ID A0A1X7UHN7_AMPQE Unreviewed; 2092 AA.
AC A0A1X7UHN7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:Aqu2.1.26988_001};
GN Name=100638010 {ECO:0000313|EnsemblMetazoa:Aqu2.1.26988_001};
OS Amphimedon queenslandica (Sponge).
OC Eukaryota; Metazoa; Porifera; Demospongiae; Heteroscleromorpha;
OC Haplosclerida; Niphatidae; Amphimedon.
OX NCBI_TaxID=400682 {ECO:0000313|EnsemblMetazoa:Aqu2.1.26988_001, ECO:0000313|Proteomes:UP000007879};
RN [1] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20686567; DOI=10.1038/nature09201;
RA Srivastava M., Simakov O., Chapman J., Fahey B., Gauthier M.E., Mitros T.,
RA Richards G.S., Conaco C., Dacre M., Hellsten U., Larroux C., Putnam N.H.,
RA Stanke M., Adamska M., Darling A., Degnan S.M., Oakley T.H.,
RA Plachetzki D.C., Zhai Y., Adamski M., Calcino A., Cummins S.F.,
RA Goodstein D.M., Harris C., Jackson D.J., Leys S.P., Shu S., Woodcroft B.J.,
RA Vervoort M., Kosik K.S., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The Amphimedon queenslandica genome and the evolution of animal
RT complexity.";
RL Nature 466:720-726(2010).
RN [2] {ECO:0000313|Proteomes:UP000007879}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lucas S., Shapiro H., Lindquist E., Tice H., Dalin E., Glavina del Rio T.,
RA Bruce D., Barry K., Pitluck S., Srivastava M., Simakov O., Chapman J.,
RA Mitros T., Hellsten U., Putnam N.H., Fahey B., Gauthier M., Larroux C.,
RA Richards G.S., Stanke M., Adamska M., Darling A., Dacre M., Degnan S.M.,
RA Zhai Y., Adamski M., Calcino A., Cummins S.F., Goodstein D.M., Harris C.,
RA Shu S., Woodcroft B., Leys S.P., Manning G., Degnan B.M., Rokhsar D.S.;
RT "The genome of the haplosclerid demosponge Amphimedon queenslandica and the
RT evolution of animal complexity.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:Aqu2.1.26988_001}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2017) to UniProtKB.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00460}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_019854276.1; XM_019998717.1.
DR EnsemblMetazoa; Aqu2.1.26988_001; Aqu2.1.26988_001; Aqu2.1.26988.
DR GeneID; 100638010; -.
DR KEGG; aqu:100638010; -.
DR eggNOG; KOG0994; Eukaryota.
DR eggNOG; KOG1836; Eukaryota.
DR InParanoid; A0A1X7UHN7; -.
DR OrthoDB; 90222at2759; -.
DR Proteomes; UP000007879; Unassembled WGS sequence.
DR CDD; cd00055; EGF_Lam; 14.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 9.
DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 3.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000034; Laminin_IV.
DR InterPro; IPR013015; Laminin_IV_B.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR10574:SF435; LAMININ SUBUNIT GAMMA-1; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
DR Pfam; PF00052; Laminin_B; 1.
DR Pfam; PF00053; Laminin_EGF; 17.
DR PRINTS; PR00011; EGFLAMININ.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00180; EGF_Lam; 17.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 6.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS01248; EGF_LAM_1; 4.
DR PROSITE; PS50027; EGF_LAM_2; 10.
DR PROSITE; PS51116; LAMININ_IVB; 1.
