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Database: UniProt
Entry: M3ZJE5_XIPMA
LinkDB: M3ZJE5_XIPMA
Original site: M3ZJE5_XIPMA 
ID   M3ZJE5_XIPMA            Unreviewed;      1824 AA.
AC   M3ZJE5;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=MAM and LDL receptor class A domain containing 1 {ECO:0000313|Ensembl:ENSXMAP00000002337.2};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000002337.2, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000002337.2}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000002337.2};
RG   Ensembl;
RL   Submitted (NOV-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   RefSeq; XP_014324092.1; XM_014468606.1.
DR   Ensembl; ENSXMAT00000002342.2; ENSXMAP00000002337.2; ENSXMAG00000002333.2.
DR   GeneID; 102221902; -.
DR   KEGG; xma:102221902; -.
DR   CTD; 340895; -.
DR   eggNOG; KOG1095; Eukaryota.
DR   GeneTree; ENSGT00940000165597; -.
DR   HOGENOM; CLU_002270_0_0_1; -.
DR   InParanoid; M3ZJE5; -.
DR   OMA; YMGDVVI; -.
DR   OrthoDB; 2905895at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   CDD; cd00112; LDLa; 9.
DR   CDD; cd06263; MAM; 7.
DR   Gene3D; 2.60.120.200; -; 7.
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:SF142; MAM AND LDL-RECEPTOR CLASS A DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00057; Ldl_recept_a; 8.
DR   Pfam; PF00629; MAM; 7.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00192; LDLa; 10.
DR   SMART; SM00137; MAM; 7.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 7.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 9.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01209; LDLRA_1; 7.
DR   PROSITE; PS50068; LDLRA_2; 10.
DR   PROSITE; PS50060; MAM_2; 7.
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:UP000002852};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1824
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017455366"
FT   TRANSMEM        1705..1727
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          64..217
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          265..429
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          476..649
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          712..878
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          927..1086
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          1142..1298
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          1349..1513
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          1649..1683
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   REGION          1756..1779
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        26..38
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        33..51
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        45..60
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        229..241
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        236..254
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        248..263
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        457..472
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        694..709
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        886..898
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        893..911
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1106..1118
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1113..1131
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1125..1140
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1314..1332
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1326..1341
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1544..1559
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1573..1585
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1580..1598
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1592..1607
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1673..1682
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1824 AA;  201764 MW;  8C9DD50ECE7358A9 CRC64;
     MALLLGTVWL LLALNLLISS VFVSACSHQE FTCRQGFCVA LDSVCDFTDD CGDGSDEENC
     STYTRCDFEE SFCDLIQNSE SLYRWTRTAE APGLKQDHRN TSAHFLSLSP IGGKKITAEL
     RSPVFLPTHG CQIRFYHYAG TGHGELQILL QPHLVAQSSE LWKHSFQLEK GTWLRAVVHF
     SSNQRFQVVI RGELSASSEA SEVLAIDDLS FSPGCVILPE GRVLTSLPCP PSWFTCARGR
     CIEESKVCDF TPYCPNGEDE ARCPSECDFE DGSCGWYELT PGDGFDWIRG SSDKVPPDYY
     DHPPLPDHTT NSTKGHFMFI LKNSSSLHPN AVLIGPWFQQ SASRCTMTFW HYNSGISVGA
     ADIYLRFKGV QNKTVIWTTL YDQGRLWNRV TIQLGRITQP FQIALAKISL GVFDGVSAFD
     DVSFKNCSMP PAVAVCPKHT HFHCLHTKAC VEHLQLCDLV DDCGDGSDEE GCSPEIQCDF
     EDGLCNWKQE TSGGDVFNWT RIQGPTPTQN TGPWKDHTLG NTSGHYLYIE SSLPQEFKDT
     AVLLSPVFEP TDQPGKDPAW SPHRRCAFRF HYCMFGSHVF SLAVYMRTTT TDRGMLLWAK
     YGNQGNLWHR KTMYLNSVQP FQILIEGTVG DDFEGDIAID DLSFLDCQLF HGELPSLITP
     PLTTPAPTVI PNNCSKGQFV CGTHGECVLL SQVCDFKQDC SDGSDETNCV KERCDFEGGV
     SCGWTVVSPS SSVNHVFRWA ADQGESSHDG EQNHRPTNDH TLNSPKGWYM YADSSNGGYG
     QFSDLQTPVI SSTAPQCTLI FWYHMSGFTV GTLQVLLRHK NVTHVVWSQT GNQGNRWKRA
     EVFLGLLNDF QVVFRAKRGI SYMGDIVIDD VSFQDCSPIL PSGQPCTSEQ FACANSHCIP
     QDNLCDFINH CGDNSDEDPF ICKGFSGRCN FEFDLCSWRQ CQEDDFDWLI KAGSTPTVGT
     GPSSDHTLRD PAGHYLYLES SFPQAVGDAA RVIGPLLSRR SSQCKMRFYY HMSGDGIGTL
     SVFTKTEASL HLLLNLTGDQ GNYWQMKELQ LSSSADYQIV FEGKVGRSEK GDICLDDITF
     SPGCLLSPSV LVIDSTPPPA PPTGFCPPGA SVCGKGSCYT PEQMCDFTYD CSDGTDEKDC
     GTSCSFENGR CGWKSSLADN VDWALGTGSV QRIRPPYDHT LMDENGHFVY LEATPLGLKG
     DKAHIRSSVW KESSAVCKLS FWYYLSHKAT GTIRLLIKTE NSLIEMWKKT GHQGNQWIQA
     VVPLRNLRNF EVIFEGIRSS DVSGGAALDD LEYIDCAPSA MEPGGCPAVT DFVCESGHCI
     ESHLVCDNKA DCADESDEKD CDYIFGLPGA CNFNMEDDRW EQICQLSQDP DDDFDWMIGH
     RTEIGVGPQS DHSPDGGGNF LYIHSGTQRE GDVAKVMTMN PFPASIGLCH LRFWFFMYGS
     TTMGTLKVYT VGPNGTPLLM WATTGNHGNQ WTYANVILSN TKDFRVTFQA KVGGDMWTDI
     ALDDISYTAE CVVGGPVTPQ PLTCDTEQFQ CTHSFQCISK SWWCDGSPDC ADQSDEERCP
     TALPGTVPPQ GDCPDENFQC SDLLCLPALL RCDGVYDCPN GEDEHGCPLL QCEPGELVCE
     SWPGCVPLHM RCDRSSDCQP FHSDESSCHE CPPTYCQDRG SCHLEENGPL CLCEPGWSGN
     RCHVKEKPFL TTSSPTVEAT QLDSVYAGIG IGSVLLLAGF AVCFLALCKK KCGFIKADPM
     KYGVMDNPSF EWRAENLSED KSPDSGPSIN PKTSDGLGLP ISVYPWRREV EQGSNWKDAK
     LSFSNPMYNY PCDTNGAGNR SAEE
//
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