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Database: UniProt
Entry: A0A369RRY9_9METZ
LinkDB: A0A369RRY9_9METZ
Original site: A0A369RRY9_9METZ 
ID   A0A369RRY9_9METZ        Unreviewed;       765 AA.
AC   A0A369RRY9;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=MAM and LDL-receptor class A domain-containing protein 2 {ECO:0000313|EMBL:RDD37229.1};
GN   ORFNames=TrispH2_010597 {ECO:0000313|EMBL:RDD37229.1};
OS   Trichoplax sp. H2.
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD37229.1, ECO:0000313|Proteomes:UP000253843};
RN   [1] {ECO:0000313|EMBL:RDD37229.1, ECO:0000313|Proteomes:UP000253843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Panama {ECO:0000313|EMBL:RDD37229.1,
RC   ECO:0000313|Proteomes:UP000253843};
RC   TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD37229.1};
RX   PubMed=30042472; DOI=10.1038/s41598-018-29400-y;
RA   Kamm K., Osigus H.J., Stadler P.F., DeSalle R., Schierwater B.;
RT   "Trichoplax genomes reveal profound admixture and suggest stable wild
RT   populations without bisexual reproduction.";
RL   Sci. Rep. 8:11168-11168(2018).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RDD37229.1}.
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DR   EMBL; NOWV01000261; RDD37229.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369RRY9; -.
DR   Proteomes; UP000253843; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   CDD; cd00108; KR; 1.
DR   CDD; cd06263; MAM; 1.
DR   Gene3D; 2.60.120.200; -; 2.
DR   Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR   Gene3D; 3.10.250.10; SRCR-like domain; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000001; Kringle.
DR   InterPro; IPR013806; Kringle-like.
DR   InterPro; IPR038178; Kringle_sf.
DR   InterPro; IPR000998; MAM_dom.
DR   InterPro; IPR001190; SRCR.
DR   InterPro; IPR017448; SRCR-like_dom.
DR   InterPro; IPR036772; SRCR-like_dom_sf.
DR   PANTHER; PTHR23282; APICAL ENDOSOMAL GLYCOPROTEIN PRECURSOR; 1.
DR   PANTHER; PTHR23282:SF146; ENDOSOMAL GLYCOPROTEIN PRECURSOR, PUTATIVE-RELATED; 1.
DR   Pfam; PF00051; Kringle; 1.
DR   Pfam; PF00629; MAM; 1.
DR   Pfam; PF00530; SRCR; 1.
DR   PRINTS; PR00018; KRINGLE.
DR   SMART; SM00130; KR; 1.
DR   SMART; SM00137; MAM; 1.
DR   SMART; SM00202; SR; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF57440; Kringle-like; 1.
DR   SUPFAM; SSF56487; SRCR-like; 2.
DR   PROSITE; PS50070; KRINGLE_2; 1.
DR   PROSITE; PS50060; MAM_2; 1.
DR   PROSITE; PS50287; SRCR_2; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00196};
KW   Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW   ProRule:PRU00121}; Membrane {ECO:0000256|SAM:Phobius};
KW   Receptor {ECO:0000313|EMBL:RDD37229.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253843};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        629..649
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          64..155
FT                   /note="MAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50060"
FT   DOMAIN          201..276
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          294..340
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          343..444
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   REGION          688..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..751
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        369..433
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        382..443
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT   DISULFID        412..422
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ   SEQUENCE   765 AA;  84533 MW;  CE027B28FC9E9CAF CRC64;
     MEYVMGSSSR KIVMLWFISM IILSASIIVE GVHESNRCQQ YREKRCQFNT SSVYSFSVPP
     VYYTRCNFDS DTCGWNQLKN IDFFDWTRSK GSLPSAGTRS LYDHTQNNGS GFYMYIDASV
     NNYGTYADLI SPPLQLSAVG DKIRISFYYH AFGSSLGELH VYAVYPRHEN AFHILLRGMV
     GSTHSSNIAI DDISVLSVET SCYTSHGEFY RGTENYARNG SVCQNWHSFN LTTSYATANH
     LMSNYCRNPF GSTRNHPWCF TDTLTRQWQY CNISRCNPLL IPTPAYPLGT PYPLSFVHNL
     VEQTNVGRVV LYHNGQWGTI CRAGLKASTA ALMCQSFGIG TVGQLTSIGG NDTSGVIYVG
     VNDRYGIICF SAWNLNSADV ACRQMGYIGA YSSNVTTSIY PTRSVLIDLI ECNGYESSIG
     QCKALIVSSS SSCLSTSIAT ASCNSGQKSY TSNNKPSNCQ FEYGLCGWNT TGNPTWIWHP
     AGTGRFAGFS NDMSYLQLVR PPGYANPITA VFSSPPFERI DTSVYITFRY ILNSHFSGVF
     EIQYAMLTMQ YFDRIYHNAF TSADFNTWLS VTTTTFRPSS SSLFRINFFY KSPPTSSNSE
     ISVIGLDDIR VYGVDGIHPS HAAHNLTRLG IGCGVGLTVL MFIIAYAYVV RYRRRLERGG
     RSTIANVNLN GQGENGVVTA DTHFNGASMN SVQNLPPPSY PAAINSHATG ETPSSQSGCD
     NNDHNSELGT NNLRYQVDSN SQLSTKSPAD PSLAPPTYDQ AASRQ
//
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