DR PROSITE; PS51117; LAMININ_NTER; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00460};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Reference proteome {ECO:0000313|Proteomes:UP000007879};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..2092
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012304701"
FT DOMAIN 16..224
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51117"
FT DOMAIN 280..325
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 319..515
FT /note="Laminin IV type B"
FT /evidence="ECO:0000259|PROSITE:PS51116"
FT DOMAIN 621..663
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 664..715
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 948..1004
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1005..1057
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1058..1111
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1218..1268
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1318..1371
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1372..1417
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 1463..1507
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT COILED 1739..1766
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1889..1937
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2040..2084
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 280..292
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 282..299
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 301..310
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 637..646
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 664..676
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 666..683
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 685..694
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 979..988
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1029..1038
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1041..1055
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1083..1092
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1095..1109
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1218..1230
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1220..1237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1252..1266
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1343..1352
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1355..1369
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1391..1400
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 1482..1491
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 2092 AA; 226775 MW; C7983736A6182055 CRC64;
MYLLTVLLFS SLVLNSSPQC IPSESVTTPS GDLTLGRLLN ISSECSGGYC PNGILLPCTS
NSSGLISDDN TDTMWISEVD PDLPVTITLD LTNLMILHDI NIQWESPTPS SMILERSSDY
GLNWSVYRYW STDCSSDFNM SSISVYDTDI MNTTDPICTD TDLADYPGSE VSFSVYSHCF
SDPSYQLVTN VRLSILNVTA ATNATNDTDC GAFVAISELS LNGSCHCNGR AENCQPLGTE
TNHTNKVYSG CECASSYKGT HCQQCQDEYY DISSGCTKSC SCNEMGSTNK SCDSVTGQCY
CKTGVTGDKC NETANGYYFR ALDHNIAEAE YGQLSMGITG YYPIDTALRY TGKGLVRIPA
TGGTVGLSMT VDKTGPYSVI LRYTTTIDID SVFVSIQSSR NVTQSLDCVN QSQPIPTSYN
STMLTLLSLQ GYNPNTRVHC FEEGITYNIT VNYYPTTGHE WMLDSVVLSP DQTDYINSLP
IVQMFSTITC LTLIAELENP QYCHPHVFNL SLLFYGEVYE CGSPNSIGIT GDTCDPYGGS
WGCSSNYTGT LCTDCSNGYY NNTNGRCIEC PFLCNSTGSI NVACDTDTGS CVCKDNVIGE
ECDSCPSSNH VFSSSGCIDT CNCTYGSCNV TNGDCICPPN VMGDQCESCD DYHYSISDAG
CIACECNPRG SLSLSCDNVT GQCDCKDAAV GTQCNDCPTN GHYKTVGSDQ SLCLPCFCFN
HSQTCQPDSS NYIQGNVQSN FTELCPLNMD CTDGWTFNDD NNTFNNPDSL SYTIFGDASP
VFIAPDRYHD DYHLSYGLNI IINIQLTSTS QRIDSFIWIN GSGLTIVHKM IVEGNQITVP
LVESYWRLGE DYDSSNTSTP YQFISVLTNI TDIRFSAKFT DNMYIEINYF QGFRIQTIDR
RNTSIDPGAD YTVGHCECPA GHTGVFCDEC MNGYYRPSGV LLDLCIPCNC NGHADSCDPA
TGVCINCTGN TEGDQCQSCS TGYSGTDCSQ CDNGYYNESN TCIKCDCNGN TDPSLFPSCN
ASTGQCINCL NNTTGDKCQT CLPGYYGDVI NSKPCEPCEC NINGTQSVDN PCIPGIPFET
CVCKPFVTGA HCTTCIDGYY GDPINGIDCL QCPCPTEENS HSSSCHEGAG GVVCNNCEDG
YTGDRCEICA DGHYGNATIG LCSNCTCNDN FDISLGSSCD KTTGHCSGCT NNTEGTQCQF
CITGYYGNVE MKVPCKSCSC NLNATISGVC DRSTGVCWCK EHVSPDSGCN TCIPGYYGNP
ANGGDCFPCS CNNRSSTCYL GNDGSGICDD CSTGYAGDQC EECSDGYFME DNGTCSRCNC
NGNIDPALPG LSCNSSTGVC LQCLYNTTGE QCEECSNGYY GNPANGTPCQ KCNCSASGTL
RCDTKTGDCI CHPNITGPDC SECMDTLWGS PDEGCRPCNC CTNNTKCDKE TGQCPCYDIT
LDRTCCDCIH GYYNYSITGC TACDCGMLSE SAQCNSTGHC QCLPEGTGTK CDSCQTGFTG
IAPNCTECDD CHFIWSDTLS SLQLNITDLS TRILTILHYY EGYTQSDISS VINNISMTLT
MSEELLMQQS IDTKIFNNIT AILTEIINNY TSLMNDISLL NPTIMDANAT LRLAEQYIQN
ITSSGYQNYT ITEIHPSLVS LNNTLNLLLG QSMNQSLLLE EYRDEVISLM NLVLALQGNA
SMEEEAILNA NITSHTAQAM VDSTRSFIKN ISVINDTLLD IEEDVRNIEI DINASDTSYT
DLDTDIQMLN NKINNLMTQL NTLSGLSEGL YISAKVLKQQ SYNSVVSVGA LMASANAAMD
DAQSLIMMIN KAQDGVMNST IKLVESDELA TNISSLELPS LSSATELAAN INSSIIPDSD
ITDLLTDANN SVVAAMEALE GAMNTSAMVT DLEYKVSNLT NNIKETRRRL ESAEQTHNET
NRNIESINTT LREVNETVQS VPDTYTLSET AKDKERDLTQ GETVLQAASM NATSLNNAVQ
QILSNVTSEQ MLMESIAVNV SSVKDEAMLR VNASMTALNK TDELTESAQQ LNNTANTVKL
QRLKSLLAEY QSKVVEAQAV RSKIGQLQNE LKTMTADFTE AMERYKRCYK TP
//
