ID A0A2K5XQ43_MANLE Unreviewed; 2157 AA.
AC A0A2K5XQ43;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=MAM and LDL receptor class A domain containing 1 {ECO:0000313|Ensembl:ENSMLEP00000005410.1};
GN Name=MALRD1 {ECO:0000313|Ensembl:ENSMLEP00000005410.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000005410.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000005410.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR STRING; 9568.ENSMLEP00000005410; -.
DR Ensembl; ENSMLET00000026155.1; ENSMLEP00000005410.1; ENSMLEG00000023899.1.
DR GeneTree; ENSGT00940000158809; -.
DR OMA; YMGDVVI; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 10.
DR CDD; cd06263; MAM; 8.
DR Gene3D; 2.60.120.200; -; 9.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 10.
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 PANTHER; PTHR23282; APICAL ENDOSOMAL GLYCOPROTEIN PRECURSOR; 1.
DR PANTHER; PTHR23282:SF146; ENDOSOMAL GLYCOPROTEIN PRECURSOR, PUTATIVE-RELATED; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00057; Ldl_recept_a; 6.
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; 9.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 9.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 10.
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; 10.
DR PROSITE; PS50060; MAM_2; 9.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..2157
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014348754"
FT TRANSMEM 2075..2097
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 71..229
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 268..427
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 474..637
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 652..816
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 863..1024
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 1088..1256
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 1305..1465
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 1519..1676
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 1727..1892
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 2023..2057
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 40..58
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 52..67
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 434..446
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 441..459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 844..859
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1070..1085
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1264..1276
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1271..1289
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1483..1495
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1490..1508
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1502..1517
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1692..1710
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1704..1719
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1923..1938
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1947..1959
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1954..1972
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1966..1981
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2047..2056
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2157 AA; 241518 MW; 6B49FC213FCD8D3C CRC64;
MLFFLDRRLA FPMSETFCFL WIACVFSSIL GQQGTESFQC DNGVSLPPDS ICDFTDQCGD
NSDERHCLNY ERCDFEDGLC NMTEDQSLQP HWTKRNGMTS LSPPFYDHNG DVSAHFLLLV
SRVDSISSSL RSRVFLPTND QHDCQITFYY FSSQVSGKLM VGLQTACGGP IQHLWQNTAA
LPNQWERNVI KIQSSQRFQV VFQGQMTSMY EQDEVIAIDD ISFSSGCLPA NDGFLLCQEA
LNAEQELCRP DTDLCRFDIT DEELRLCQAC GFEFDMCEWT SEASVGQISW MRTKAREVPA
LESTPQQDQG GDDEGYYVWV GAKHAFPLNH LDNRAYLNSS VCHCLGKSCH LQFYYTMESS
VLRIRLYNNK EEEMFWIYNT STHSQWVKAD VLIPEGLKTF KIIFEGTLLS QRSFIGLDHL
WVYACGQAQS RKLCSADEFP CSCGQCIAKE SVCDSRQDCS DGSDEDPETC AKHLTCDFES
GFCGWERFLT EDSHWKLMKG LNSGEHHFPA ADHTANINHG SFIYLEAQHS PGVAKLGSPV
LTKLLTASNP CQVQFWYHLS QHSHLSVFTR TSLDGNLQKQ GKIIRFSESQ WSHAKIDLIA
KAGESTLPFQ LILEATVFSS NATVALDDIS VSQECEISYK SLPRTSTQSK FSKCDFEANS
CGWFEAISGD HFDWMWSSRS ELSADFEHQA PPRDHSLNAS QGHFMFILKK GSSLWQVAKL
QSPTFSQTGP GCILSFWFYN YGLSVGAAEL QLHMEESHDS TVLWRVLYNQ GERWSDATIQ
LGRLSQPFHL SLDKVSLGIY DGVSAIDDIR FENCSLPLPA ESCEGLDHFW CRHTRACIEK
LRLCDLVDDC GDRTDEVNCT PELQCNFENG ICNWEQDTKD DFDWTRSQGP TPTLNTGPMK
DNTLGTAKGH YLYIESSEPQ AFQDSAALLS PILNATDTKG CTFRFYYHMF GKQIYRLAIY
QRIWRDSRGQ LLWQIFGNQG NRWIRKHLNI SSRQPFQILV EASVGDGFTG DIAIDDLSFL
DCTLYPGNLP ADFPTPPEIS VPVTLPPHNC TDNEFVCRSD GHCIKKMQKC DFKYDCPDKS
DEASCVMEVC SFEKRSLCKW YQPIPVHLLQ DSNTFRWGLG NGISIHHGEE NHRPSVDHTQ
NTTDGWYLYA DSSNGKFGDT ADILTPVISF TGPKCTLVFW THMNGATVGS LQVLIKKDNV
TSKLWAQTGW QGAQWKRAEV FLGIRSHTQI VFRAKRGISY IGDVAVDDIS FQDCSPLLNP
DRKCNAHEFM CANKHCIAKD KLCDFVNDCA DNSDETTFIC RTSSGRCDFE FDLCSWEQEK
DEDFDWNLKA SSIPAAGTEP AADHTLGNSS GHYIFIKSLF PQQPMRAARI SSPVISKRSK
NCKIIFHYHM YGNGIGALTL MQVSVTNQTK VLLNLTVEQG NFWRREELSL FGDEDFQLKF
EGRVGKGQRG DIALDDIVLT ENCLSLRESM QEQLAVPLPT GFCPLGYWEC QNGKCYRLEQ
SCNFVDDCGD NTDENECGSS CTFEKGWCGW HNSLADNFDW VLGVGSHQSL RPPKDHTLGN
ENGHFMYLEA TPVGLRGDKA HIRSTMWRES STACTMSFWY FISAKATGSI QILIKTEKGL
SKVWQESKQN PGNHWQKANI LLGKLRNFEV IFQGIRTRDL GGGAAIDDIE FKNCTTVGEI
SEICPETTDF LCRDKKCIAS HLVCDYKPDC SDRSDEAHCA QYTSTTGSCN FETSSGNWTT
ACSLTQDSED DLDWAIGSRI PAEALIPDSD HTPGSGKHFL YVNSSGSKEG SIARVTTSKS
FPASLGMCTV RFWFYTIDPR SMGILKVYTI EESGLNILVW SVIGNKRTGW TYGYVPLSSN
SPFKVAFEAD LDGNEDIFIA LDDISFTPEC VTGGPVPAQP SPCEADQFSC IYTLQCVPLS
GKCDGHEDCT DGSDEMDCPP SPTPPLCSNM EFPCSTDECI PSLLLCDGVP DCHFNEDELI
CSNKSCSNGA LVCASSNSCI SAHQRCDGFA DCMDFQLDES SCSECPLNYC RNGGTCVVEK
NGPMCRCGQG WKGNRCHIKF NPPTTDFTDA QNNTWTLLGI GLAFLMTHIT VAVLCFLANR
KVPVRKTEGS GNCAFVNPVY GNWSDPEKTE SSVYSFSNPL YGTTSGSLDT MSHHLKQ
//
