ELP_ACRMI
ID ELP_ACRMI Reviewed; 1124 AA.
AC B8UU78;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 25-MAY-2022, entry version 18.
DE RecName: Full=EGF and laminin G domain-containing protein {ECO:0000303|PubMed:23765379};
DE Flags: Fragment;
OS Acropora millepora (Staghorn coral) (Heteropora millepora).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC Astrocoeniina; Acroporidae; Acropora.
OX NCBI_TaxID=45264;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=22490231; DOI=10.1111/j.1365-294x.2012.05554.x;
RA Moya A., Huisman L., Ball E.E., Hayward D.C., Grasso L.C., Chua C.M.,
RA Woo H.N., Gattuso J.P., Foret S., Miller D.J.;
RT "Whole transcriptome analysis of the coral Acropora millepora reveals
RT complex responses to CO(2)-driven acidification during the initiation of
RT calcification.";
RL Mol. Ecol. 21:2440-2454(2012).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 11-23; 37-72; 319-332; 426-450 AND 485-497, TISSUE
RP SPECIFICITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23765379; DOI=10.1093/molbev/mst109;
RA Ramos-Silva P., Kaandorp J., Huisman L., Marie B., Zanella-Cleon I.,
RA Guichard N., Miller D.J., Marin F.;
RT "The skeletal proteome of the coral Acropora millepora: the evolution of
RT calcification by co-option and domain shuffling.";
RL Mol. Biol. Evol. 30:2099-2112(2013).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}. Note=Presence in the organic matrix of the
CC skeleton may be due to shedding of a soluble peptide. {ECO:0000255,
CC ECO:0000303|PubMed:23765379}.
CC -!- TISSUE SPECIFICITY: Component of the acid-insoluble organic matrix of
CC the aragonitic skeleton (at protein level).
CC {ECO:0000269|PubMed:23765379}.
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DR EMBL; JR980881; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; B8UU78; -.
DR SMR; B8UU78; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR CDD; cd00110; LamG; 3.
DR InterPro; IPR028875; CASPR4.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR PANTHER; PTHR15036:SF40; PTHR15036:SF40; 1.
DR Pfam; PF02210; Laminin_G_2; 3.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00282; LamG; 4.
DR SUPFAM; SSF49899; SSF49899; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS50025; LAM_G_DOMAIN; 3.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; EGF-like domain; Membrane;
KW Repeat; Transmembrane; Transmembrane helix.
FT CHAIN <1..>1124
FT /note="EGF and laminin G domain-containing protein"
FT /id="PRO_0000429499"
FT TOPO_DOM 1..1055
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1056..1076
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1077..1124
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 8..203
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 210..369
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 371..413
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 621..788
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 789..825
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1011..1047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1090..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 167..203
FT /evidence="ECO:0000255"
FT DISULFID 342..369
FT /evidence="ECO:0000255"
FT DISULFID 375..386
FT /evidence="ECO:0000255"
FT DISULFID 380..395
FT /evidence="ECO:0000255"
FT DISULFID 397..412
FT /evidence="ECO:0000255"
FT DISULFID 761..788
FT /evidence="ECO:0000255"
FT DISULFID 792..803
FT /evidence="ECO:0000255"
FT DISULFID 797..812
FT /evidence="ECO:0000255"
FT DISULFID 814..824
FT /evidence="ECO:0000255"
FT NON_TER 1
FT /evidence="ECO:0000305"
FT NON_TER 1124
FT /evidence="ECO:0000305"
SQ SEQUENCE 1124 AA; 125297 MW; 09D0FB5A73D4B5E6 CRC64;
RTFVKKYSAS RQFTGEGYLE YRTTSGNIID SDKDELRVEF STVQPSGLLF YARNSGGPFA
DYVALELVGG RLRFSIRYGR SSHSTENLHE TLLGKNLNDA KSHSVEILHD KDVTTIYLDK
TSDQEKAEHS FKTKYTKLDI DVAMYVGGAF DFKALLSVKS NALFMGCIFQ AEFKKILPGP
EKVIDFLKDD KVTTYPRTMN QKCVAQTYEP FTFSSDDSSF VCSVGGLSSA NSLSGSFVFR
TYKPSGVLLK QVDGGNGFEL SYMEMDVQLK VIIRNSETLL NINYQNELTK INKGNWHYVT
FNISQTSFEL SVGSKRETRT PAVTLPSNFF KDGLTAGGFV GCMNELIINK QKCQPNAGSR
IKNVEWSGCN ITDFCIFSPC LHGGECTQTG KTFSCGCSGT GYDKGPNSLS VCQFSESEST
CESLKKNNPS LSLSDRSYAL DFDDSGPIRT YKAFCNFSAD PPTTRVESRD FKIKLTPSKQ
PISQRISYEP SLDAAKALAR RSEWCYQFVD FGCKKAKLHT GSNNEKLGFW VSSNGVYQSY
WGGAKQGSRS CACGETNPNS CIDSSKKCNC DAGLDKWHND EGYLNSTTLL PVVEVMFKGV
TSGTEANFTV GHLYCAGEIS NTATFVNEDG FIKLEKWSPP SNGVISLFFK TPYEKGVLLY
NGMPEKDFFQ VEIINETSVG LSYNIGNGVR KIELSLGDKQ VNDRSWHHVM IYHNMKVFGF
RLDNQEGKHE NPLFLKRELN LNNELYVAGY PYDVSKGFVG CIRGLDVNGE VQDLSKLAGE
AVFVKSGCGA ACENNSCKNH AKCLDNYNVY FCDCSKTPYY GYFCHEENGA SFKDPGSQLV
YEYPSASDVF RFDIVVGFKL GEGKPCIGDI IRLGSSDKSQ FYRLSLTNRK LQFDFKGPRG
QGSITIDPPS VGDFCRDVHT FALSRRYKVV NYTIDGVKKP KEEIERLDGL FTSMKKVTIG
KEGDGGFKGC ITGVKVTREA VGQKPETVEP IKEYLYDDKN TDLVTSKHVS RATCGPEPKV
PEIPTPRPVG QRADVSTPQG ITTNPKLQAE DDDKTAIIVV VVLILVLLLV VLILVIYWYW
ARHKGEYHTH EDDEELKATD PYIEPAAPRK LKGEEPEKKK EWYI
