FREM3_HUMAN
ID FREM3_HUMAN Reviewed; 2139 AA.
AC P0C091;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=FRAS1-related extracellular matrix protein 3;
DE Flags: Precursor;
GN Name=FREM3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2]
RP IDENTIFICATION.
RX PubMed=15345741; DOI=10.1073/pnas.0402760101;
RA Smyth I., Du X., Taylor M.S., Justice M.J., Beutler B., Jackson I.J.;
RT "The extracellular matrix gene Frem1 is essential for the normal adhesion
RT of the embryonic epidermis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13560-13565(2004).
CC -!- FUNCTION: Extracellular matrix protein which may play a role in cell
CC adhesion. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- DOMAIN: The Calx-beta domains bind calcium with high affinity and
CC undergo a major conformational shift upon binding. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FRAS1 family. {ECO:0000305}.
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DR EMBL; AC139713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS54808.1; -.
DR RefSeq; NP_001161707.1; NM_001168235.1.
DR AlphaFoldDB; P0C091; -.
DR BioGRID; 127932; 2.
DR IntAct; P0C091; 1.
DR STRING; 9606.ENSP00000332886; -.
DR GlyGen; P0C091; 4 sites.
DR iPTMnet; P0C091; -.
DR PhosphoSitePlus; P0C091; -.
DR BioMuta; FREM3; -.
DR DMDM; 357528797; -.
DR jPOST; P0C091; -.
DR MassIVE; P0C091; -.
DR PaxDb; P0C091; -.
DR PeptideAtlas; P0C091; -.
DR PRIDE; P0C091; -.
DR ProteomicsDB; 52290; -.
DR Antibodypedia; 64705; 5 antibodies from 5 providers.
DR DNASU; 166752; -.
DR Ensembl; ENST00000329798.5; ENSP00000332886.5; ENSG00000183090.5.
DR GeneID; 166752; -.
DR KEGG; hsa:166752; -.
DR MANE-Select; ENST00000329798.5; ENSP00000332886.5; NM_001168235.2; NP_001161707.1.
DR UCSC; uc021xsj.2; human.
DR CTD; 166752; -.
DR DisGeNET; 166752; -.
DR GeneCards; FREM3; -.
DR HGNC; HGNC:25172; FREM3.
DR HPA; ENSG00000183090; Tissue enhanced (brain).
DR MIM; 608946; gene.
DR neXtProt; NX_P0C091; -.
DR OpenTargets; ENSG00000183090; -.
DR VEuPathDB; HostDB:ENSG00000183090; -.
DR eggNOG; KOG1306; Eukaryota.
DR eggNOG; KOG3597; Eukaryota.
DR GeneTree; ENSGT00940000162501; -.
DR HOGENOM; CLU_001041_1_0_1; -.
DR InParanoid; P0C091; -.
DR OMA; CYTHTGQ; -.
DR OrthoDB; 13258at2759; -.
DR PhylomeDB; P0C091; -.
DR TreeFam; TF316876; -.
DR PathwayCommons; P0C091; -.
DR SignaLink; P0C091; -.
DR BioGRID-ORCS; 166752; 13 hits in 1072 CRISPR screens.
DR GenomeRNAi; 166752; -.
DR Pharos; P0C091; Tdark.
DR PRO; PR:P0C091; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P0C091; protein.
DR Bgee; ENSG00000183090; Expressed in middle temporal gyrus and 83 other tissues.
DR Genevisible; P0C091; HS.
DR GO; GO:0005604; C:basement membrane; ISS:BHF-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; NAS:BHF-UCL.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR Gene3D; 2.60.40.2030; -; 3.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR039005; CSPG_rpt.
DR InterPro; IPR045658; FRAS1-rel_N.
DR InterPro; IPR032833; FREM3.
DR PANTHER; PTHR45739:SF5; PTHR45739:SF5; 1.
DR Pfam; PF03160; Calx-beta; 3.
DR Pfam; PF19309; Frem_N; 1.
DR SMART; SM00237; Calx_beta; 3.
DR SUPFAM; SSF141072; SSF141072; 3.
DR PROSITE; PS51854; CSPG; 12.
