MALR1_MOUSE
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 03-AUG-2022, entry version 104.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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, SUBCELLULAR
RP 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 modulate
RT 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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT 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 and
RT atherosclerosis on mouse chromosome 2.";
RL J. Lipid Res. 41:573-582(2000).
CC -!- FUNCTION: Enhances production and/or transport of FGF15 and thus has a
CC 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 small
CC intestine. Also detected in kidney cortex, and testis.
CC {ECO:0000269|PubMed:23747249}.
CC -!- DISRUPTION PHENOTYPE: Viable, with enhanced resistance to diet-induced
CC hypercholesterolemia and atherosclerosis (PubMed:10744778). Increased
CC bile acid levels in blood, liver and gastrointestinal tract, associated
CC with significantly reduced levels of FGF15 in the ileum
CC (PubMed:23747249). {ECO:0000269|PubMed:23747249}.
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; 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 AlphaFoldDB; A2AJX4; -.
DR SMR; A2AJX4; -.
DR STRING; 10090.ENSMUSP00000116869; -.
DR GlyGen; A2AJX4; 4 sites.
DR PhosphoSitePlus; A2AJX4; -.
DR PaxDb; A2AJX4; -.
DR PRIDE; A2AJX4; -.
DR ProteomicsDB; 287304; -.
DR Antibodypedia; 62980; 14 antibodies from 6 providers.
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 VEuPathDB; HostDB:ENSMUSG00000075520; -.
DR eggNOG; KOG1095; Eukaryota.
DR GeneTree; ENSGT00940000158809; -.
DR HOGENOM; CLU_002270_0_0_1; -.
DR InParanoid; A2AJX4; -.
DR OMA; GGDMWTD; -.
DR OrthoDB; 72691at2759; -.
DR TreeFam; TF343455; -.
DR BioGRID-ORCS; 102635496; 0 hits in 32 CRISPR screens.
DR ChiTaRS; Malrd1; mouse.
DR PRO; PR:A2AJX4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AJX4; protein.
DR Bgee; ENSMUSG00000075520; Expressed in ileum and 15 other tissues.
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 Gene3D; 4.10.400.10; -; 9.
DR InterPro; IPR013320; ConA-like_dom_sf.
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 Cytoplasmic vesicle; Disulfide bond; EGF-like domain; Glycoprotein;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..2123
FT /note="MAM and LDL-receptor class A domain-containing
FT protein 1"
FT /evidence="ECO:0000255"
FT /id="PRO_5007184230"
FT TOPO_DOM 27..2039
FT /note="Vesicular"
FT /evidence="ECO:0000305"
FT TRANSMEM 2040..2060
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 2061..2123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 27..68
FT /note="LDL-receptor class A 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 71..235
FT /note="MAM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 234..402
FT /note="MAM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 399..437
FT /note="LDL-receptor class A 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 443..603
FT /note="MAM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 618..782
FT /note="MAM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 788..826
FT /note="LDL-receptor class A 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 829..990
FT /note="MAM 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 1015..1052
FT /note="LDL-receptor class A 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1054..1222
FT /note="MAM 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 1229..1267
FT /note="LDL-receptor class A 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1271..1431
FT /note="MAM 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 1448..1484
FT /note="LDL-receptor class A 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1485..1642
FT /note="MAM 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 1649..1686
FT /note="LDL-receptor class A 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1693..1858
FT /note="MAM 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 1868..1905
FT /note="LDL-receptor class A 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1912..1948
FT /note="LDL-receptor class A 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1951..1989
FT /note="LDL-receptor class A 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DOMAIN 1990..2023
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1015
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 52..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 400..412
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 419..436
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 789..803
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 797..816
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 810..825
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1016..1029
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1023..1042
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1036..1051
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1230..1242
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1237..1255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1249..1266
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1449..1461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1456..1474
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1468..1483
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1650..1663
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1658..1676
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1670..1685
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1869..1882
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1876..1895
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1889..1904
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1913..1925
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1920..1938
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1932..1947
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1952..1965
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1959..1978
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1972..1988
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00124"
FT DISULFID 1991..2002
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1996..2011
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 2013..2022
FT /evidence="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
