GenomeNet

Database: UniProt
Entry: A2AJX4
LinkDB: A2AJX4
Original site: A2AJX4 
ID   MALR1_MOUSE             Reviewed;        2123 AA.
AC   A2AJX4; R9W764;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   04-FEB-2015, sequence version 2.
DT   10-APR-2019, entry version 90.
DE   RecName: Full=MAM and LDL-receptor class A domain-containing protein 1 {ECO:0000312|MGI:MGI:1928271};
DE   Flags: Precursor;
GN   Name=Malrd1 {ECO:0000312|MGI:MGI:1928271};
GN   Synonyms=Diet1 {ECO:0000303|PubMed:23747249},
GN   Gm13318 {ECO:0000312|MGI:MGI:1928271};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000312|Proteomes:UP000000589};
RN   [1] {ECO:0000312|EMBL:AGN95783.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH FGF15,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AGN95783.1};
RC   TISSUE=Small intestine {ECO:0000312|EMBL:AGN95783.1};
RX   PubMed=23747249; DOI=10.1016/j.cmet.2013.04.007;
RA   Vergnes L., Lee J.M., Chin R.G., Auwerx J., Reue K.;
RT   "Diet1 functions in the FGF15/19 enterohepatic signaling axis to
RT   modulate bile acid and lipid levels.";
RL   Cell Metab. 17:916-928(2013).
RN   [2] {ECO:0000312|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0000305}
RP   DISRUPTION PHENOTYPE.
RX   PubMed=10744778;
RA   Mouzeyan A., Choi J., Allayee H., Wang X., Sinsheimer J., Phan J.,
RA   Castellani L.W., Reue K., Lusis A.J., Davis R.C.;
RT   "A locus conferring resistance to diet-induced hypercholesterolemia
RT   and atherosclerosis on mouse chromosome 2.";
RL   J. Lipid Res. 41:573-582(2000).
CC   -!- FUNCTION: Enhances production and/or transport of FGF15 and thus
CC       has a role in regulation of bile acid synthesis.
CC       {ECO:0000269|PubMed:23747249}.
CC   -!- SUBUNIT: Interacts with FGF15. {ECO:0000269|PubMed:23747249}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC       {ECO:0000269|PubMed:23747249}; Single-pass type I membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Strongly expressed in epithelial cells of the
CC       small intestine. Also detected in kidney cortex, and testis.
CC       {ECO:0000269|PubMed:23747249}.
CC   -!- DISRUPTION PHENOTYPE: Viable, with enhanced resistance to diet-
CC       induced hypercholesterolemia and atherosclerosis
CC       (PubMed:10744778). Increased bile acid levels in blood, liver and
CC       gastrointestinal tract, associated with significantly reduced
CC       levels of FGF15 in the ileum (PubMed:23747249).
CC       {ECO:0000269|PubMed:23747249}.
DR   EMBL; KC836882; AGN95783.1; -; mRNA.
DR   EMBL; AL772224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL844839; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL845271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL845417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL845543; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL928841; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL935116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS79736.1; -.
DR   RefSeq; NP_001297384.1; NM_001310455.1.
DR   SMR; A2AJX4; -.
DR   STRING; 10090.ENSMUSP00000116869; -.
DR   PhosphoSitePlus; A2AJX4; -.
DR   PaxDb; A2AJX4; -.
DR   PRIDE; A2AJX4; -.
DR   Ensembl; ENSMUST00000146205; ENSMUSP00000116869; ENSMUSG00000075520.
DR   GeneID; 102635496; -.
DR   KEGG; mmu:102635496; -.
DR   UCSC; uc033hll.1; mouse.
DR   CTD; 340895; -.
DR   MGI; MGI:1928271; Malrd1.
DR   eggNOG; ENOG410IGZP; Eukaryota.
DR   eggNOG; ENOG410XPKY; LUCA.
DR   GeneTree; ENSGT00940000158809; -.
DR   HOGENOM; HOG000197794; -.
DR   InParanoid; A2AJX4; -.
DR   OMA; LPPHNCT; -.
DR   OrthoDB; 72691at2759; -.
DR   TreeFam; TF343455; -.
DR   ChiTaRS; Malrd1; mouse.
