ID A0A369RXL3_9METZ Unreviewed; 2796 AA.
AC A0A369RXL3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Mucin-like protein {ECO:0000313|EMBL:RDD39428.1};
DE Flags: Fragment;
GN ORFNames=TrispH2_007837 {ECO:0000313|EMBL:RDD39428.1};
OS Trichoplax sp. H2.
OC Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC Trichoplax.
OX NCBI_TaxID=287889 {ECO:0000313|EMBL:RDD39428.1, ECO:0000313|Proteomes:UP000253843};
RN [1] {ECO:0000313|EMBL:RDD39428.1, ECO:0000313|Proteomes:UP000253843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Panama {ECO:0000313|EMBL:RDD39428.1,
RC ECO:0000313|Proteomes:UP000253843};
RC TISSUE=Whole clonal animals {ECO:0000313|EMBL:RDD39428.1};
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:RDD39428.1}.
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DR EMBL; NOWV01000135; RDD39428.1; -; Genomic_DNA.
DR STRING; 287889.A0A369RXL3; -.
DR Proteomes; UP000253843; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 21.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.10.25.10; Laminin; 27.
DR InterPro; IPR005533; AMOP_dom.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003886; NIDO_dom.
DR InterPro; IPR000082; SEA_dom.
DR InterPro; IPR001846; VWF_type-D.
DR PANTHER; PTHR24039; FIBRILLIN-RELATED; 1.
DR PANTHER; PTHR24039:SF28; FIBULIN-1; 1.
DR Pfam; PF12662; cEGF; 2.
DR Pfam; PF12947; EGF_3; 1.
DR Pfam; PF07645; EGF_CA; 19.
DR Pfam; PF12661; hEGF; 1.
DR Pfam; PF06119; NIDO; 1.
DR SMART; SM00723; AMOP; 1.
DR SMART; SM00181; EGF; 28.
DR SMART; SM00179; EGF_CA; 25.
DR SMART; SM00539; NIDO; 1.
DR SMART; SM00216; VWD; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 7.
DR PROSITE; PS50856; AMOP; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 22.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 23.
DR PROSITE; PS50026; EGF_3; 24.
DR PROSITE; PS01187; EGF_CA; 9.
DR PROSITE; PS51220; NIDO; 1.
DR PROSITE; PS50024; SEA; 1.
DR PROSITE; PS51233; VWFD; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000253843};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 2664..2688
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 629..669
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 670..710
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 711..751
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 752..792
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 793..833
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 834..874
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 875..915
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 916..956
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 957..997
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 998..1038
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1039..1079
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1080..1120
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1121..1160
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1161..1201
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1202..1241
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1318..1497
FT /note="NIDO"
FT /evidence="ECO:0000259|PROSITE:PS51220"
FT DOMAIN 1500..1637
FT /note="AMOP"
FT /evidence="ECO:0000259|PROSITE:PS50856"
FT DOMAIN 1649..1848
FT /note="VWFD"
FT /evidence="ECO:0000259|PROSITE:PS51233"
FT DOMAIN 2055..2097
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2139..2178
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2220..2260
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2261..2300
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2301..2342
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2343..2382
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2383..2420
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2428..2540
