FREM3_MOUSE
ID FREM3_MOUSE Reviewed; 2123 AA.
AC Q5H8B9;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=FRAS1-related extracellular matrix protein 3;
DE AltName: Full=NV domain-containing protein 2;
DE Flags: Precursor;
GN Name=Frem3; Synonyms=Gm795, Nv2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-271.
RX PubMed=15878328; DOI=10.1016/j.yexcr.2005.01.020;
RA Kiyozumi D., Osada A., Sugimoto N., Weber C.N., Ono Y., Imai T., Okada A.,
RA Sekiguchi K.;
RT "Identification of a novel cell-adhesive protein spatiotemporally expressed
RT in the basement membrane of mouse developing hair follicle.";
RL Exp. Cell Res. 306:9-23(2005).
RN [3]
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; AC130675; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC132606; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB160989; BAD89017.1; -; mRNA.
DR AlphaFoldDB; Q5H8B9; -.
DR STRING; 10090.ENSMUSP00000038015; -.
DR GlyGen; Q5H8B9; 5 sites.
DR iPTMnet; Q5H8B9; -.
DR PhosphoSitePlus; Q5H8B9; -.
DR PaxDb; Q5H8B9; -.
DR PRIDE; Q5H8B9; -.
DR ProteomicsDB; 267625; -.
DR MGI; MGI:2685641; Frem3.
DR eggNOG; KOG1306; Eukaryota.
DR eggNOG; KOG3597; Eukaryota.
DR InParanoid; Q5H8B9; -.
DR PRO; PR:Q5H8B9; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q5H8B9; protein.
DR GO; GO:0005604; C:basement membrane; IDA:BHF-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Extracellular matrix; Glycoprotein; Metal-binding;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..2123
FT /note="FRAS1-related extracellular matrix protein 3"
FT /id="PRO_0000010128"
FT REPEAT 298..399
FT /note="CSPG 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 424..514
FT /note="CSPG 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 535..668
FT /note="CSPG 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 693..799
FT /note="CSPG 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 820..911
FT /note="CSPG 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 939..1030
FT /note="CSPG 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1059..1161
FT /note="CSPG 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1182..1274
FT /note="CSPG 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1295..1394
FT /note="CSPG 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1413..1505
FT /note="CSPG 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1525..1613
FT /note="CSPG 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1647..1745
FT /note="CSPG 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT DOMAIN 1752..1850
FT /note="Calx-beta 1"
FT DOMAIN 1863..1974
FT /note="Calx-beta 2"
