CADN_ACRMI
ID CADN_ACRMI Reviewed; 1675 AA.
AC B3EWZ3;
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=Coadhesin {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 72-84; 192-215; 607-616; 620-630; 664-724; 736-764;
RP 849-869; 877-904; 933-957; 986-1001; 1014-1031; 1037-1050; 1093-1120;
RP 1135-1150 AND 1176-1187, TISSUE SPECIFICITY, AND IDENTIFICATION BY MASS
RP 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; JT016638; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; B3EWZ3; -.
DR SMR; B3EWZ3; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 8.
DR Gene3D; 3.40.50.410; -; 3.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF00090; TSP_1; 8.
DR Pfam; PF00092; VWA; 3.
DR SMART; SM00231; FA58C; 2.
DR SMART; SM00209; TSP1; 8.
DR SMART; SM00327; VWA; 3.
DR SUPFAM; SSF49785; SSF49785; 2.
DR SUPFAM; SSF53300; SSF53300; 3.
DR SUPFAM; SSF82895; SSF82895; 8.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS50092; TSP1; 8.
DR PROSITE; PS50234; VWFA; 3.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Membrane; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN <1..1675
FT /note="Coadhesin"
FT /id="PRO_0000429491"
FT TOPO_DOM 1..1356
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1357..1377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1378..1675
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 11..160
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 168..220
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 224..279
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 281..336
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 338..393
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 403..458
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 460..515
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 517..572
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 595..769
FT /note="VWFA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 778..958
FT /note="VWFA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 966..1141
FT /note="VWFA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT DOMAIN 1144..1198
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1192..1336
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REGION 567..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1463..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1463..1481
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 180..216
FT /evidence="ECO:0000255"
FT DISULFID 184..219
FT /evidence="ECO:0000255"
FT DISULFID 194..206
FT /evidence="ECO:0000255"
FT DISULFID 236..273
FT /evidence="ECO:0000255"
FT DISULFID 240..278
FT /evidence="ECO:0000255"
FT DISULFID 251..263
FT /evidence="ECO:0000255"
FT DISULFID 293..330
FT /evidence="ECO:0000255"
FT DISULFID 297..335
FT /evidence="ECO:0000255"
FT DISULFID 308..320
FT /evidence="ECO:0000255"
FT DISULFID 350..387
FT /evidence="ECO:0000255"
FT DISULFID 354..392
FT /evidence="ECO:0000255"
FT DISULFID 365..377
FT /evidence="ECO:0000255"
FT DISULFID 415..452
FT /evidence="ECO:0000255"
FT DISULFID 419..457
FT /evidence="ECO:0000255"
FT DISULFID 430..442
FT /evidence="ECO:0000255"
FT DISULFID 472..509
FT /evidence="ECO:0000255"
FT DISULFID 476..514
FT /evidence="ECO:0000255"
FT DISULFID 487..499
FT /evidence="ECO:0000255"
FT DISULFID 528..566
FT /evidence="ECO:0000255"
FT DISULFID 532..571
FT /evidence="ECO:0000255"
FT DISULFID 543..555
FT /evidence="ECO:0000255"
FT DISULFID 1156..1192
FT /evidence="ECO:0000255"
FT DISULFID 1160..1197
FT /evidence="ECO:0000255"
FT DISULFID 1175..1182
FT /evidence="ECO:0000255"
FT NON_TER 1
FT /evidence="ECO:0000305"
SQ SEQUENCE 1675 AA; 182850 MW; D7A30C344A1171B0 CRC64;
QGNYYSYGGT TPGTPIGCTN LITLSNVKFF ASSSSDGPDI PVLNSTDYWC SEFNWKNQSL
TVDLGFVTFF DRLLVQGEPF TSRSVSEYFV LTSIDGINYT YILGTNGQSM KFVGPLFNGD
QTRDTNLTAP VQARYVQFNP QEPMIAEDDS ICMRVGVESC QLVPAAVNGA WSHWSPYGPC
THACLGTAKR TRTCADPAPV FGGSPCEGVN EEEKICNDCV GTVNGGWSPW GLWSRCSTTC
NPGQRSRQRT CTNPSPKNGG TDCSGPSTQS EPCQVQFCPV DGGWSAWSGL SRCTRACGGG
RQYQSRTCSN PFPGHGGRDC VGVRSLSFTC NTQCCPVHGG WSPWGSFSSC TRTCGGGQKS
RTRVCNSPAP SCNGITCPGG NQDIQPCNQQ TCPTSPSTSF PINGNYSNWG QWTACSVTCG
QGTRERTRLC DNPAPAQGGS QCQGPSSELV GCTEIPCPVN GNWSSWGDWS NCSSGCGPGK
SYRYRDCDNP APANNGLNCT GPDQESKDCN STACPVDGGW SAWSSTPCSA TCGQGTLKRT
RECNNPKPQY GGASCFGNET EQEVACNKGP CPTSPPTISP PTTGSPADSN IPELDLVFAV
SATSSNRLAT YNSMRDTINR FITTYGSNKV HYSIIVYGKA VQRVISFNHT FPPSVGELQE
AISRHAPISG PTVLKNALQE TQTIFQEIPS RPNAKKVLVV FTDSNSPSDG NLVQAVRPLE
NNKILVVSVG VGDVNRTELL TISPNPLDVL SVQPTAGPGA LSKRIMDRIL RRDIPLIDIG
FALSATSSDF QDIFVKMKNV IRTIVERYGV ERVKFSLIVY GQNVTTVLGD FNRNLTQADL
VNYVNNLQRV PQNKNLDSAL LEAESLFRQR ARPNSKKVFV VLTDGVSTLS NANSLLINTA
ELRKSDVLIL SVGFGSQTNQ VGNQMNSVVF APRDYIAVPN YPAERDVVIA ETIMFKALEV
NLPLIDLTFA LSSSSILSQE TFKLMKETVQ SLVHTYGIDR IHYGVIVFGS VATRSFDFAT
NFPDQNELIR KVSQLTRSGG SPDLVAALKE ARKVFQLKEV RPYARKVLVV MIDDESSANK
NDLNEEVRAL RNRSVLVIGV GIGTQTLPKD LGIITDDKRN TLKAGINKNR DELAREIISI
ILRPSGLSKW SSWSACSKTC RYLGKAGTQI RTRDCKIPEL GCDGMRIDTV ECNKMDCEGC
GQRGPLNESA YTASSNSESP AFLAALNTSD PTAWCLINNE NGGYVQLDLG ELTRVYKVAT
KGEQQGDRWV TSYYLTLSED GETFFDYKAA QRLSGNTDST SVAFNVVNTT RPYRYVRFHP
VNFKGEPCMQ AAVFGCNEEK ILPPPETIAD QADAAKGILI VLWILAGILT FLLLMACCYY
CCWHVCCGRG KKRKGLVYRE RSIEDDGYLI NDEKRWTLGS APMTPVPRVR EDEIQEVTIE
MKEDNEQPLG VIQFGIETDE TKEKHVTAED VKSEKPKYSE EASSGTIKSG STMMRMKAND
GSDRRKRTKS EGDAIDAVDG DLDWSYLSDE QGTAFTNEAF VKSQEQFLEP PGSASFRGNK
VDMRRSLSAD ELATLDYDLF EDRQGPLHTA TLGRDGYMRM HKANQGSLPP SDGGREMGTV
DVAIGGIRVP NSPKDDPIYD TAGQEIHLAV EQAGRSVYPL EDGGYRGEEW YSRWG
