MFP1_ACRMI
ID MFP1_ACRMI Reviewed; 422 AA.
AC B3EX02;
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=MAM and fibronectin type III domain-containing protein 1 {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 130-143 AND 285-294, 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: Secreted {ECO:0000305|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; JT013217; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; B3EX02; -.
DR SMR; B3EX02; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR CDD; cd00063; FN3; 2.
DR CDD; cd06263; MAM; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR000998; MAM_dom.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF00629; MAM; 1.
DR SMART; SM00060; FN3; 2.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49854; SSF49854; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50060; MAM_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Repeat; Secreted.
FT CHAIN <1..>422
FT /note="MAM and fibronectin type III domain-containing
FT protein 1"
FT /id="PRO_0000429547"
FT DOMAIN <1..75
FT /note="MAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT DOMAIN 2..74
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 196..286
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 291..386
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT NON_TER 1
FT /evidence="ECO:0000305"
FT NON_TER 422
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 47051 MW; AA36D1C215DE3F24 CRC64;
KFYYHMYGAT INRLNVFNGN CTVFTKLGHQ GNMWMYAEVT VFVQNNITFE GIRGYSYTGD
IAIDDVSLME GICAGCKENL TDSFGHLHIT YSAKFSPDCT WTIRNSSISE PVAIISIEEV
QFAYCRGYIK VFDGSGAQIF TRRGCNENHT SNTFLEITFQ ESQNVTIQVS LENNQSYARF
GYGILEGGLE SALLLPGWNA SLENKTSTSL QLRWMDISSW LRDGLRFFVV TAKSSYSNLT
VKGLFSSNTT FAEISGLDPY MAYDVSVVAV DGDGSQFKST VLQARTDEWV PSRAPSVFVT
SVTSTSVTVQ WNPLPQQYHN GRLLGYRVFI RKTANSPFPL DESNVAVYNT SWVTLNNLKP
GQPYEVNVSA FTSKGDGPRS THYIVTTAVC GKRPTHSTLN CRRHSSTHQR LALASNATDA
RW
