MLP_ACRMI
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 25-MAY-2022, entry version 21.
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 of
RT 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; 506-529;
RP 562-575; 606-618; 634-650 AND 697-706, TISSUE SPECIFICITY, AND
RP 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 and acid-soluble
CC organic matrix of the aragonitic skeleton (at protein level).
CC {ECO:0000269|PubMed:23765379}.
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DR EMBL; JR987773; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; B3EWY9; -.
DR SMR; B3EWY9; -.
DR PRIDE; 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:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR Gene3D; 2.20.100.10; -; 3.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR005533; AMOP_dom.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
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; IPR013783; Ig-like_fold.
DR InterPro; IPR003886; NIDO_dom.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR001846; VWF_type-D.
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
FT /note="Mucin-like protein"
FT /id="PRO_0000429549"
FT TOPO_DOM <1..1530
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1531..1551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1552..1593
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 141..196
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 198..253
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 255..310
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 400..566
FT /note="NIDO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00570"
FT DOMAIN 568..706
FT /note="AMOP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00347"
FT DOMAIN 706..901
FT /note="VWFD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 1063..1108
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1110..1156
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1157..1191
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1281..1321
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1322..1364
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 153..190
FT /evidence="ECO:0000255"
FT DISULFID 157..195
FT /evidence="ECO:0000255"
FT DISULFID 168..180
FT /evidence="ECO:0000255"
FT DISULFID 210..247
FT /evidence="ECO:0000255"
FT DISULFID 214..252
FT /evidence="ECO:0000255"
FT DISULFID 225..237
FT /evidence="ECO:0000255"
FT DISULFID 267..304
FT /evidence="ECO:0000255"
FT DISULFID 271..309
FT /evidence="ECO:0000255"
FT DISULFID 282..294
FT /evidence="ECO:0000255"
FT DISULFID 1067..1075
FT /evidence="ECO:0000255"
FT DISULFID 1069..1096
FT /evidence="ECO:0000255"
FT DISULFID 1098..1107
FT /evidence="ECO:0000255"
FT DISULFID 1114..1127
FT /evidence="ECO:0000255"
FT DISULFID 1121..1141
FT /evidence="ECO:0000255"
FT DISULFID 1144..1155
FT /evidence="ECO:0000255"
FT DISULFID 1161..1173
FT /evidence="ECO:0000255"
FT DISULFID 1169..1182
FT /evidence="ECO:0000255"
FT DISULFID 1285..1296
FT /evidence="ECO:0000255"
FT DISULFID 1292..1305
FT /evidence="ECO:0000255"
FT DISULFID 1307..1320
FT /evidence="ECO:0000255"
FT DISULFID 1326..1341
FT /evidence="ECO:0000255"
FT DISULFID 1334..1350
FT /evidence="ECO:0000255"
FT DISULFID 1352..1363
FT /evidence="ECO:0000255"
FT NON_TER 1
FT /evidence="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
