HCU0-2]
DR   ABCD; Q9HCU0; 2 sequenced antibodies.
DR   Antibodypedia; 30126; 432 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   AGR; HGNC:18219; -.
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; APNKRIT; -.
DR   OrthoDB; 19806at2759; -.
DR   PhylomeDB; Q9HCU0; -.
DR   TreeFam; TF330714; -.
DR   PathwayCommons; Q9HCU0; -.
DR   SignaLink; Q9HCU0; -.
DR   BioGRID-ORCS; 57124; 10 hits in 1138 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 170 other cell types or tissues.
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: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   CDD; cd03600; CLECT_thrombomodulin_like; 1.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd19941; TIL; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
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; 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   PANTHER; PTHR14789; CHONDROLECTIN VARIANT CHODLFDELTAE; 1.
DR   PANTHER; PTHR14789:SF4; ENDOSIALIN; 1.
DR   Pfam; PF14670; FXa_inhibition; 1.
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; C-type lectin-like; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   Genevisible; Q9HCU0; HS.
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
//