FT /note="SEA"
FT /evidence="ECO:0000259|PROSITE:PS50024"
FT DOMAIN 2579..2619
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2620..2654
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REGION 2699..2732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2752..2796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2701..2721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2759..2784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 2143..2153
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2644..2653
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RDD39428.1"
SQ SEQUENCE 2796 AA; 308237 MW; CBA4AAF02F05C555 CRC64;
YDDEEDNTET SNDILSTLSP NIITSSPIYD SLQSQTSYVS AYSVDTSVSR IISLLQDILT
STITLTEIEN QSATSLVISS QQVSTLITSE DLLESSLLEN RQETTSMLSS TAYDDEEDNT
ETFNDILSTL SPNIITSSPI YDSLQSQISY VSAYSVDTSV SRIISLLQDI LTSTITLTEI
ENQSTTSLVI SSQQLSTLVT SEDQSVLSFQ ERPYSSEITG FSEKTLPPSL STINIIESSI
VFKDFQVKSG NVSLLTPSTS VLSSLLQDTK TLVFTPTSDI FHYSDTSSSF LVADSSMTSI
PIATYSLYSS RNSPSSELRS SIQSSTDSIL ATSIQQSMLT MISSSTRISS YLFSDVSSLM
KYPNSVKLDQ VITFSTPQSE FSTVSEMYTT STGLSLDSSF AFSLLQSEYS IVSSSYLSIF
SSKTGLLSSI YSSALITPDI FSTTPIQRSE LKLTSALTLD SSIKSSIEPP HDIVSTTPEF
SISTTSIYYP TRFNKSSSFI DLLISAKPSL SSDLVTSISL SEYSIISLSI NQSLSHSYDF
ISNTFLSSMP LAISSSSFSK YSMTLSSLAT DLVSFHSNII SSEGSITVIS TSIETSYPST
TYVVHPILLE STTIAPSTTS EVTSSRLPDI YDCSINTNLC HSKADCINTS GLYNCLCCSG
FTGNGTYCAD IDECAKNQHE CPNRSVCINN IGSYQCQCMS GFSGNGTLCE DIDECTMNQY
RCHNKSMCIN IIGSYQCQCI KGFSGNGTFC EDINECVINE DRCHNRSICI NNIGSYQCQC
INGFSGNGKF CDDKDECALN QHGCHNRSIC INTIGSYQCQ CMNGFSGNGT LCEDIDECAI
NQHECHNRSI CINNIGSYQC QCINGFSDNG TFCEDIDECA LNQHGCHNKS ICINNIGSYQ
CQCINGFSGN GTFCEDIDEC LANEHRCHNR SICINNIGSY QCQCINGFSG NGTLCEDIDE
CVTNAHGCHN RSICINNIGS YQCQCIRGFS GNGTLCKDID ECVAIEHGCH NKSVCINNVG
SYQCRCINGF LGNGTLCEDI DECVTNQHKC HNRSICINNI GSYQCQCING FSGSGTLCED
IDECLANQHN CHSQANCING IGSYECFCRV GYTGNGTICE DVNECKNGNR CHPNSTCHNN
IGSFNCLCLT GFSGNGTHCT DVDECATNQH QCHQQAICSN ILGSYECNCR SGYIGSGTSC
SDINECNGLH NCSSLATCYN TAGSYYCTCN YGLQGNGIYC FREGTRLYPY GLQFGDRSFG
RTDQGSLYLY LSEPIYFVQT SYRGIYISAD GLVSLGFPYL GFRPRRFPRP FNRAIIAPYF
ADCDLRSQSL SSVYYQQYFS YQNTPIAKEI IKNATNDVQQ FQQIAAQNPN NAIYGIFREV
VSNFSATHVI VITWYKVVPY PFWYYWHYPP RKYNTFQLVL ISNGENLFGL FNYEVNGFNW
WKRTPWIRAR VGYSYGVAPF YYEIPWSQRR DQNLLRIDQY RGNTGEIGKW AFRLDDPDIK
HVNYARRCTR WYYAQAYSVY YRRTLPACPC RAAQAILDPR FIYNRRTGCA ISRFSFPGWG
WWWFWPRTYF YLWSRPPRVQ QRCCYSTNRN TAGALIRSYP GGSSFTYVTR SLRQNDEEAY
SACCKLSRLC YLYRIRRPID TCRFYRPPRW SWMWGDPHVE TLDGKKYSFN GVGEYTLIRS
ENNYFTFQGR TKRPFIANTT KLAKATIYTS FAMSKNDSDT VEVKLNENSN TIAIIINKNS
TYNDSHLTNG TVLSFNNIEI SKSSTTYIIS FTSGISAEIQ AVTETLVASV VTSSSLLGIT
KGLLGTYNGN VTDDFLRPDG TYLSINATDE EIYHQFGQLW QIDGNASLFT YPPGRGPGYY
SDPSFVPNFS KDINSLFENN TQLRDEAVKS CNGDAACLFD AAETLSLAVA VGSKNVSESI
ATAQKDINIF PPTITGESIF NVTFGQVFTT VLNISDGNSN KMLELNAANL PPGASIDNET
FVFTWNVTTY KNISFEFTVI NSHNLSAIFK PAIFMCYCAN NGTCQYDSES ITINDTGYAV
CQCASGWVGS FCTQDLDECA GNPCYENVTC TPMQAPATGY TCGLCPGGLQ GDGVKCYDVN
ECETGASLCN QTCVNTVGCY SCLCNAGFEL DANKFDCKDI DECSIIQPCH QICVNSFGSY
SCACNHGYSL NSDNRTCSPI ISCSSISNNC SQTCAVINNK IACSCNEGFN LATDQATCQD
QDECTSNPTI CAHNCTNTVG SYKCSCRSGY QLRADGRTCQ DIDECTNITT CPLNTICTNT
PGSYECQCVD GFQFIGTECE DIDECGRPEL NACNRYASCV NFAGSYNCLC KSGFDGNGIV
CTDINECNNI NNCSGNAQCQ NDIGSYRCIC RNGFTGNGFT CTDINECDNL SSCRREEICY
NTLSSYYCAC KKGFYLDSNT NGTTHCKAGL YYVGEIKLNG RFTSDLSNKG SQAYLLLTTE
TVNKLNAALL ADIRTQYTVR QLIITNVRPG SIVIDFSITL QPNATSVTAQ FLDSVTNRSI
KQIGNYPVAL ITFQDYDQCA DPQANSCSKL QNCTKKPGTY GCTCINGYQL DLQSNNCQDI
DECLVPSRCA NNSICINEPG GFQCQCLDGY SGNGLTECRS LCSSNLCKNG GTCFYSNGTS
LCNCSAGFDG QYCESTSVLT IPTLGIAFGI AGGVLILILT LIGVFVFYHR NKKARSKAEC
GKNSGNASIA SSASSNSDVD DPTQHHGQHQ SQRIESVISL FSEKRYRSSY YQGIRSDEQS
STDRTKRKVP KAENIDLVKN SKKKGVKEKL QRVNRN
//