FT DOMAIN 1989..2095
FT /note="Calx-beta 3"
FT REGION 582..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 845
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1577
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 2123 AA; 234999 MW; 3D1953C3785D1111 CRC64;
MAGDSLSLPG MSLQLLVTLT CLLLTCALRE RVPLSENVSH CELYLPPWGA LNGGSHQNPG
ILIANSGFQV PQGRSVWLNP LRDLVIRVQR GDQCKVTVLD FPRLQGALSP HQFPCDFGAQ
QVKYTHFGSP SSTRTRIQLQ VRYDAGNSTL VLPFTLQVNV VFPKLQLVAR NRPLKVFKVL
GCSHAIDRRV LNFASRSRCR LTVLPHPGGP LPKYGLLVDT AGNPLSRGHL ADCEAFIQAG
VRYQHTTTPS SPSRDYVPML VELLGPESQG TRSVEVLAQE YFQIQVRIQK RARSTAPIPS
LAALMIVEVE QSLLTALTPD VLAAEDSESD PDDLVFNILN VPEAPPGHHG GQGYVVNTDD
PLGLPVSFFT QKELRELKIA YRPPTGSSEG DHVFQLKLQV VDEDGDTSEP FAFMVVVKSM
NVLAPIASYR GGLVVFEGQA RPLSDALSFQ VSDKDNSKEI KIVAVRGLQH GQLVVHGAPA
GCKNFTLADL SAGRVVYQHD GSDSYSDNII LKMEGEHHRV DFLFPITIVP VDDAAPVLTA
NMGLSVTEGQ VVQISPFVLC ATDIDSEDSA ILFVLEDEHL EGKEEETHED LAPGSYSSSQ
HPGNMLLRQA EPPSSLLYSD WHYVEKEGLY ETVVTEWLQR DIMEGRLFFS HPGPHSPSPV
AHLAFHVQDD QDPPNLSNQH FFTISIQPAD TSQPQLSPET TLEMTVQGYQ LTPFQQKYLQ
YTDQNSDEQN LWYTLLTRPT DADSNHQVQA GEIVLTDSPG RPIVHFTQTQ VNHQKIAYRP
PQRNLGIVPR VVQFTYKVED TAGNSVSGTF TVFLQPLNNQ PPKVINRGFA VLEGDSFILG
RGELNVSDPD TNDDQIFFIL VWGPQHGHLQ YFKKYMVPGE SFMLADVING SISYQNSRDQ
TDSDVIYLEV SDGVHHIPIT VQVSVQPTVA DRSPGISITG TPVLATSLTV LENAASEITM
DVTHGRKNTN DLMLSFIVED KPKLGMILVN GWPAEQVTQE DLLGGAVSYV HTSGEIGFQR
VHDTFSFILS KDAYHRAMRD NILERVLVEV TVLPVDNMAP KVLVRKPFIV YEGGKNLLTP
QHVNIEDVDT SKDEILCTLT VQPSSGYLEN LAPAPGSEVS RAGNPISAFF VKDVRVGCIN
YVQSIHKGIE PGADQFTFYC SDGINFSPKV LLPLTILPTN DEQPQLFTRE FVVLEGMSRV
IDTSLVNGVD ADFPSDKHFR LTVFPQHGQI TQQLATGSKP IHSFTLQEIQ EPSSIAYEHD
DSESTEDSFE VWLSDGRHTT HTTVPIAVIL VDDEVPQLTI NDGLEIETGH SEIITNHILK
AIDLDSDNKS LSFVLHSEPQ QGLLQRLRKP GGDAKHNLTV GMNFTQDEID RGLIHYIHTG
QGEAVDLKFD VTDGVNTLRD RYFYITIDNS NSAVPEIVSK RVTLTEGNRM TLTTELLNTS
DIHSPGEQLL YSITRAPSTG HLESSDQPGE PMASFTQLQL ARNKISYVHI SNDKIKLDHF
ELRVTGGHHS ESRIFRIFVT EQDNKKPTLT IQALALQRGD NIVVTPSQLT VEDEDTPADF
ILFTITQIPI HGRILYNGSR PVTTFTKKDL TKSLIYCHDG SETSKDSFSF TVTDGIHTGF
YVFPDTSLET HVPQTVWIQI SPFDDRLPQM GINRGATALK LLHTGHLGFL ITNEYLQATH
QGVPHRLLTY KVTRGPEHGY IVNAGLGNEN THMFTQADID EMRVYYILNK GRGRATRDTF
YFSVETRGGK QLRNQPFHLN WAWISLEKEY YIVDEDSPFF EVTLRRGYLG GTSVVSIGTK
GDTAEENKDF KGKAPMLVQF SPGQSTATWR VGLIPDTKYE TSETFQIILS EPGAAALEFP
EMATVEIVDP EDESTVYIPE AEYQLAEAVG EFLVPVRRSG DTSQELTVIC STRPGSATGT
IPSVQLSLSD YVSRPEDNTS MLHFEKDESE KTCQVLIIND SLYEEEESFS IALSLPTGGQ
LGAKFPTARV TILADREDEP ALHFECSEYH AEESAGYVEV AVWRRGTGLS QASSVIVRSR
GTEEQAAEAG TDYIGVRQHL HFSPGVSVQR LRVTILDDLP QPAFEGPEMF ELLLQMPTGA
VIGEPNKTTV TINDSVTNCE ECV
