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CD5 antigen-like (Apoptosis inhibitor expressed by macrophages) (mAIM) (Apoptosis inhibitory 6) (SP-alpha)

 CD5L_MOUSE              Reviewed;         352 AA.
Q9QWK4; O35300; O35301; Q3TXN5; Q505P6; Q91W05;
16-APR-2002, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
28-FEB-2018, entry version 133.
RecName: Full=CD5 antigen-like;
AltName: Full=Apoptosis inhibitor expressed by macrophages {ECO:0000303|PubMed:9892623};
Short=mAIM {ECO:0000303|PubMed:23236605};
AltName: Full=Apoptosis inhibitory 6;
AltName: Full=SP-alpha {ECO:0000303|PubMed:10651944};
Flags: Precursor;
Name=Cd5l; Synonyms=Aim {ECO:0000303|PubMed:9892623}, Api6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MET-61; SER-197 AND ARG-205,
TISSUE SPECIFICITY, AND GLYCOSYLATION.
STRAIN=BALB/cJ; TISSUE=Thymus;
PubMed=10651944; DOI=10.1046/j.1365-2567.2000.00903.x;
Gebe J.A., Llewellyn M.-B.C., Hoggatt H., Aruffo A.;
"Molecular cloning, genomic organization and cell-binding
characteristics of mouse Spalpha.";
Immunology 99:78-86(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION IN APOPTOSIS.
PubMed=9892623; DOI=10.1084/jem.189.2.413;
Miyazaki T., Hirokami Y., Matsuhashi N., Takatsuka H., Naito M.;
"Increased susceptibility of thymocytes to apoptosis in mice lacking
AIM, a novel murine macrophage-derived soluble factor belonging to the
scavenger receptor cysteine-rich domain superfamily.";
J. Exp. Med. 189:413-422(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-197.
STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION.
PubMed=16054063; DOI=10.1016/j.cmet.2005.02.002;
Arai S., Shelton J.M., Chen M., Bradley M.N., Castrillo A.,
Bookout A.L., Mak P.A., Edwards P.A., Mangelsdorf D.J., Tontonoz P.,
Miyazaki T.;
"A role for the apoptosis inhibitory factor AIM/Spalpha/Api6 in
atherosclerosis development.";
Cell Metab. 1:201-213(2005).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FASN.
PubMed=20519120; DOI=10.1016/j.cmet.2010.04.013;
Kurokawa J., Arai S., Nakashima K., Nagano H., Nishijima A.,
Miyata K., Ose R., Mori M., Kubota N., Kadowaki T., Oike Y., Koga H.,
Febbraio M., Iwanaga T., Miyazaki T.;
"Macrophage-derived AIM is endocytosed into adipocytes and decreases
lipid droplets via inhibition of fatty acid synthase activity.";
Cell Metab. 11:479-492(2010).
[7]
FUNCTION.
PubMed=21730133; DOI=10.1073/pnas.1101841108;
Kurokawa J., Nagano H., Ohara O., Kubota N., Kadowaki T., Arai S.,
Miyazaki T.;
"Apoptosis inhibitor of macrophage (AIM) is required for obesity-
associated recruitment of inflammatory macrophages into adipose
tissue.";
Proc. Natl. Acad. Sci. U.S.A. 108:12072-12077(2011).
[8]
FUNCTION.
PubMed=22579686; DOI=10.1016/j.bbrc.2012.05.018;
Iwamura Y., Mori M., Nakashima K., Mikami T., Murayama K., Arai S.,
Miyazaki T.;
"Apoptosis inhibitor of macrophage (AIM) diminishes lipid droplet-
coating proteins leading to lipolysis in adipocytes.";
Biochem. Biophys. Res. Commun. 422:476-481(2012).
[9]
SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-99 AND ASN-229, LACK OF
GLYCOSYLATION AT ASN-316, AND MUTAGENESIS OF ASN-99; ASN-229 AND
ASN-316.
