ID CD5L_MOUSE Reviewed; 352 AA. AC Q9QWK4; O35300; O35301; Q3TXN5; Q505P6; Q91W05; DT 16-APR-2002, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 22-FEB-2023, entry version 158. DE RecName: Full=CD5 antigen-like; DE AltName: Full=Apoptosis inhibitor expressed by macrophages {ECO:0000303|PubMed:9892623}; DE Short=mAIM {ECO:0000303|PubMed:23236605}; DE AltName: Full=Apoptosis inhibitory 6; DE AltName: Full=SP-alpha {ECO:0000303|PubMed:10651944}; DE Flags: Precursor; GN Name=Cd5l; Synonyms=Aim {ECO:0000303|PubMed:9892623}, Api6; 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], VARIANTS MET-61; SER-197 AND ARG-205, TISSUE RP SPECIFICITY, AND GLYCOSYLATION. RC STRAIN=BALB/cJ; TISSUE=Thymus; RX PubMed=10651944; DOI=10.1046/j.1365-2567.2000.00903.x; RA Gebe J.A., Llewellyn M.-B.C., Hoggatt H., Aruffo A.; RT "Molecular cloning, genomic organization and cell-binding characteristics RT of mouse Spalpha."; RL Immunology 99:78-86(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION IN APOPTOSIS. RX PubMed=9892623; DOI=10.1084/jem.189.2.413; RA Miyazaki T., Hirokami Y., Matsuhashi N., Takatsuka H., Naito M.; RT "Increased susceptibility of thymocytes to apoptosis in mice lacking AIM, a RT novel murine macrophage-derived soluble factor belonging to the scavenger RT receptor cysteine-rich domain superfamily."; RL J. Exp. Med. 189:413-422(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; 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], AND VARIANT SER-197. RC STRAIN=FVB/N; TISSUE=Liver, and 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 FUNCTION. RX PubMed=16054063; DOI=10.1016/j.cmet.2005.02.002; RA Arai S., Shelton J.M., Chen M., Bradley M.N., Castrillo A., Bookout A.L., RA Mak P.A., Edwards P.A., Mangelsdorf D.J., Tontonoz P., Miyazaki T.; RT "A role for the apoptosis inhibitory factor AIM/Spalpha/Api6 in RT atherosclerosis development."; RL Cell Metab. 1:201-213(2005). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FASN. RX PubMed=20519120; DOI=10.1016/j.cmet.2010.04.013; RA Kurokawa J., Arai S., Nakashima K., Nagano H., Nishijima A., Miyata K., RA Ose R., Mori M., Kubota N., Kadowaki T., Oike Y., Koga H., Febbraio M., RA Iwanaga T., Miyazaki T.; RT "Macrophage-derived AIM is endocytosed into adipocytes and decreases lipid RT droplets via inhibition of fatty acid synthase activity."; RL Cell Metab. 11:479-492(2010). RN [7] RP FUNCTION. RX PubMed=21730133; DOI=10.1073/pnas.1101841108; RA Kurokawa J., Nagano H., Ohara O., Kubota N., Kadowaki T., Arai S., RA Miyazaki T.; RT "Apoptosis inhibitor of macrophage (AIM) is required for obesity-associated RT recruitment of inflammatory macrophages into adipose tissue."; RL Proc. Natl. Acad. Sci. U.S.A. 108:12072-12077(2011). RN [8] RP FUNCTION. RX PubMed=22579686; DOI=10.1016/j.bbrc.2012.05.018; RA Iwamura Y., Mori M., Nakashima K., Mikami T., Murayama K., Arai S., RA Miyazaki T.; RT "Apoptosis inhibitor of macrophage (AIM) diminishes lipid droplet-coating RT proteins leading to lipolysis in adipocytes."; RL Biochem. Biophys. Res. Commun. 422:476-481(2012). RN [9] RP SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-99 AND ASN-229, LACK OF RP GLYCOSYLATION AT ASN-316, AND MUTAGENESIS OF ASN-99; ASN-229 AND ASN-316. RX PubMed=23236605; DOI=10.1016/j.febslet.2012.08.017; RA Mori M., Kimura H., Iwamura Y., Arai S., Miyazaki T.; RT "Modification of N-glycosylation modulates the secretion and lipolytic RT function of apoptosis inhibitor of macrophage (AIM)."; RL FEBS Lett. 586:3569-3574(2012). RN [10] RP FUNCTION. RX PubMed=23562157; DOI=10.1016/j.celrep.2013.03.006; RA Arai S., Maehara N., Iwamura Y., Honda S., Nakashima K., Kai T., Ogishi M., RA Morita K., Kurokawa J., Mori M., Motoi Y., Miyake K., Matsuhashi N., RA Yamamura