FREM2_LYTVA
ID FREM2_LYTVA Reviewed; 3103 AA.
AC Q9GV77; Q25429;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Extracellular matrix protein 3;
DE AltName: Full=FREM2 homolog;
DE Flags: Precursor;
GN Name=ECM3;
OS Lytechinus variegatus (Green sea urchin) (Echinus variegatus).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Temnopleuroida; Toxopneustidae; Lytechinus.
OX NCBI_TaxID=7654;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10885756; DOI=10.1006/dbio.2000.9696;
RA Hodor P.G., Illies M.R., Broadley S., Ettensohn C.A.;
RT "Cell-substrate interactions during sea urchin gastrulation: migrating
RT primary mesenchyme cells interact with and align extracellular matrix
RT fibers that contain ECM3, a molecule with NG2-like and multiple calcium-
RT binding domains.";
RL Dev. Biol. 222:181-194(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 489-1125.
RA Wessel G.M., Berg L.;
RT "A spatially restricted molecule of the extracellular matrix is contributed
RT both maternally and zygotically in the sea urchin embryo.";
RL Dev. Growth Differ. 37:517-527(1995).
CC -!- FUNCTION: Extracellular matrix protein that may serve as substrate for
CC the migratory primary mesenchyme cells (PMCs), the interaction possibly
CC providing guidance information to migrating PMCs.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10885756};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:10885756};
CC Extracellular side {ECO:0000269|PubMed:10885756}.
CC -!- TISSUE SPECIFICITY: Component of extracellular matrix fibers that
CC interact with PMC filopodia during gastrulation (at protein level).
CC {ECO:0000269|PubMed:10885756}.
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; AF287478; AAG00570.1; -; mRNA.
DR EMBL; U34202; AAA77050.2; -; mRNA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR Gene3D; 2.60.40.2030; -; 5.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR039005; CSPG_rpt.
DR InterPro; IPR045658; FRAS1-rel_N.
DR Pfam; PF03160; Calx-beta; 5.
DR Pfam; PF19309; Frem_N; 1.
DR SMART; SM00237; Calx_beta; 5.
DR SUPFAM; SSF141072; SSF141072; 5.
DR PROSITE; PS51854; CSPG; 12.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Developmental protein; Glycoprotein;
KW Membrane; Metal-binding; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..3103
FT /note="Extracellular matrix protein 3"
FT /id="PRO_0000010126"
FT TOPO_DOM 20..3047
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 3048..3068
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 3069..3103
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 289..388
FT /note="CSPG 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 411..499
FT /note="CSPG 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 520..630
FT /note="CSPG 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 656..762