PubMed=23236605; DOI=10.1016/j.febslet.2012.08.017;
Mori M., Kimura H., Iwamura Y., Arai S., Miyazaki T.;
"Modification of N-glycosylation modulates the secretion and lipolytic
function of apoptosis inhibitor of macrophage (AIM).";
FEBS Lett. 586:3569-3574(2012).
[10]
FUNCTION.
PubMed=23562157; DOI=10.1016/j.celrep.2013.03.006;
Arai S., Maehara N., Iwamura Y., Honda S., Nakashima K., Kai T.,
Ogishi M., Morita K., Kurokawa J., Mori M., Motoi Y., Miyake K.,
Matsuhashi N., Yamamura K., Ohara O., Shibuya A., Wakeland E.K.,
Li Q.Z., Miyazaki T.;
"Obesity-associated autoantibody production requires AIM to retain the
immunoglobulin M immune complex on follicular dendritic cells.";
Cell Rep. 3:1187-1198(2013).
[11]
FUNCTION.
PubMed=26607794; DOI=10.1016/j.cell.2015.11.009;
Gaublomme J.T., Yosef N., Lee Y., Gertner R.S., Yang L.V., Wu C.,
Pandolfi P.P., Mak T., Satija R., Shalek A.K., Kuchroo V.K., Park H.,
Regev A.;
"Single-cell genomics unveils critical regulators of Th17 cell
pathogenicity.";
Cell 163:1400-1412(2015).
[12]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=26607793; DOI=10.1016/j.cell.2015.10.068;
Wang C., Yosef N., Gaublomme J., Wu C., Lee Y., Clish C.B.,
Kaminski J., Xiao S., Meyer Zu Horste G., Pawlak M., Kishi Y.,
Joller N., Karwacz K., Zhu C., Ordovas-Montanes M., Madi A.,
Wortman I., Miyazaki T., Sobel R.A., Park H., Regev A., Kuchroo V.K.;
"CD5L/AIM regulates lipid biosynthesis and restrains Th17 cell
pathogenicity.";
Cell 163:1413-1427(2015).
[13]
REVIEW.
PubMed=26048980; DOI=10.1189/jlb.3RU0215-074R;
Sanjurjo L., Aran G., Roher N., Valledor A.F., Sarrias M.R.;
"AIM/CD5L: a key protein in the control of immune homeostasis and
inflammatory disease.";
J. Leukoc. Biol. 98:173-184(2015).
-!- FUNCTION: Secreted protein that acts as a key regulator of lipid
synthesis: mainly expressed by macrophages in lymphoid and
inflammed tissues and regulates mechanisms in inflammatory
responses, such as infection or atherosclerosis (PubMed:26048980).
Able to inhibit lipid droplet size in adipocytes (PubMed:20519120,
PubMed:22579686). Following incorporation into mature adipocytes
via CD36-mediated endocytosis, associates with cytosolic FASN,
inhibiting fatty acid synthase activity and leading to lipolysis,
the degradation of triacylglycerols into glycerol and free fatty
acids (FFA) (PubMed:20519120). CD5L-induced lipolysis occurs with
progression of obesity: participates in obesity-associated
inflammation following recruitment of inflammatory macrophages
into adipose tissues, a cause of insulin resistance and obesity-
related metabolic disease (PubMed:21730133). Regulation of
intracellular lipids mediated by CD5L has a direct effect on
transcription regulation mediated by nuclear receptors ROR-gamma
(RORC) (PubMed:22579686, PubMed:26607793). Acts as a key regulator
of metabolic switch in T-helper Th17 cells (PubMed:26607794,
PubMed:26607793). Regulates the expression of pro-inflammatory
genes in Th17 cells by altering the lipid content and limiting
synthesis of cholesterol ligand of RORC, the master transcription
factor of Th17-cell differentiation (PubMed:26607793). CD5L is
mainly present in non-pathogenic Th17 cells, where it decreases
the content of polyunsaturated fatty acyls (PUFA), affecting two