K., Ohara O., Shibuya A., Wakeland E.K., Li Q.Z., Miyazaki T.; RT "Obesity-associated autoantibody production requires AIM to retain the RT immunoglobulin M immune complex on follicular dendritic cells."; RL Cell Rep. 3:1187-1198(2013). RN [11] RP FUNCTION. RX PubMed=26607794; DOI=10.1016/j.cell.2015.11.009; RA Gaublomme J.T., Yosef N., Lee Y., Gertner R.S., Yang L.V., Wu C., RA Pandolfi P.P., Mak T., Satija R., Shalek A.K., Kuchroo V.K., Park H., RA Regev A.; RT "Single-cell genomics unveils critical regulators of Th17 cell RT pathogenicity."; RL Cell 163:1400-1412(2015). RN [12] RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE. RX PubMed=26607793; DOI=10.1016/j.cell.2015.10.068; RA Wang C., Yosef N., Gaublomme J., Wu C., Lee Y., Clish C.B., Kaminski J., RA Xiao S., Meyer Zu Horste G., Pawlak M., Kishi Y., Joller N., Karwacz K., RA Zhu C., Ordovas-Montanes M., Madi A., Wortman I., Miyazaki T., Sobel R.A., RA Park H., Regev A., Kuchroo V.K.; RT "CD5L/AIM regulates lipid biosynthesis and restrains Th17 cell RT pathogenicity."; RL Cell 163:1413-1427(2015). RN [13] RP REVIEW. RX PubMed=26048980; DOI=10.1189/jlb.3ru0215-074r; RA Sanjurjo L., Aran G., Roher N., Valledor A.F., Sarrias M.R.; RT "AIM/CD5L: a key protein in the control of immune homeostasis and RT inflammatory disease."; RL J. Leukoc. Biol. 98:173-184(2015). CC -!- FUNCTION: Secreted protein that acts as a key regulator of lipid CC synthesis: mainly expressed by macrophages in lymphoid and inflamed CC tissues and regulates mechanisms in inflammatory responses, such as CC infection or atherosclerosis (PubMed:26048980). Able to inhibit lipid CC droplet size in adipocytes (PubMed:20519120, PubMed:22579686). CC Following incorporation into mature adipocytes via CD36-mediated CC endocytosis, associates with cytosolic FASN, inhibiting fatty acid CC synthase activity and leading to lipolysis, the degradation of CC triacylglycerols into glycerol and free fatty acids (FFA) CC (PubMed:20519120). CD5L-induced lipolysis occurs with progression of CC obesity: participates in obesity-associated inflammation following CC recruitment of inflammatory macrophages into adipose tissues, a cause CC of insulin resistance and obesity-related metabolic disease CC (PubMed:21730133). Regulation of intracellular lipids mediated by CD5L CC has a direct effect on transcription regulation mediated by nuclear CC receptors ROR-gamma (RORC) (PubMed:22579686, PubMed:26607793). Acts as CC a key regulator of metabolic switch in T-helper Th17 cells CC (PubMed:26607794, PubMed:26607793). Regulates the expression of pro- CC inflammatory genes in Th17 cells by altering the lipid content and CC limiting synthesis of cholesterol ligand of RORC, the master CC transcription factor of Th17-cell differentiation (PubMed:26607793). CC CD5L is mainly present in non-pathogenic Th17 cells, where it decreases CC the content of polyunsaturated fatty acyls (PUFA), affecting two CC metabolic proteins MSMO1 and CYP51A1, which synthesize ligands of RORC, CC limiting RORC activity and expression of pro-inflammatory genes CC (PubMed:26607793). Participates in obesity-associated autoimmunity via CC its association with IgM, interfering with the binding of IgM to CC Fcalpha/mu receptor and enhancing the development of long-lived plasma CC cells that produce high-affinity IgG autoantibodies (PubMed:23562157). CC Also acts as an inhibitor of apoptosis in macrophages: promotes CC macrophage survival from the apoptotic effects of oxidized lipids in CC case of atherosclerosis (PubMed:9892623, PubMed:16054063). Involved in CC early response to microbial infection against various pathogens by CC acting as a pattern recognition receptor and by promoting autophagy (By CC similarity). {ECO:0000250|UniProtKB:O43866, CC ECO:0000269|PubMed:16054063, ECO:0000269|PubMed:20519120, CC ECO:0000269|PubMed:21730133, ECO:0000269|PubMed:22579686, CC ECO:0000269|PubMed:23562157, ECO:0000269|PubMed:26607793, CC ECO:0000269|PubMed:26607794, ECO:0000269|PubMed:9892623, CC ECO:0000303|PubMed:26048980}. CC -!