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Database: UniProt
Entry: U3EIW3_CALJA
LinkDB: U3EIW3_CALJA
Original site: U3EIW3_CALJA 
ID   U3EIW3_CALJA            Unreviewed;      1229 AA.
AC   U3EIW3;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Multimerin-1 {ECO:0000313|EMBL:JAB21875.1};
GN   Name=MMRN1 {ECO:0000313|EMBL:JAB21875.1};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB21875.1};
RN   [1] {ECO:0000313|EMBL:JAB21875.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Hippocampus {ECO:0000313|EMBL:JAB21875.1};
RX   PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA   Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA   Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT   "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT   sequences.";
RL   Gigascience 3:14-14(2014).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; GAMS01001261; JAB21875.1; -; mRNA.
DR   AlphaFoldDB; U3EIW3; -.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR   CDD; cd00054; EGF_CA; 1.
DR   Gene3D; 2.60.120.40; -; 1.
DR   Gene3D; 2.10.25.10; Laminin; 1.
DR   InterPro; IPR001073; C1q_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR011489; EMI_domain.
DR   InterPro; IPR008983; Tumour_necrosis_fac-like_dom.
DR   PANTHER; PTHR15427; EMILIN ELASTIN MICROFIBRIL INTERFACE-LOCATED PROTEIN ELASTIN MICROFIBRIL INTERFACER; 1.
DR   PANTHER; PTHR15427:SF3; MULTIMERIN-1; 1.
DR   Pfam; PF00386; C1q; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF07546; EMI; 1.
DR   PRINTS; PR00007; COMPLEMNTC1Q.
DR   SMART; SM00110; C1Q; 1.
DR   SMART; SM00181; EGF; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF49842; TNF-like; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS50871; C1Q; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS51041; EMI; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1229
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004640344"
FT   DOMAIN          207..282
FT                   /note="EMI"
FT                   /evidence="ECO:0000259|PROSITE:PS51041"
FT   DOMAIN          1042..1078
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1097..1229
FT                   /note="C1q"
FT                   /evidence="ECO:0000259|PROSITE:PS50871"
FT   REGION          69..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..201
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        1068..1077
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   1229 AA;  138487 MW;  4D5A1C9A9C243723 CRC64;
     MKGARLFVLL SSLWSGGIGL NNSKHSWTIL DDGNSQKTTT SASVPSNKIQ RLQILPTTQV
     MSAEIVTTPE ARTSEESLLK STLPPSETSA PAEGVRNQTL TSTEKAEEAV KFQNLTLPTK
     SSTKFNPGAE SAVLSNSTLN FLQSFAGKSN EQATSLQAVG GDGGSGGVGG SGGTGNRGPR
     ETYLSRGDSS PSRRTDYQKS SFETTRGKNW CAYVHTRLSP TVILDNQVSY VPGGRGPCGW
     TSGSCPQRSQ RISNPIYRMQ HKIVTSLDWR CCPGYSGPKC QLKAQEQQHL IHTNQAESHT
     AIGKGVAEQQ QQQDCGDPEV MQKMTDQMNY QAMKLTLLQK KIDNISLTVN DVRNIYSSLE
     EKVSEDKGRE FQSFLKGLES KSINVLIRDI VKEQFNILQN DMQETVAQLF KTVSSISEDL
     ESTRQIIQRV NESVVSVAAQ QKFVLMKENR PTLTDVVDLR NHIVNVRQEM TLTCEKPIKE
     LEVKQAHLEG ALEQEHSRSI QYYESLNKTL SEMKEIHEQL LPTEKVSDQK NVPAAESVSN
     NVTEYMSTLH ENIKKQSLMM LQMFDDLHIQ ESKINNLTIS LEMEKESLRG ECKDMLSKCR
     NDFKFQLKDT EESLHVLNQT LAEVIFPMDN KMDKMSEQLN DLTYDMEILQ PLLEQGASLR
     QTVIHEQPKE AVMTRKKIEN LTSAVNSLNF IIKELTKRHN LLRNEVQSRD DALERRISEY
     ALEMEDGLNK TMTIVNNAID FIQDNYVLKE TLSTIKDNYE IHHKCPSNME TILTFIPQFQ
     RLNDSIQILV NDNQRYNLVL QVAKTLAGFP RDEKLNQSNF QKMYQMFNET TSQMRKYQQT
     VSHLEEKILS AIKISKTFET RLQDVESKVT QTLIPYYISL NKGSAVTNER DRVLQLQVLN
     SRFKALEVKS IHLSINFSLL NKTLHEVLTM CHNASTSVSE LNATIPKWIK RYMPDIQLLQ
     KGLTEFVESI IEIKTQAVLS NLTCCLDQSL PGSLANAKSQ KQAKSLLKKI NTLKKPTVNL
     TTVLIGRTQR NTDNIIYPVT EEYSSCSRHP CQNGGTCING RTSFTCACRH PFTGDNCTIK
     LVEENALAPD FSKGSYRYAP MVAFFASHTY GMTTPGPILF NNLDVNYGAS YTPRTGKFRI
     PYLGVYVFKY TIESFSAHIS GFLVVDGIDK LAFESENIDS EIHCDRVLTG DALLELNYGQ
     EVWLRLAKGT IPAKFPPVTT FSGYLLYRT
//
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