ID M3XSS4_MUSPF Unreviewed; 1214 AA.
AC M3XSS4;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Multimerin-1 {ECO:0000313|Ensembl:ENSMPUP00000002124.1, ECO:0000313|RefSeq:XP_004756126.1};
GN Name=MMRN1 {ECO:0000313|Ensembl:ENSMPUP00000002124.1,
GN ECO:0000313|RefSeq:XP_004756126.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000002124.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000002124.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004756126.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004756126.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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; AEYP01040711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01040712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004756126.1; XM_004756069.3.
DR STRING; 9669.ENSMPUP00000002124; -.
DR Ensembl; ENSMPUT00000002168.1; ENSMPUP00000002124.1; ENSMPUG00000002146.1.
DR GeneID; 101688764; -.
DR KEGG; mpuf:101688764; -.
DR CTD; 22915; -.
DR eggNOG; ENOG502QTYP; Eukaryota.
DR GeneTree; ENSGT01030000234633; -.
DR HOGENOM; CLU_011016_0_0_1; -.
DR OMA; NCTVKLV; -.
DR OrthoDB; 5350046at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:1990972; C:multimerin complex; IEA:Ensembl.
DR GO; GO:0031091; C:platelet alpha granule; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0061045; P:negative regulation of wound healing; IEA:Ensembl.
DR GO; GO:1901731; P:positive regulation of platelet aggregation; IEA:Ensembl.
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; 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; 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 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1214
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041158594"
FT DOMAIN 191..266
FT /note="EMI"
FT /evidence="ECO:0000259|PROSITE:PS51041"
FT DOMAIN 1027..1063
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1082..1214
FT /note="C1q"
FT /evidence="ECO:0000259|PROSITE:PS50871"
FT REGION 75..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 662..707
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 166..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1053..1062
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1214 AA; 136851 MW; EEAC30028D9CB856 CRC64;
MKRAKLFILL SSLWNGGFGL INTTHTWTTP EDASSQENIA SATVPLNKML PTPQIMSAEI
ATIPEARTFE KRLLKSTLPP SKRGTPPEGV GNQTLTPPEK TEGALKLQPL ALPTKPSLKF
SPRAESVVLS NSTMKFLQSF ARKSNQQAIS PKAVAGDLGN RSPRETYLSR GDSSGSQKTN
YQKSSFETTR GKNWCAYVHT RLSPTVILDN QVTYIPSGRG SCGWASGSCP QRSQKISNPV
YRMQHKIVTS LEWKCCPGFS GAKCQLKAQE QQHLIHSNQA ESHTAVGRET PEQPQQQDCG
DPAVTQKMTE QMNYQAMKLT LLQKKIDNIS SAVSDVRNTY SSLEGKINED KNREFQSFLK
GLKSKSINDL VKNIVREQFK IFQNDMQETI AQLFKTVSSL SEDLENTRQI IRQVNESVVL
IAVQQKSVLM QENRPTLTDV LDLKNRIVNI RQEITVTCEK PIKELEAKQA HLEGALEQEH
SRNIFYYESL NKTLSKMKEV HKQLLSMEQV SGQKGVPTAE SVHSNVTEYM SALQENIKKQ
GLMMLHMFDD LHIQDSKINN LTIALEMEKE SIRGECEDML SKCRNDFKFQ IKDTEENLQV
LNQTLAEVLF PMDNKMDKMN EQLNDLTYDM EILQPLLEQA TPFRETVVQE PPKEAIATRK
KVENLISAVN SLNILIKELS KRHNSLKNEV QSRSDALDRR INEYASEMED GLNKTMIIIN
NAIDFIQDNY MLKEALNSIK YNPEVHHQCT QNMETILTFI SQFQHLNDSI QMLVNDDQRY
NFVLQVAKVL ANMPKEENLS QSSFQKIYQM FNETTSQVIK YQQNMSHLEE KMLSATNISK
NFETRLQGIE TKVAKTLIPY YVSLKKGSVT TNERDQALQL QVLTSRFKAL EAKSIHLSVH
LTALNKTLSE VLLMCHNAST RISELNASIP KRIESSQPDL QLLQKGLTEF VESVIEIKSQ
IAISNLTWYI NQTLSGSLAN VAKSQKQIKP VLKKPSSLKK PTVNLTTVLI GRSQRNTDNL
LVPATEEYSD CSRSPCQNGG TCINGRGSSV CACRHPFTGD NCTVKLVQEN ALAPDFSKGS
YRYAPMVAFF ASHTYGMSTP GPILFNNLDV NYGSSYTPRT GKFRIPYLGV YVFKYTIESF
SAHISGFLVV DGRDKLAFES ENINGEIRCD RVLTGDALLE LNYGQEVWLR LVKGTIPAKF
PPATTFSGYL LYRT
//
