FP_ACRMI
ID FP_ACRMI Reviewed; 1280 AA.
AC B8VIW9;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 25-MAY-2022, entry version 22.
DE RecName: Full=Fibronectin type III domain-containing protein;
DE AltName: Full=Neuroglian-like protein {ECO:0000303|PubMed:23765379};
DE Flags: Precursor;
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 148-161; 288-304; 433-443 AND 693-704, 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; JR993827; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; B8VIW9; -.
DR SMR; B8VIW9; -.
DR PRIDE; B8VIW9; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 2.60.40.10; -; 9.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR026966; Neurofascin/L1/NrCAM_C.
DR Pfam; PF13882; Bravo_FIGEY; 1.
DR Pfam; PF00041; fn3; 3.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00409; IG; 6.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 5.
DR SUPFAM; SSF49265; SSF49265; 3.
DR PROSITE; PS50853; FN3; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Membrane; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1280
FT /note="Fibronectin type III domain-containing protein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000429543"
FT TOPO_DOM 20..1156
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1157..1177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1178..1280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 628..722
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 730..824
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 830..933
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 939..1033
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1039..1131
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1118..1144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1206..1280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 58..111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 268..321
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 369..417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 460..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 553..604
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 1280 AA; 142532 MW; 1DDB58DA38ACC460 CRC64;
MWQILLAISI FSLSKLSNAQ QQPKVAPPQI TNFLAEDKVA PEEVKFRDTD VWQLVLPCRA
TGSNPLKWVW KHNNAEINKN KFIFDRDWEL LSDGTLRARG LNISDRGTYQ CFVEDTVTKV
STFSRKLRVE VTAVGDFKSH KDFTSSVKLG EPLNVECPPR GPSFGVTFAW TSKKARSIQF
PISNRVAIDP STGNLHIMYI TEEDVSTFND LEGIRCTISA ANTFYSSGAL TLQIIPGKEI
KLSSPSFTSS TSSPNENAVE GRRKDLYCEA TARPPPKLVW KKNGVELKSG IDFIEIPEAF
EGRLLSITSV KESLHETTFT CEASNNQTIA SGPAQQNFVL NVEVAPRWAS KPPDSLKEIP
ISSNGNLSCD VYAQPEPEIK WYRDGREITQ SSSKVEVSGS KLLFKDTTLD EAGIYQCSAE
NVHGMIVSST YVKVLAIAPS FKNGFGPFYL FQDSEGRLKC DPEAAPRPST FKWFDENGAE
IKSGNGYTIE EDGTLVITKV ERSQHAGKFS CYAKNFLGNA TAEGTATVYD RTRIVRGPSD
LSVNEGTRVD LRCEAVADSS LELHYTWKRD DATIEYNRRV QWLKDQNVLT IADLTVEDAG
IYTCVAYTPQ PKYSEAKASA IVNIAGAPFP PTNLMLSSEC QNRNTTLSWV TGESNNASIL
YFLIERKSQY ADDFWQVIAN VTNPNATSHP LVKLAGNADL AFRIRAVNRF GPSRPSEPTG
SFCRTIRAVP EKWPDNFRGV PGKAEELTIA WTAMRRVEWN GPGLYYKLWY RRVNSGDALV
EVRREASSDS FVVPDAGYYR QWEFQIQAIN EVGEGPKSPL VKQFSGQDPP TGKPEDVTVG
TITARSVELS WKKVTFTRGS VDGYRIYFWG ESRVSAKRRR RAIPGYASVT NVTGVNTERY
TVTGLKPYTN YKFVITAYNS GGNGPESDQV AADTDEAEPG PPSDVQVFVF AKYILVTWQP
PSEPNGVITN YRVGTETYTG SQPTDVTVNM EETGVEARRK LLRDLVPETN YVVEMQAATS
KGWGTSFRKT EKTVAWAAPA KPEKPIVEGT AVDEVRVDYK FGLGGGYTHD FLVMFRKKIE
GQEFQNTSWV DHFQQQSIII GNLDPELYQF KTVARNDYPS QENPQESPAS DITEARPRPG
ISNVGKRVST PIYQSAWFIA LLVLIALLLL VLLTFVLYTR HQGAKYLVGK REKKRAAALI
DREHFDEEEG SFSNNGRADH PPPYPSQGSL PRGADSDRDS LDDYGEGPQF NEDGSFIEEY
GDEKKAPPEE KDPSSLATFV