PE 3: Inferred from homology;
KW Calcium; Cell adhesion; Extracellular matrix; Glycoprotein; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..2139
FT /note="FRAS1-related extracellular matrix protein 3"
FT /id="PRO_0000010127"
FT REPEAT 306..409
FT /note="CSPG 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 432..522
FT /note="CSPG 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 543..677
FT /note="CSPG 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 702..807
FT /note="CSPG 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 828..920
FT /note="CSPG 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 948..1040
FT /note="CSPG 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1069..1171
FT /note="CSPG 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1192..1285
FT /note="CSPG 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1306..1404
FT /note="CSPG 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1425..1516
FT /note="CSPG 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1536..1625
FT /note="CSPG 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1659..1756
FT /note="CSPG 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT DOMAIN 1764..1862
FT /note="Calx-beta 1"
FT DOMAIN 1875..1985
FT /note="Calx-beta 2"
FT DOMAIN 2000..2106
FT /note="Calx-beta 3"
FT CARBOHYD 846
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1374
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 412
FT /note="D -> N (in dbSNP:rs4478130)"
FT /id="VAR_055819"
FT VARIANT 417
FT /note="D -> N (in dbSNP:rs184496)"
FT /id="VAR_059291"
SQ SEQUENCE 2139 AA; 238179 MW; 0F086CB8AFB64E9C CRC64;
MAGASRHPTG TPRQLLVALA CLLLSRPALQ GRASSLGTEP DPALYLPARG ALDGTRPDGP
SVLIANPGLR VPLGRSLWLD PLRDLVIGVQ PGDRCEVTVL DALPRLKGAL SPRRFPCTFG
PRQVQYTHFG SHSPGRARVL LQLRYDAPTH TLVLPFTLAV DLVFSQLELV TRNRPLVVEK
LRSWSRAIDR RVLDFASLKS GATATRRCRL TPLPHEDGPL PKYGRLVDAV GAPLPRGKGV
DCEAFLRAGV RYQHTATSSP NRDYVPMMVE LLGPEGQDAG SAGVLVREHF QLLVRIRGGA
ENTPPRPSFM ATMMMEVDPL VLTALTPDAL AAEDVESDPG DLVFNILNAP THPPGHPGQQ
GYVVSTDDPL GLPVSFFTQQ ELRELKIAYQ PPAENSHGER LFQLELEVVD GDGAASDPFA
FMVTVKSMNT LVPVASHNRG LVLFEGQSRP LSSTHSIPIS DKDNLEEVKM AAVRGLRHGQ
LVVFGAPAGC KYFTPADLAA GRVVYQHDGS NTYSDNIIFR MEDGHHQVDF LFPLTILPVD
DEPPMVNTNT GLSLTEGQVV QISPFVLSAT DIDSEDSTIH FVLENQPLKG NEEEPQWELA
PGSSHSGHYL GDLLLQQAEL PLSTEDEDWH YMEKEGLYEK VVTEWLQRDI MEGRLFYRHL
GPHSPQSVMV QLAFHVQDDH DPPNLSKQHI FTIKVQPVDI LSPQLYPGTT LEMTVQEYQL
THFQKNFLRY IDQDSDDQNL WYTLLTLPTD TDGNHQVRAG EIVLTDSPDT LIMHFTQAQV
NQHKVAYQPP QKLGIAPRVV QFTYQVEDAA GNSVPGTFTL FLQPVDNQPP EVTNRGFAIL
EGGSFNLSSN ELHVTDPDTD IDQIVFILVR GPQHGHLQYF KRCMVPGESF MQADVINGSV
SYQHGRDQTT TSDTFHLEVS DGVHHIPITI PISVHPNVAN RSPRISLRSS SLLDVSIDVL
ENKATEITMG VIHGKRKDVG DLMLSFIVKD SPKLGTILVN GLPTERFTQE DLINGRVAYA
HTAGEVGFQK QHDAFSLILS KDSYQWVVGN SIIEKVQVQV TVLPVDNVGP KVFVGESFIV
YEGEKNSLTL QHLHVEDVDT HQDELLCTVT SQPASGYLEK IASAPGSKMS QSGSPISAFS
LRDIQVRHIN YVQSIHKGVE PQEDQFTFYC SDGINFSPNV FFPIIILPTN DEQPKLFAHE
FKVLEGMSLV IDTQLLNGAD ADLPPNELHF QLTALPRHGR IIQQLATGSQ PIHSFTLKEI
QEASTIVYEH DDSETKEDSF EVWLSDGKHT THRKVPIVVT LVDDETPHLT VNNGLKVEKG
HSEIITNRIL KATDLDSDDK SLSFVLHSGP QQGLLQRLRK PRGEVRNNLT LGMNFTQDEI
NRGLICYIHT GQEGIVDIIK FDVTDGVNTL TDHYFYVTIG NLDSVFPEVI SKRITLIEGA
RVTLTNNLLT NSDINSSDEH HFSITRAPSL GHLESSDYAG EPIASFTQLQ LASNKISYVH
TSNDEKKMDS FEFQVIGELY PVFRTFRIFI TDVDNKKPIL TIHRLTLQKE DSQLITLLEL
TVEDSDTPDD LILFTITQVP MHGKILYNGS RPVTTFTKQD LNKNLISYKH DGSETTEDSF
SLTVTDGTHT DFYVLPDTAL ATHKPQVMRV QIRSLDNRLP QITTNRGAPA LKRLHTGHMG
FLITSKSLKA EDQDSPHRLL KYKVTRGPEH GFIIKTGLGN QSTRVFTQAD IDEMKISYVL
NEGSNASKDI FYFSVEDNGG NKLTNQPFHL NWAWICLEKE YYIVDEDSTF LEVTLTRRGY
LGETSFISIG TKDETAKKDK DFKWKTNKQI QFNPGQTTAT WRVRIIPDNE YETSETFQII
LSEPLMAVLE FPEMATVEIV DPGDESTVYI PEAEYKIEED IGELLIPVRR SGDASQELIV
ICSTRQGSAT GTISSTVLFS DYISRPEDHT SILHFDKNET QKTCQVLIID DSLYEEEESF
SVSLRLPVGG QLGARFPTTK VTILADRYDE PVLHFGDAEY HVNESARYVE VCVWRRGTDL
SQPSSIAVRS RKSEQESAEA GTDYVGISRN LDFAPGVRMQ TFQVTILDDL GQPTLEGPEK
FELLLQMPMG AVLGEPNKTT IFIEDTITDC KQSACSSFD
