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Database: UniProt
Entry: A0A3Q3ANM4_KRYMA
LinkDB: A0A3Q3ANM4_KRYMA
Original site: A0A3Q3ANM4_KRYMA 
ID   A0A3Q3ANM4_KRYMA        Unreviewed;      1527 AA.
AC   A0A3Q3ANM4;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=MAM and LDL receptor class A domain containing 1 {ECO:0000313|Ensembl:ENSKMAP00000018001.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000018001.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000018001.1}
RP   IDENTIFICATION.
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   Ensembl; ENSKMAT00000018252.1; ENSKMAP00000018001.1; ENSKMAG00000013362.1.
DR   GeneTree; ENSGT00940000165597; -.
DR   OMA; YMGDVVI; -.
DR   Proteomes; UP000264800; Unplaced.
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; 6.
DR   Gene3D; 2.60.120.200; -; 6.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 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   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; 6.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00192; LDLa; 10.
DR   SMART; SM00137; MAM; 6.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 6.
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; 5.
DR   PROSITE; PS50068; LDLRA_2; 9.
DR   PROSITE; PS50060; MAM_2; 6.
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:UP000264800};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1476..1500
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          111..273
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          319..492
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          544..707
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          755..917
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          951..1106
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          1155..1319
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          1418..1457
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DISULFID        7..19
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        14..32
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        76..88
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        83..101
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        95..110
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        301..316
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        527..542
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        715..727
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        722..740
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        915..927
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        922..940
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        934..949
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1121..1139
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1133..1148
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1349..1364
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1378..1390
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1385..1403
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1397..1412
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1447..1456
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1527 AA;  168730 MW;  9A9C054DD816CEB4 CRC64;
     RVFVTTCSDH EFTCSQGLCV DQDSVCDFTD DCGDGSDEEN QVVIRGELSA NSEAAEVLAI
     DDLSFAEGGA PPPPSCPPSW FHCGEGECVE DSKVCDFTPH CSNGEDEASC SECSFESSSC
     GWYELTLGDG FDWIRGSSVE IPPDYYNHPA LPDHSTNSTE HFMFILKNSS SLHPKAILRG
     PWFQQSASGC TLTFHYNSGI SVGAADMYLR LKGVQNNTAI WTTLYDQGRR WNQVTVQLGR
     ITQPFQIALA KISLGVFDGI SAFDDVSFRN CSMPLAVAAC PTDTHFHCVH TKACVEHLQL
     CDLVDDCGDG SDEEGCPELQ CDFEDGLCNW KQETRGGDEF NWTRISGPTP TLNTGPWRDH
     TLGTWYGHYL YIESSSPQEF KDTAVLLSPV FKPTYQPGKD PAFSHRSHCV FRFYYCMFGS
     HVFSLAVYLR TTSTGRGPML WAKYGNQGNL WHRKTLYLHS AQPFQILIEG TVGDDFKGDI
     AIDDLSFLDC ETLDVTTPAP TVLPHSCPEG QFVCGAYGEC VDLSQVCDFK RDCSDGSDET
     NCKGRCDFEG GDTCGWTIFN PSLVLNHAFV WATDQGETIH DGEQNHRPAN DHTEGWYMCA
     DSSNGGYGQI SDLQTPVISL TGPRCTLVFW YHMSGFTVGS LQVLLRHKNV TYVVWSQTGN
     QSNKWRQGEV FLGLTNNIQQ VVFRAKRGIS YMGDVVIDDV SFQDCSPLLP SDKPCTSEQY
     ACANGHCIPQ DSLCDFINHC GDNSDEDPYI CGFSGRCDFE FDLCSWRQCQ QDDFDWLIKA
     GSTPTIGTGP SSDHTLRDPT GHYLYLESSF PQAVGDAARV IGPLLSRRSS QCKMRFYFHM
     SGDGIGTLNV FTKTDGHDHL LLNLTGDQGN YWQMREIQLS SSRDFKVVFE GKVGRSEKGD
     ICLDDITFSP GCLFCPPGSM LCEKGSCFTP EQSCDFTDDC GDGTDEKDCG TSCSFENGRC
     GWKTSLADNF DWALGTGSVQ SIRPPYDHTL MNENHFVYLE ATPVGLKGDK AHVRSSVWKE
     SSALCKLSFW YYISHKATGT IRLLIKTENN LMEMWNKTGH QGNKWNRAEV PLRKLRNFEV
     IFEGIRSFDV SGGAAVDDLE FIDCAPAAEP GSCPAVTDFV CHSGGCIESH LVCDNKADCA
     DESDEMDCHI FDSPGACDFN MEEEGWEDSC QLFQDADDDF DWRIGHKTET PGAGPHTDHS
     PGEGNFLYIH SAPQREGDVA KVTTRNPFPA SIGLCHLRFW FFMHGSDRMG TLKVYTVGPS
     GAHLLMWAAT GNHGNQWTYA NVILSNTAPF RVTFQAEVGG DVWTDIALDD ISYTAECTVG
     PVTPQPLTCG GDQFQCLYSF QCIPKSWWCD DEPDCTDYSD EEHCPTAVPG TLPPQGLCPA
     RYYQCSDHQC IPSVLRCDGV LDCPDGEDEH SCELVCESPS GCIPPLKRCD ESTDCLPFHT
     DESSCHCLPG WTGNRCHVKE KPSLPTSSPT PEDTRLSVYA GIGIGLLLLA AGVTVCFLAL
     CRKKSNFKSD PMKYGVMDDP DSDWGAE
//
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