CD5L_MOUSE
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 03-AUG-2022, entry version 155.
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 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 PRIDE; Q9QWK4; -.
DR ProteomicsDB; 281138; -.
DR Antibodypedia; 20452; 511 antibodies from 37 providers.
DR DNASU; 11801; -.
DR Ensembl; ENSMUST00000015998; ENSMUSP00000015998; ENSMUSG00000015854.
DR GeneID; 11801; -.
DR KEGG; mmu:11801; -.
DR UCSC; uc008psa.2; mouse.
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; 158600at2759; -.
DR PhylomeDB; Q9QWK4; -.
DR TreeFam; TF329295; -.
DR BioGRID-ORCS; 11801; 1 hit in 71 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; -; 3.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR Pfam; PF00530; SRCR; 3.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00202; SR; 3.
DR SUPFAM; SSF56487; SSF56487; 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
