ID A0A340WKI1_LIPVE Unreviewed; 1215 AA.
AC A0A340WKI1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Multimerin-1 {ECO:0000313|RefSeq:XP_007450078.1};
GN Name=MMRN1 {ECO:0000313|RefSeq:XP_007450078.1};
OS Lipotes vexillifer (Yangtze river dolphin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Lipotidae; Lipotes.
OX NCBI_TaxID=118797 {ECO:0000313|Proteomes:UP000265300, ECO:0000313|RefSeq:XP_007450078.1};
RN [1] {ECO:0000313|RefSeq:XP_007450078.1}
RP IDENTIFICATION.
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 RefSeq; XP_007450078.1; XM_007450016.1.
DR AlphaFoldDB; A0A340WKI1; -.
DR STRING; 118797.A0A340WKI1; -.
DR GeneID; 103076612; -.
DR KEGG; lve:103076612; -.
DR CTD; 22915; -.
DR InParanoid; A0A340WKI1; -.
DR OrthoDB; 5350046at2759; -.
DR Proteomes; UP000265300; Unplaced.
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 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:UP000265300};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1215
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016246980"
FT DOMAIN 195..270
FT /note="EMI"
FT /evidence="ECO:0000259|PROSITE:PS51041"
FT DOMAIN 1028..1064
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1083..1215
FT /note="C1q"
FT /evidence="ECO:0000259|PROSITE:PS50871"
FT REGION 68..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 665..692
FT /evidence="ECO:0000256|SAM:Coils"
FT DISULFID 1054..1063
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1215 AA; 136687 MW; 47DFA27E7C71D230 CRC64;
MKGARLFILL SSLWSGGIGR NNTTHTWTTP EDENSWNSQT SAPVPLSKIQ SLQVLPTTQI
TSVEMATAPE ASTSEESLLK STLLPSETSA SPERVRNQTL TPTGKTEVVL KLQTPALPTK
SSIRFSPKAE SVVLSNSTLK FLQSFARKSN EQAISLNSVR GVGNRSPREA YLSGGDSPGS
QRTSYQKSSF ETTRGKNWCA YVHTRLSPTV ILDNQVTYVP TGRGPCGWTS GSCPQRSQKI
SNPVYRMQHK IVTSLEWKCC PGFSGPKCQL EAQEQQQLIH SKQAESHAAG GRGTPEQQQQ
DCGDPAVTQK MTDQMNYQAT KLTLLQKKMD NISLAVSDIK NTYSSLEGKV NEDKGREFQS
FLKGLKSKSI NDLVKDIVRE QFKIFQNDMQ ETIVQLFKTV STLSEDLKNA RQIIQQVNET
VVSVAVQQKS VLMQENRPTS TDILDLKNRI VNVRQEMTFT CEKPIKELEA KQTHLEGALE
QERSRSILYH ESLNKTLSKM KDVQEHLLST EQVSNQKSVP AAGSVSNNVT EYMSTLHETV
KKQGLMLLHM FDDLHTQDSK INNLTLALET EKESVREECE HMLSKCRDDF KFQIKDTEEN
LQVLNQTLVE VLFPMDNKMD KMNEQLNDLT YDMEILQPLL EQGASFRETM SYEQPKEAVA
TKKKVENLIT AVSSLNSLIK ELTKRYNLLR NEVQSRGDSL DRRINEHALE MEDGLNKTIT
IINNAIDFIQ DNYMLKETSD TTKYNPEVHH KCTQNMETIL TFISQFQRLN DSIEILVSDS
QRYNFVLQVA KALAYIPKDE KLSLSNFQKI SQMINETSSQ LIKYQQNMSH LEEKILSATK
ISKNFETRLQ GIESNVTKTL IPYYVSLKKR FVATNERDQA LQLQVLNSRF KALEAKSIHL
SINLSLLNKT LYEALTICHD ASTSISELNA TIPKRIKGSI PDIQPLQKGL TEFVESVIEI
KTQIALSNLT RYINQSLSGS LENIVKSQKQ IKPLLKKPNT LKKPTVNLTT VLMGRTQRNT
DSILLPEEYS DCSRSPCQNG GTCINGRPGF ICACRHPFTG DNCTVKVVEE NALAPDFSKG
SYRYAPMVAF FASHTYGMTT PGPILFNNLD VNYGASYTPR TGKFRIPYLG VYVFKYTIES
FSAHISGFLV VDGVDKLAFE SESINSEICC DRVLTGDALL ELNYGQEVWL HLVKGTIPAK
FPPATTFSGY LLYRT
//