- SUBUNIT: Interacts with FASN; the interaction is direct CC (PubMed:20519120). Interacts with IgM; protecting CD5L from renal CC excretion and leading to increased CD5L levels in circulating blood CC (PubMed:23562157). {ECO:0000269|PubMed:20519120, CC ECO:0000269|PubMed:23562157}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20519120, CC ECO:0000269|PubMed:23236605, ECO:0000269|PubMed:9892623}. Cytoplasm CC {ECO:0000269|PubMed:20519120}. Note=Secreted by macrophages and CC circulates in the blood (PubMed:20519120). Transported in the cytoplasm CC via CD36-mediated endocytosis (PubMed:20519120). CC {ECO:0000269|PubMed:20519120}. CC -!- TISSUE SPECIFICITY: Specifically expressed in tissue macrophages CC (PubMed:9892623). Expressed in thymus, liver, spleen and lymph nodes CC (PubMed:10651944). Present in Th17 cells; mainly present in non- CC pathogenic Th17 cells (PubMed:26607793). {ECO:0000269|PubMed:10651944, CC ECO:0000269|PubMed:26607793, ECO:0000269|PubMed:9892623}. CC -!- INDUCTION: Transcription is activated by nuclear receptor liver X CC /retinoid X (RXR/LXR). CC -!- PTM: N-glycosylated (PubMed:10651944, PubMed:23236605). N-glycan at CC Asn-99 possesses only alpha2,6-sialylated terminals, while Asn-229 CC possesses both alpha2,6-sialylated and non-sialylated terminals CC (PubMed:23236605). N-glycosylation increases secretion. CC {ECO:0000269|PubMed:10651944, ECO:0000269|PubMed:23236605}. CC -!- DISRUPTION PHENOTYPE: Mice are apparently healthy under specific CC pathogen-free conditions. However, thymus of mice display much fewer CC thymocytes and CD4/CD8 double-positive (DP) thymocytes are more CC susceptible to apoptosis (PubMed:9892623). Increased adipocyte size and CC adipose tissue mass (PubMed:20519120). Higher level of free cholesterol CC in Th17 cells (PubMed:26607793). {ECO:0000269|PubMed:20519120, CC ECO:0000269|PubMed:26607793, ECO:0000269|PubMed:9892623}. 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; AF018268; AAB70571.1; -; mRNA. DR EMBL; AF018269; AAB70572.1; -; mRNA. DR EMBL; AF011428; AAD01445.1; -; mRNA. DR EMBL; AK159132; BAE34844.1; -; mRNA. DR EMBL; AK159181; BAE34880.1; -; mRNA. DR EMBL; AK159823; BAE35403.1; -; mRNA. DR EMBL; BC006799; AAH06799.1; -; mRNA. DR EMBL; BC094459; AAH94459.1; -; mRNA. DR CCDS; CCDS17451.1; -. DR RefSeq; NP_033820.2; NM_009690.2. DR AlphaFoldDB; Q9QWK4; -. DR SMR; Q9QWK4; -. DR BioGRID; 198152; 1. DR IntAct; Q9QWK4; 1. DR MINT; Q9QWK4; -. DR STRING; 10090.ENSMUSP00000015998; -. DR GlyCosmos; Q9QWK4; 2 sites, No reported glycans. DR GlyGen; Q9QWK4; 2 sites. DR iPTMnet; Q9QWK4; -. DR PhosphoSitePlus; Q9QWK4; -. DR CPTAC; non-CPTAC-5585; -. DR CPTAC; non-CPTAC-5586; -. DR MaxQB; Q9QWK4; -. DR PaxDb; Q9QWK4; -. DR PeptideAtlas; Q9QWK4; -. DR ProteomicsDB; 281138; -. DR Antibodypedia; 20452; 514 antibodies from 37 providers. DR DNASU; 11801; -. DR Ensembl; ENSMUST00000015998.8; ENSMUSP00000015998.7; ENSMUSG00000015854.8. DR GeneID; 11801; -. DR KEGG; mmu:11801; -. DR UCSC; uc008psa.2; mouse. DR AGR; MGI:1334419; -. DR CTD; 922; -. DR MGI; MGI:1334419; Cd5l. DR VEuPathDB; HostDB:ENSMUSG00000015854; -. DR eggNOG; ENOG502SHID; Eukaryota. DR GeneTree; ENSGT00940000161974; -. DR HOGENOM; CLU_002555_11_0_1; -. DR InParanoid; Q9QWK4; -. DR OMA; LHKGVWG; -. DR OrthoDB; 5292724at2759; -. DR PhylomeDB; Q9QWK4; -. DR TreeFam; TF329295; -. DR BioGRID-ORCS; 11801; 1 hit in 76 CRISPR screens. DR PRO; PR:Q9QWK4; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; Q9QWK4; protein. DR