metabolic proteins MSMO1 and CYP51A1, which synthesize ligands of
RORC, limiting RORC activity and expression of pro-inflammatory
genes (PubMed:26607793). Participates in obesity-associated
autoimmunity via its association with IgM, interfering with the
binding of IgM to Fcalpha/mu receptor and enhancing the
development of long-lived plasma cells that produce high-affinity
IgG autoantibodies (PubMed:23562157). Also acts as an inhibitor of
apoptosis in macrophages: promotes macrophage survival from the
apoptotic effects of oxidized lipids in case of atherosclerosis
(PubMed:9892623, PubMed:16054063). Involved in early response to
microbial infection against various pathogens by acting as a
pattern recognition receptor and by promoting autophagy (By
similarity). {ECO:0000250|UniProtKB:O43866,
ECO:0000269|PubMed:16054063, ECO:0000269|PubMed:20519120,
ECO:0000269|PubMed:21730133, ECO:0000269|PubMed:22579686,
ECO:0000269|PubMed:23562157, ECO:0000269|PubMed:26607793,
ECO:0000269|PubMed:26607794, ECO:0000269|PubMed:9892623,
ECO:0000303|PubMed:26048980}.
-!- SUBUNIT: Interacts with FASN; the interaction is direct
(PubMed:20519120). Interacts with IgM; protecting CD5L from renal
excretion and leading to increased CD5L levels in circulating
blood (PubMed:23562157). {ECO:0000269|PubMed:20519120,
ECO:0000269|PubMed:23562157}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20519120,
ECO:0000269|PubMed:23236605, ECO:0000269|PubMed:9892623}.
Cytoplasm {ECO:0000269|PubMed:20519120}. Note=Secreted by
macrophages and circulates in the blood (PubMed:20519120).
Transported in the cytoplasm via CD36-mediated endocytosis
(PubMed:20519120). {ECO:0000269|PubMed:20519120}.
-!- TISSUE SPECIFICITY: Specificaly expressed in tissue macrophages
(PubMed:9892623). Expressed in thymus, liver, spleen and lymph
nodes (PubMed:10651944). Present in Th17 cells; mainly present in
non-pathogenic Th17 cells (PubMed:26607793).
{ECO:0000269|PubMed:10651944, ECO:0000269|PubMed:26607793,
ECO:0000269|PubMed:9892623}.
-!- INDUCTION: Transcription is activated by nuclear receptor liver X
/retinoid X (RXR/LXR).
-!- PTM: N-glycosylated (PubMed:10651944, PubMed:23236605). N-glycan
at Asn-99 possesses only alpha2,6-sialylated terminals, while Asn-
229 possesses both alpha2,6-sialylated and non-sialylated
terminals (PubMed:23236605). N-glycosylation increases secretion.
{ECO:0000269|PubMed:10651944, ECO:0000269|PubMed:23236605}.
-!- DISRUPTION PHENOTYPE: Mice are apparently healthy under specific
pathogen-free conditions. However, thymus of mice display much
fewer thymocytes and CD4/CD8 double-positive (DP) thymocytes are
more susceptible to apoptosis (PubMed:9892623). Increased
adipocyte size and adipose tissue mass (PubMed:20519120). Higher
level of free cholesterol in Th17 cells (PubMed:26607793).
{ECO:0000269|PubMed:20519120, ECO:0000269|PubMed:26607793,
ECO:0000269|PubMed:9892623}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF018268; AAB70571.1; -; mRNA.
EMBL; AF018269; AAB70572.1; -; mRNA.
EMBL; AF011428; AAD01445.1; -; mRNA.
EMBL; AK159132; BAE34844.1; -; mRNA.
EMBL; AK159181; BAE34880.1; -; mRNA.
EMBL; AK159823; BAE35403.1; -; mRNA.
EMBL; BC006799; AAH06799.1; -; mRNA.
EMBL; BC094459; AAH94459.1; -; mRNA.