DR   PRO; PR:A2AJX4; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; ENSMUSG00000075520; Expressed in 5 organ(s), highest expression level in colon.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR   GO; GO:0070858; P:negative regulation of bile acid biosynthetic process; IMP:MGI.
DR   CDD; cd00112; LDLa; 9.
DR   CDD; cd06263; MAM; 8.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR000998; MAM_dom.
DR   Pfam; PF00057; Ldl_recept_a; 4.
DR   Pfam; PF00629; MAM; 9.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   PRINTS; PR00020; MAMDOMAIN.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00192; LDLa; 10.
DR   SMART; SM00137; MAM; 8.
DR   SUPFAM; SSF49899; SSF49899; 9.
DR   SUPFAM; SSF57424; SSF57424; 9.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01209; LDLRA_1; 6.
DR   PROSITE; PS50068; LDLRA_2; 9.
DR   PROSITE; PS50060; MAM_2; 9.
PE   1: Evidence at protein level;
KW   Complete proteome; Cytoplasmic vesicle; Disulfide bond;
KW   EGF-like domain; Glycoprotein; Membrane; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     26       {ECO:0000255}.
FT   CHAIN        27   2123       MAM and LDL-receptor class A domain-
FT                                containing protein 1. {ECO:0000255}.
FT                                /FTId=PRO_5007184230.
FT   TOPO_DOM     27   2039       Vesicular. {ECO:0000305}.
FT   TRANSMEM   2040   2060       Helical. {ECO:0000255}.
FT   TOPO_DOM   2061   2123       Cytoplasmic. {ECO:0000305}.
FT   DOMAIN       27     68       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN       71    235       MAM 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00128}.
FT   DOMAIN      234    402       MAM 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00128}.
FT   DOMAIN      399    437       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      443    603       MAM 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00128}.
FT   DOMAIN      618    782       MAM 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00128}.
FT   DOMAIN      788    826       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      829    990       MAM 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00128}.
FT   DOMAIN     1015   1052       LDL-receptor class A 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1054   1222       MAM 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00128}.
FT   DOMAIN     1229   1267       LDL-receptor class A 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1271   1431       MAM 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00128}.
FT   DOMAIN     1448   1484       LDL-receptor class A 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1485   1642       MAM 8. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00128}.
FT   DOMAIN     1649   1686       LDL-receptor class A 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1693   1858       MAM 9. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00128}.
FT   DOMAIN     1868   1905       LDL-receptor class A 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1912   1948       LDL-receptor class A 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1951   1989       LDL-receptor class A 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1990   2023       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD    111    111       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1015   1015       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1380   1380       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1749   1749       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     40     58       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID     52     67       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    400    412       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    419    436       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    789    803       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    797    816       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID    810    825       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1016   1029       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1023   1042       