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Database: UniProt
Entry: B3EWY9
LinkDB: B3EWY9
Original site: B3EWY9 
ID   MLP_ACRMI               Reviewed;        1594 AA.
AC   B3EWY9;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   09-JUL-2014, sequence version 1.
DT   10-APR-2019, entry version 14.
DE   RecName: Full=Mucin-like 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
RT   of calcification.";
RL   Mol. Ecol. 21:2440-2454(2012).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 57-68; 116-126; 280-293; 312-351; 376-389;
RP   506-529; 562-575; 606-618; 634-650 AND 697-706, TISSUE SPECIFICITY,
RP   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
RT   of 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.
CC       {ECO:0000255, ECO:0000303|PubMed:23765379}.
CC   -!- TISSUE SPECIFICITY: Component of the acid-insoluble and acid-
CC       soluble organic matrix of the aragonitic skeleton (at protein
CC       level). {ECO:0000269|PubMed:23765379}.
DR   EMBL; JR987773; -; NOT_ANNOTATED_CDS; mRNA.
DR   SMR; B3EWY9; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005176; F:ErbB-2 class receptor binding; IEA:InterPro.
DR   GO; GO:0030197; F:extracellular matrix constituent, lubricant activity; IEA:InterPro.
DR   GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR   GO; GO:0010669; P:epithelial structure maintenance; IEA:InterPro.
DR   GO; GO:0010469; P:regulation of signaling receptor activity; IEA:InterPro.
DR   Gene3D; 2.20.100.10; -; 3.
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; IPR009030; Growth_fac_rcpt_cys_sf.
DR   InterPro; IPR039898; Mucin_4.
DR   InterPro; IPR003886; NIDO_dom.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   InterPro; IPR001846; VWF_type-D.
DR   PANTHER; PTHR42668; PTHR42668; 1.
DR   Pfam; PF12662; cEGF; 3.
DR   Pfam; PF06119; NIDO; 1.
DR   Pfam; PF00090; TSP_1; 3.
DR   Pfam; PF00094; VWD; 1.
DR   SMART; SM00181; EGF; 7.
DR   SMART; SM00179; EGF_CA; 6.
DR   SMART; SM00539; NIDO; 1.
DR   SMART; SM00209; TSP1; 3.
DR   SMART; SM00216; VWD; 1.
DR   SUPFAM; SSF57184; SSF57184; 2.
DR   SUPFAM; SSF82895; SSF82895; 3.
DR   PROSITE; PS50856; AMOP; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 3.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 4.
DR   PROSITE; PS50026; EGF_3; 5.
DR   PROSITE; PS01187; EGF_CA; 3.
DR   PROSITE; PS51220; NIDO; 1.
DR   PROSITE; PS50092; TSP1; 3.
DR   PROSITE; PS51233; VWFD; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Membrane; Repeat; Transmembrane; Transmembrane helix.
FT   CHAIN        <1   1594       Mucin-like protein.
FT                                /FTId=PRO_0000429549.
FT   TOPO_DOM     <1   1530       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1531   1551       Helical. {ECO:0000255}.
FT   TOPO_DOM   1552   1593       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      141    196       TSP type-1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      198    253       TSP type-1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      255    310       TSP type-1 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00210}.
FT   DOMAIN      400    566       NIDO. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00570}.
FT   DOMAIN      568    706       AMOP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00347}.
FT   DOMAIN      707    933       VWFD. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00580}.
FT   DOMAIN     1063   1108       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1110   1156       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN     1157   1191       EGF-like 3; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1281   1321       EGF-like 4; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN     1322   1364       EGF-like 5; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    153    190       {ECO:0000255}.
FT   DISULFID    157    195       {ECO:0000255}.
FT   DISULFID    168    180       {ECO:0000255}.
FT   DISULFID    210    247       {ECO:0000255}.
FT   DISULFID    214    252       {ECO:0000255}.
FT   DISULFID    225    237       {ECO:0000255}.
FT   DISULFID    267    304       {ECO:0000255}.
FT   DISULFID    271    309       {ECO:0000255}.
FT   DISULFID    282    294       {ECO:0000255}.
FT   DISULFID   1067   1075       {ECO:0000255}.
FT   DISULFID   1069   1096       {ECO:0000255}.
FT   DISULFID   1098   1107       {ECO:0000255}.
FT   DISULFID   1114   1127       {ECO:0000255}.
FT   DISULFID   1121   1141       {ECO:0000255}.
FT   DISULFID   1144   1155       {ECO:0000255}.
FT   DISULFID   1161   1173       {ECO:0000255}.