FT /note="CSPG 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 784..875
FT /note="CSPG 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 901..993
FT /note="CSPG 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1022..1124
FT /note="CSPG 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1145..1238
FT /note="CSPG 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1259..1357
FT /note="CSPG 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1378..1470
FT /note="CSPG 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1490..1579
FT /note="CSPG 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT REPEAT 1613..1710
FT /note="CSPG 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01201"
FT DOMAIN 1717..1816
FT /note="Calx-beta 1"
FT DOMAIN 1829..1942
FT /note="Calx-beta 2"
FT DOMAIN 1956..2062
FT /note="Calx-beta 3"
FT DOMAIN 2077..2179
FT /note="Calx-beta 4"
FT DOMAIN 2197..2302
FT /note="Calx-beta 5"
FT REGION 2983..3013
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2985..3000
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 989
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1024
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1042
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1294
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1674
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1725
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1739
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2080
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2932
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 489..500
FT /note="TYSDNIIFRMTD -> KCKYVYEKGIPF (in Ref. 2; AAA77050)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="S -> P (in Ref. 2; AAA77050)"
FT /evidence="ECO:0000305"
FT CONFLICT 778
FT /note="L -> V (in Ref. 2; AAA77050)"
FT /evidence="ECO:0000305"
FT CONFLICT 1046
FT /note="L -> H (in Ref. 2; AAA77050)"
FT /evidence="ECO:0000305"
FT CONFLICT 1112
FT /note="M -> I (in Ref. 2; AAA77050)"
FT /evidence="ECO:0000305"
FT CONFLICT 1118..1125
FT /note="QFTFRCTD -> HSLSVVLM (in Ref. 2; AAA77050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3103 AA; 343775 MW; 79D7EBEDE1C54393 CRC64;
MASALLCFLA AILPGMIAAQ NTWVLGTSDV RTVEPVNPVG GGVSLGGIDI DSTENRIIVQ
NTGIAVPFGR EKAIDPNSEL VINVQAGDSC SIKVLPRQSD PLSQIPGRLV PPSFPCDFSP
GEVKYVHFGS RKPQTDKVKL QLRYDTATDV YIIPFTIDVR VESKQLEIVT RNVPLVVQDL
MGTSDALDAD KLEFEFDSNT EVCKVTVLSS TSGLPRYGEV MNHDEQGQMI DCNDFLELGI
QYRHTAATSS PREDYIPLVV ELQNQQGQVI KQEYFQSMVR IIDGDDNTPP SLVLSSDMMM
EVDQFVMTAI TPSILAAEDV ETPADMLIFN ITSQTLGPDD GMIVSTDDRN QPITSFTQKD
LRDLKIAYKP PPRDTDVQTI YQIELEIVDS ELATSETHSL LIVVKPKNTL APVVTTNTGL
VLFEGQSRPL LGGQNLGISD EDNLQDVIIA PINGSRYGEL RIGNQRIKQF TIADLIEGAV
TYHHYGTDTY SDNIIFRMTD GQHEVEFLFP ITIAPIDDEA PIVDVNTGVT VNENEVVAIT