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1036   1051       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1230   1242       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1237   1255       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1249   1266       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1449   1461       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1456   1474       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1468   1483       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1650   1663       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1658   1676       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1670   1685       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1869   1882       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1876   1895       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1889   1904       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1913   1925       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1920   1938       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1932   1947       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1952   1965       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1959   1978       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1972   1988       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1991   2002       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   1996   2011       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID   2013   2022       {ECO:0000255|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   2123 AA;  236194 MW;  BD6937E5F0C08F21 CRC64;
     MFLPKAAVSA FSMHGSLCFL WTVCLSISPL SQQGVQAFQC SNGVSLPSDY VCDFTDHCGD
     NSEEQQCWSY GRCNFEDRLC SMTEDQTLQP GWTRRSGIIS NSPPFWDHNG NISAHFLALV
     SRVDSISSNL RSRIFLPTND QQVCQITFYN FSSNQNGKLI AGLQTLCGDP IEHLWQKTEI
     LQSRWERNVI TVQSSQQFQV IFQAQMLATH GQEEVIAIDD ISFSSGCLPA DVCQTCGFDL
     DTCGLATEAS AGRTSWMCTK VREIPSLDSV PWQDQRGHDE GSFVWMRAGH ASVSRLVESS
     AYLNSSVCHC MDGNCRLQFN YTMENSILRV RLYNDKEEKK TWTFNTSTYS TWMKADVLIP
     EDLKAFKVVL EGTVLSQKSF IGIDQLLVYN FGQTHSQKLC SVNEYTPASR QCLTHSSVCD
     SGMDHSNGID EDSEACASLL TWDFESGFCG WEPFPTEDSH WEVVRGLSNG EHLFLEAGHT
     VSRNQGSFIY FGPQKSTAVA RLGSPILTKS LTTFTPCQVR FWYHLSEHSS LSVFTRTSVD
     GSLLKQSEVT QFSDSQWSQA KVDLHAKAEE STLPFQLVLE ATILSSNATV AVDDISISHE
     CEISYKSLRS TSIQNKVADC DFEANSCGWF EASGGDHFDW VWSSQSNLSA DLEQQAPPRD
     HTHGTAQGHF MFILKTSNSL FQTAKLQSPT FSQTGPGCTM SFWFYNYGLS VGAAELQLHL
     ENSRDTTALW RVLYNQGNQW SEATVQLGRL TQPFYLSLEK VSLAVYSGVS AVDDIHFENC
     ALPPPVESCD EPDHFWCRQT KACIGRHQLC DLVDDCGDYT DETGCAPGLQ CNFENGICNW
     EQSTKDDFNW TRYQGPTSTM NTGPMKDHTL GTAKGHYLYI ETSGPQGFQD KAVLLSPILN
     ATEAKVCTFR LYYHMFGKHI YRLAIYQRIW SNTKGQLLWQ IFGDQGNRWI RKDLSITSRK
     PFQILIMASV GDGFTGDIAI DDLSFMDCTL YPDNLPMDIP SPPETSVPVT LPPNNCTDDQ
     FVCRSNGHCV GNIQKCDFRY DCIDKSDESS CVLEVCTFEE RKLCKWYQPI PANSLHDSNT
     FRWGLGNGIS IHHGEENHRP SVDHTKNTTD GWYLYADSSN GKFGDLADIV TPVISLMGPR
     CTLVFWTYMN GATVGSLQVL IKMGNTISKV WAQSGQQGPQ WKKAEVFLGI HSHVEIVFRA
     KRGVSYIGDV AVDDVSFQNC SPLLSTNRKC TTDEFMCANK HCIEKDKLCD FVNDCADNSD
     ETTFICGTSS GRCDFEFDLC TWEQDQDEDI DWNLKASNIP ATSTEPAVDH TLGNSSGHYI
     ILKSFFPQQP VKTGRISSPV ISKRSKDCKI IFNYHMYGSG IAALLLLQVT VTNHTRVLLN
     LTKEQGNFWQ RKELSLSSDE DFRVKFEGRV GEGIRGNIAL DDIVLTKSCL PSHHSTREEP
     AFPLPTGFCP RGYEECQNGR CYSPEQRCNF VDDCGDNSDE NECGGSCTFE KGWCGWKNSL
     AENSDWVLGI GSYKSQRPPK DHTLGNEHGH FMYLEATPVG LHGDKAHFKS ATWQESSAAC
     TMSFWYFISA KATGSIQILI KTDKGLWEVW QQSKPDPGNH WRRATILLGK LRNFEVIFQG
     IRTRDLGGGA AIDDIEFNNC TTVGETTDIC SEETDFLCQD KKCIASHLVC DYKPDCSDTS
     DEAHCGYYTS TAGSCNFETT SGDWTVECGL TQDPEDDLDW SIGSIIPTEG LSRDSDHTPG
     SGRHFLYVNT SLAEEGSTAR IITSHFFPAS LGICTVRFWF YMVDPHIVGI LKVYLIEKSG
     LNILMWSMMR NKNTGWTYAH VPLSSNSPFK VAFEADLGGK EDIFIALDDI TFTPTCASGG
     PALPQPPLCE EGQFACIYAL QCVSASEKCD GQEDCIDGSD EMNCSLGPSP QPCSDTEFQC
     FESQCIPSLL LCDGVADCQF NEDESSCVNQ SCPSGALACN SSGLCIPAHQ RCDGTAHCKD
     IQVDESSCSE CPIHYCRNGG TCVIENIGPT CRCVQGWTGN RCHIRSNLST EGSVHTQNYI
     WTLLGIGLGF LLTHIAVAIL CSLGIRRRPM RKSEGVGNHS FINPVYRNCI NQEKTQSSIY
     SFPNPFYGAA SGSLETVSHH LKS
//
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