ID A0A2Y9FXZ6_TRIMA Unreviewed; 2158 AA.
AC A0A2Y9FXZ6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=LOW QUALITY PROTEIN: MAM and LDL-receptor class A domain-containing protein 1 {ECO:0000313|RefSeq:XP_012412174.1};
GN Name=LOC101355277 {ECO:0000313|RefSeq:XP_012412174.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_012412174.1};
RN [1] {ECO:0000313|RefSeq:XP_012412174.1}
RP IDENTIFICATION.
RG RefSeq;
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_012412174.1; XM_012556720.1.
DR STRING; 127582.A0A2Y9FXZ6; -.
DR GeneID; 101355277; -.
DR KEGG; tmu:101355277; -.
DR InParanoid; A0A2Y9FXZ6; -.
DR OrthoDB; 2905895at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 8.
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; 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:SF146; ENDOSOMAL GLYCOPROTEIN PRECURSOR, PUTATIVE-RELATED; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00057; Ldl_recept_a; 7.
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; 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; 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:UP000248480};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..2158
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016165992"
FT TRANSMEM 2076..2099
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..228
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 267..426
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 473..636
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 651..815
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 862..1027
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 1091..1259
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 1308..1468
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 1521..1678
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 1729..1893
FT /note="MAM"
FT /evidence="ECO:0000259|PROSITE:PS50060"
FT DOMAIN 2024..2058
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 39..57
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 51..66
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 433..445
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 440..458
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 843..858
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1073..1088
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1267..1279
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1274..1292
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1485..1497
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1492..1510
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1504..1519
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1694..1712
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1706..1721
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1924..1939
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1948..1960
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1955..1973
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1967..1982
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2048..2057
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 2158 AA; 241893 MW; 53FA5ADBFF93619A CRC64;
MLFWLTRMLA LPMNEVCYFL WISCAFISTV QQGTEDFQCN NGVSLPPDNV CDFTDQCGDN
SDEQQCSYYE RCNFEDGLCT MTQDQSLQLG WIKRNGMSDT SPPFYDHNGD MTAHFLSLVS
RLDSTSSNLR SRIFLPTNNQ NACQITFYHF FSQVSGQLMV GLQTACDSPI QHLWQNTAGL
KDAWERNVIK IHSSQRFQIV IQGQMISTHE QDEVIAIDDI SFSSGCVPTN DESLQCQEAS
NTKQELCYPD TNLCQFDSTD EGLRSCQACE FEFDMCDWSS DVSTGQISWT RTKAREVPAL
ESTPHQDQSG DEEGYYVWIG AKQAFTLNHL VRRAFLNSSV CHCLGKGCHL QFYYSMENSV
LRVGLYNNEE EEVFWTYNTS TNSKWVKADV LIPEDMKEFK IVFEGALLSQ ISFIGLDHLW
VYACAQARSG KLCSADEFTC ATGQCIAQEL VCDAQQDCSD RSDEDPATCS NHIMCDFETG
FCGWKQLLTE DPHWEVVNGL MGREYHLPNA DHTTNTSHGS FIYFGTQQPP GVAKLGSPIL
TKLLTASTPC QVRFWYHLSQ HSRLSVFTRT SLDEKLQKQC DLTGFSKSQW SQAKIDLYVK
TGETTVPFQL ILEATILSSN ATVALDDIDI SQECEISYES LPGTSIKNQA SKCDFEENSC
GWFEAISGDH FDWIWSSRSN LSADFEQQAP SEDHTHNTVQ GHFMFILKKN SSFSQVAKLQ
SPTFGQTGPE CTLSFWFYNY GLLVGAAELQ LHVGRSNDST VLWRVLYNQG NQWSEATIQL
GRLTQPFHLS LDKVSFGFYD GISAIDDIRF ENCSLPPPAE SCEGPDHFWC RYTKACVEKL
RLCDLVDDCG DNSDEADCAP ELQCNFENGI CNWEQDTEDD FDWTRNQGPT STLNTGPMKD
NTMGTAKGHY LYIESSEPQV FQNRAALLSP ILNATDTMGC TFRLYYHMFG KHIYRLAIYQ
RIWRNTRGQL LWQIFGNQGN RWIRKCLNVS SVQPFQILFE NSLLNDFFVG DXFLEDPSYL
DYVVCVLMPG NLPVDFPTPT KTSIPVTLSP HNCTDHEFAC RSNGHCIEKI QKCDFRHDCP
DKSDESSCVM EVCSFEEESL CKWYQPIPVN LFQNLNTFRW GLGNGRGIHH GEENHRPSVD
HTTNTMDGWY LYADSSNGKF GDTADILTPV ISLTGPKCAL LFWTHMNGAT VGSLQVLNKK
GNVTSKLWAQ TGQQGAQWKK VEVFLGIHSH IQIVFRAKRG ISYIGDVAVD DISFQDCSPL
LSPDRKCTAQ EFMCANKHCI PKDKLCDFVN DCADNSDETT LICSNSVVRC DFEFDLCSWE
QDQDDDFDWN LKASSIPTVG TEPAADHTLQ NSSGHYIFIK SLFTQQPMRE ARISSPVISK
RSKNCKIIFY YHMYGNGIGG LTLIQVSVSN QTKVLFNLTG EQGNFWQRKE LSLFGDEDFQ
LKFEGRVGKG HCGDIALDDI VLTRSCLSSH SIKEEQAMPL PAGYCPHGYP ECQNGKCYRP
AQSCNFAGDC GHNTDENECG SSCTFEKGWC GWQNSLAENF NWVLGVGSHQ NLRPPTDHTL
GNETGHFLYL EATPVGLQGE EAHLKSAVWQ ESSAACTMSF WYFLSAKATG SIQVLIKTEK
GLSKVWQESD QNSRDHWQKA IILLGKLRNF EVIFQGIRMR DLGGGAAIDD IEFKNCMTVG
ETSEICPEGT DFLCNNKKCI ASHLVCDYKP DCSDKSDEAH CSQYTSTTGS CNFEASGNWT
TVCSLTQDSQ DDLDWVIGKR IPAETWEPDS DHTPGNGQHF LYVNSSGPRE GYTARITTSK
YFPASLGICT VRFWFYMVDP NNMGILKVYT IEESGLNILV WSVIGNKRTG WIYGYVPLSS
NSPFKVAFEA DLAGDEDIFI ALDDISFTPE CVFGGPVTPQ PSPCEADQFS CIYVLQCVPL
TGTCNGQEEC IDGSDEMDCS LSPPPQLCSE MEFQCSANQC IPSLLLCDGV PDCHFNEDES
SCSNESCTNG ALTCTSSNSC IPAHQRCDGF ANCHDFQLDE SSCSECPVSY CKNGGTCVVE
KNGPMCRCGQ GWKGNRCHIK FDPPPPADFA YMQNSIWTLL GIGLVFLITH ITVAVLCFLA
NRKLRIRKTE ERGNCAFVPA IYGNWSNPEK TESPLYSFSN PLYGTTSGSL ESISNHLR
//