NFVLSATDID SDDSEIRFVL EQPLSDMGNL FLRQVNIPED PQNWISQDNF YEREVTEFTL
EDIQNGHLFY QHGGSHNADP VFDRILFRVV DSADPQPNES PVQELLVKVM PQDLQPPEMF
GGTTLQLSVD EFQITPILKK NLRFTDMDSN DRELKYTIVS PLTDSDSNNN LPVGDIVLTD
EPNTPINMFT QAQINHMKVS YKPPSTELGI APRAITFQFV VQDTQGNMGS PHNFIILLRP
VDNQPPTITN TGVQVFERGT VIIDQTMLDA TDPDTDRNSI RVVLVQPPVF GTMNLNDIAL
EKGDEFTLGD IENSRVKYVS GDAEEQSDEI HLEITDGVHV VPIVIHINVA PIDDEAPTLD
LPPGTIGSFL EVQENSFSLI TSNILSASDP DTEDLLLTFI VDRQPNEGRI ESNGVVADVF
TQQDIVNGLV RYVHTGGEIG PSKRDDSFNL TLSDMSPDWI LGGNEITQVE VYVTVLPVDN
LAPNVTMGVQ FYVDEAGKGN INMTHLQAPD VDTEDDDILC TIVVAPSVGY LENISPAPGS
EKSRGGMPIS AFSIKDLRLN HINYVQSIHQ GMEPEEDQFT FRCTDGVNES PNFLFPINII
PVNDEEPQVY AREIIVDEGG QRIIDEPLLR AEDGDVPADE LHFFIVTPPQ HGTITYTRLE
GDIPILNFTM DQIANGNDIK YIHDDSETTE DSFTVLLTDG KYEITKEITI TILEVDDETP
RLTINDGIDI EIGESRIISN RILKATDLDS ADSNLTYTVR YAPEKGLLQR LSKFDGSVVE
NITLGMNFTQ WEVDNQRIRY VHTDGDGGRD LIKFDITDGT NPLIDRYFYV TVDHIDNVHP
SIINAGVTMQ EGSRVTLTTS IISTSDLNSP DEDLLFTITT APTKGHLEST DNPGMPINSF
TQLDLAGSKI YYVHTADDEV KMDSFQFQVT DGFNTVVRTF RISFTDVDNK EPVVRYDTIR
LQEGDNKLIT PFELGIDDRD TPANELRFTI TQLPIHGNIL RNNTALVTEF TMHDINENLI
SYQHDGSEQT ADSFSFIVTD GTHNEFYVLP DITTLTRQPQ QVPIEIVPVD NGAPQIVVNR
GAPTLDLLGT GELGFMITNK YLMSEDRDSV DNSLLYVITT QPQHGYIMNI ALGNISITNF
TQSDVNNMYI QYIVYPNVDA TSDTFFVEVR DAGGNTLPNQ PFRLNWSWIS LEKEYYEVNE
TERYLNIKLV RRGYLGETSF VGIQTADGTA IADEDFRGKS ARQVQFNPGQ TEGFWRVRIL
NDRLYEQAEV FEIILHDPVM GALEYPDRAV VTIFDAEDES GVFIDLPDNY VIEEDIGEFL
VPIRRTGDLS QELMASCSTM PGSATGSDPS PVLSFSDYIS RMEEDPDNMV AFDKGEDLAY
CRILIIDDSL YEEDETFQVK LSNPMGGRIG NPSAINVIIA GDTDDVPSFY FGEPEYKVDE
NAPFVEVTVF RTGTDVSKMA SVTVRSRASN PVSAVAGEDY AGISRNLDFA PGVNQQTVKV
YIIDDRGQPR LEGPETFELV LNMPMNGVLG APSKTVITIN DTISDLPKVE FRHPTYEVNE
NDIRITAEVV RSGDLSIESS VRCYTRQGSA QVMMDYDERP NTEASIITFL PGERSKTCTV
LLMDDNVFEP DEAFRLVLGS PRTASGVPAV VGEQNVTVVT VHDVGDAPII KFPETKFSID
EPTDLDSVVT VSIPVIRMGD NTQTSIVRVF TKDGSARSGI DYNPLSQVLE FGFNVTERVV
EIEILPDEDR NEMREAFTLH ITNDQMMIAD VQMNHAIIYI EQEGQASGVT FPSQPVVVSL
LDYDDIPNAR TNPPRGYPLI CVSPCNPKYP DFATTGPICD SEGLNDTVTQ FRWMVSAPTS
ESGVTSPLRQ TDSDTFFSST KSITLDSVYF GPGSRVQCVA RAVGSEGDAG REHPSNSIVI
STTDGMCMPR VANAIGAEPF TARMRYTGPA DPDYPNKVRL TVTMPHVDGM LPVISTRQLS
NFELALSKDG YRVGTHRCSN LLDYNEIPTD FGFITEETKN PNVVGDTYAY QYSPELRGEE
TLRFYRNLNL EACLWEFNAY YDMSELLDEC GGLVGTDGQV LDLVQSYVSM RIPLFVSFVF
HSPVATGGWK HFDQQSTLQL TFVYDTSILW QNGIGSQVTT GTQSLQGNLY PTSMRIDEDG
RLVVNFRTEA LFNGLFVQSH QSTDVVSTVN SIDHPGITYS LSLLRTEPTY AQPEQLWQFV
SDLSVSDYSG TYTIQLVPCT TLPNTVYSQP PVCNPEDIIT FELPIRFQQV SDPVPEEYSL
NTEFVLVGKE SIYLSDGSMG FGEGSDVAYN PGDTIFGRIH VDPVQNLGAG FNLDIQKVFL
CTGRDGYIPK YNPAANEYGC VADTPNLLYA FKILDRGAPD TIVREFNGLP FNATLAIDNA
ADLELVQQPG ADGFRLASDA LFEVDYGRTW YLHSIYSMRS SESSGIGKRE TEHHAISSRQ
RRQANSEALV DPAQGQGTNM KRVALQGPQD VDNNLGGTYE LAPKGTNVVM IAVVIGVILI
ILLVALVIGV VVRRRQAKQQ PVVVVNGSAK VVSNVHFDDN TEV