CCDS; CCDS17451.1; -.
RefSeq; NP_033820.2; NM_009690.2.
UniGene; Mm.6676; -.
ProteinModelPortal; Q9QWK4; -.
SMR; Q9QWK4; -.
BioGrid; 198152; 1.
IntAct; Q9QWK4; 1.
MINT; Q9QWK4; -.
STRING; 10090.ENSMUSP00000015998; -.
iPTMnet; Q9QWK4; -.
PhosphoSitePlus; Q9QWK4; -.
MaxQB; Q9QWK4; -.
PaxDb; Q9QWK4; -.
PeptideAtlas; Q9QWK4; -.
PRIDE; Q9QWK4; -.
Ensembl; ENSMUST00000015998; ENSMUSP00000015998; ENSMUSG00000015854.
GeneID; 11801; -.
KEGG; mmu:11801; -.
UCSC; uc008psa.2; mouse.
CTD; 922; -.
MGI; MGI:1334419; Cd5l.
eggNOG; ENOG410IKHN; Eukaryota.
eggNOG; ENOG4110209; LUCA.
GeneTree; ENSGT00900000140803; -.
HOGENOM; HOG000290652; -.
HOVERGEN; HBG031373; -.
InParanoid; Q9QWK4; -.
OMA; YHGEDAS; -.
OrthoDB; EOG091G0DF7; -.
TreeFam; TF329295; -.
PRO; PR:Q9QWK4; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000015854; -.
CleanEx; MM_CD5L; -.
Genevisible; Q9QWK4; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
Gene3D; 3.10.250.10; -; 3.
InterPro; IPR001190; SRCR.
InterPro; IPR017448; SRCR-like_dom.
InterPro; IPR036772; SRCR-like_dom_sf.
Pfam; PF00530; SRCR; 3.
PRINTS; PR00258; SPERACTRCPTR.
SMART; SM00202; SR; 3.
SUPFAM; SSF56487; SSF56487; 3.
PROSITE; PS00420; SRCR_1; 1.
PROSITE; PS50287; SRCR_2; 3.
1: Evidence at protein level;
Apoptosis; Complete proteome; Cytoplasm; Disulfide bond; Glycoprotein;
Immunity; Inflammatory response; Polymorphism; Reference proteome;
Repeat; Secreted; Signal.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 352 CD5 antigen-like.
/FTId=PRO_0000033226.
DOMAIN 27 128 SRCR 1. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 141 241 SRCR 2. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
DOMAIN 246 348 SRCR 3. {ECO:0000255|PROSITE-
ProRule:PRU00196}.
SITE 316 316 Not glycosylated.
{ECO:0000269|PubMed:23236605}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23236605}.
CARBOHYD 229 229 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:23236605}.
DISULFID 36 70 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 52 117 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 65 127 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 98 108 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 166 230 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 179 240 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 211 221 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 255 289 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 271 337 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 284 347 {ECO:0000255|PROSITE-ProRule:PRU00196}.
DISULFID 317 327 {ECO:0000255|PROSITE-ProRule:PRU00196}.
VARIANT 61 61 V -> M. {ECO:0000269|PubMed:10651944}.
VARIANT 197 197 N -> S. {ECO:0000269|PubMed:10651944,
ECO:0000269|PubMed:15489334}.
VARIANT 205 205 W -> R. {ECO:0000269|PubMed:10651944}.
MUTAGEN 99 99 N->Q: Decreased glycosylation.
{ECO:0000269|PubMed:23236605}.
MUTAGEN 229 229 N->Q: Decreased glycosylation.
{ECO:0000269|PubMed:23236605}.
MUTAGEN 316 316 N->Q: Does not affect glycosylation.
{ECO:0000269|PubMed:23236605}.
CONFLICT 13 13 S -> N (in Ref. 1; AAB70571).
{ECO:0000305}.
CONFLICT 113 113 D -> Y (in Ref. 2; AAD01445).
{ECO:0000305}.
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


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