Bgee; ENSMUSG00000015854; Expressed in stroma of bone marrow and 52 other tissues. DR Genevisible; Q9QWK4; MM. DR GO; GO:0009986; C:cell surface; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro. DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:1903661; P:positive regulation of complement-dependent cytotoxicity; IMP:MGI. DR GO; GO:0030449; P:regulation of complement activation; IMP:MGI. DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central. DR Gene3D; 3.10.250.10; SRCR-like domain; 3. DR InterPro; IPR001190; SRCR. DR InterPro; IPR017448; SRCR-like_dom. DR InterPro; IPR036772; SRCR-like_dom_sf. DR PANTHER; PTHR48071:SF8; CD5 ANTIGEN-LIKE; 1. DR PANTHER; PTHR48071; SRCR DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00530; SRCR; 3. DR PRINTS; PR00258; SPERACTRCPTR. DR SMART; SM00202; SR; 3. DR SUPFAM; SSF56487; SRCR-like; 3. DR PROSITE; PS00420; SRCR_1; 1. DR PROSITE; PS50287; SRCR_2; 3. PE 1: Evidence at protein level; KW Apoptosis; Cytoplasm; Disulfide bond; Glycoprotein; Immunity; KW Inflammatory response; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000255" FT CHAIN 22..352 FT /note="CD5 antigen-like" FT /id="PRO_0000033226" FT DOMAIN 27..128 FT /note="SRCR 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196" FT DOMAIN 141..241 FT /note="SRCR 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196" FT DOMAIN 246..348 FT /note="SRCR 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196" FT SITE 316 FT /note="Not glycosylated" FT /evidence="ECO:0000269|PubMed:23236605" FT CARBOHYD 99 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:23236605" FT CARBOHYD 229 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:23236605" FT DISULFID 36..70 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196" FT DISULFID 52..117 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196" FT DISULFID 65..127 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196" FT DISULFID 98..108 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196" FT DISULFID 166..230 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196" FT DISULFID 179..240 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196" FT DISULFID 211..221 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196" FT DISULFID 255..289 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196" FT DISULFID 271..337 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196" FT DISULFID 284..347 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196" FT DISULFID 317..327 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00196" FT VARIANT 61 FT /note="V -> M" FT /evidence="ECO:0000269|PubMed:10651944" FT VARIANT 197 FT /note="N -> S" FT /evidence="ECO:0000269|PubMed:10651944, FT ECO:0000269|PubMed:15489334" FT VARIANT 205 FT /note="W -> R" FT /evidence="ECO:0000269|PubMed:10651944" FT MUTAGEN 99 FT /note="N->Q: Decreased glycosylation." FT /evidence="ECO:0000269|PubMed:23236605" FT MUTAGEN 229 FT /note="N->Q: Decreased glycosylation." FT /evidence="ECO:0000269|PubMed:23236605" FT MUTAGEN 316 FT /note="N->Q: Does not affect glycosylation." FT /evidence="ECO:0000269|PubMed:23236605" FT CONFLICT 13 FT /note="S -> N (in Ref. 1; AAB70571)" FT /evidence="ECO:0000305" FT CONFLICT 113 FT /note="D -> Y (in Ref. 2; AAD01445)" FT /evidence="ECO:0000305" SQ SEQUENCE 352 AA; 38863 MW; 41596AA8012E1AEE CRC64; MAPLFNLMLA ILSIFVGSCF SESPTKVQLV GGAHRCEGRV EVEHNGQWGT VCDDGWDRRD VAVVCRELNC GAVIQTPRGA SYQPPASEQR VLIQGVDCNG TEDTLAQCEL NYDVFDCSHE EDAGAQCENP DSDLLFIPED VRLVDGPGHC QGRVEVLHQS QWSTVCKAGW NLQVSKVVCR QLGCGRALLT YGSCNKNTQG KGPIWMGKMS CSGQEANLRS CLLSRLENNC THGEDTWMEC EDPFELKLVG GDTPCSGRLE VLHKGSWGSV CDDNWGEKED QVVCKQLGCG KSLHPSPKTR KIYGPGAGRI WLDDVNCSGK EQSLEFCRHR LWGYHDCTHK EDVEVICTDF DV //