FT   DISULFID   1169   1182       {ECO:0000255}.
FT   DISULFID   1285   1296       {ECO:0000255}.
FT   DISULFID   1292   1305       {ECO:0000255}.
FT   DISULFID   1307   1320       {ECO:0000255}.
FT   DISULFID   1326   1341       {ECO:0000255}.
FT   DISULFID   1334   1350       {ECO:0000255}.
FT   DISULFID   1352   1363       {ECO:0000255}.
FT   NON_TER       1      1       {ECO:0000305}.
SQ   SEQUENCE   1594 AA;  176622 MW;  A080A39BA586CFF7 CRC64;
     DTTAGPDTTS APQPTTPTGL CGFIRRQPLP EDNLNALNFT LSNFTVERWC AREPEFKQFL
     AQSVSDRCFG NGSCGVESGI PEVFIFPGFP VVNSPLLVRF YVRLQVNSSV SVVLERTVLT
     SILDRVLENL TAEFGVQFSV DGGFTEWSPF GPCSTSCGPG IQVRFRNCTN PPPINNGSDC
     VGPRNETRPC NNGSCPIDGN FTQWEIWSGC SVTCGKGVQR RFRSCTKPPP SNGGQDCIGD
     RLETRECLKP PCPVDGNFTE WGAWSKCSQT CENGTQVRFR SCTNPPPAFG GRDCMGPTNE
     TRACNDGPCP GRLYPHGLLA NDNLLPNRDA FSNFCGRINL FNQEIPFFIR RHRRVYICRN
     GMLKFRRSAI IRYPQRFPGP RNEDFLFRFR NSYIIAPYWL TISDDAFEQP INTSKVFYRI
     YSKFSRRDRD VLDRANHDVR RFQTSVPQFE AQWVLVVTWL QLYPPTFPGV RLSNSFQVVL
     ITDGQHTFSL FNYPENGIQW STPTGRLFPN LYPPGSGLPV AGYNAGDRNL PFFNLPNSGT
     VNIQNIDQMM GNTNLTGVWF FRLEMNSILS LAGKKCNEWS RQRTSRISPT LPPCPCLFGQ
     ATLDKRYFVD YNQTVSKRGN GTICAYSLPS GSRRWVQQCC YTDLPSGGKV LSSSPPESGG
     PYLIALPGSP VISDADGHEF CCSSSQCSLY YRLRPPRSCF GYTLRRRGLI FGDPHFTTLD
     NTTYTFNGLG EYTIVAIDDE AFEMQARTAR TSGRGLGTAF SAAVAKERGT ATVEARINQK
     AGDLEVLIAG KPFNISTITT TGTNIPDGNI TLVRDSNGSI TALFPSNIAF TFTDVEGTLA
     IAFEAPDDFK NRTKGLLGTW NDDPSDDFVT PDGTLVPADA APRRIHYEFG LKWQINASQS
     LFTYSDLESP STFVDLSYIP MFIDNITWVN DSFRYEAVKA CGNNTQCLFD AAVTEDTSYG
     INTKKLEDNN NEINKELANF PPKILGPKVI NATIGQAIEV KITAEHNSSD FFVFTVNNLP
     DVIILANTSR YLLIRWTPTS LQKVEPVFIV TDSHNSSSEL RPLILLCPCA NGSRCIDDEE
     VSNQRNKGFS FLLLSCTCPA GLTGQYCQHK IDACVENNQP CFPGVKCTDV SSSSNGTRYQ
     CDPCPKGYSG NGSICEDIDE CSDANVSKCD HSCINLPGSY VCDCNQGFSL EGDGTSCKDI
     NECLISNDCM QNCTNLPGGR TCSCLDGFQI DPKDQTACVP ISRCDTFKVG CQQVCVMDRG
     QPKCACHKGY SLNADGRTCD DINECTTHRH KCSQICHNLD GSYTCSCQPG FNLSPDQTTC
     EDIDECGLIN EAHCEGSLEI CINTMGSFRC ECQDGFHRVN DTCQESLPST NGPTGTTGIV
     ASSVSIALTI KDADLHEWQA RLSRMFMDAV AKVVVDYCKG NANGNCYGNA VIAKRYTRSI
     SGTSLVARVH ILNDFPETRD ANLLVAFYVM LSTNQGEVYV MNKDSLLRAL QESQTELSWA
     IKKEISEIRA LKVDDESPTP YETREDGLEM IWLLVGVSVA VAVPLMIVIV ILYREYRRIA
     KQRRKTNNFD LRQWSGARER TIYSGFTNSK SARL
//
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