MFAP3_PONAB
ID MFAP3_PONAB Reviewed; 362 AA.
AC Q5R9E4;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Microfibril-associated glycoprotein 3;
DE Flags: Precursor;
GN Name=MFAP3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the elastin-associated microfibrils.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- PTM: Glycosylated. {ECO:0000305}.
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DR EMBL; CR859445; CAH91616.1; -; mRNA.
DR RefSeq; NP_001125952.1; NM_001132480.1.
DR AlphaFoldDB; Q5R9E4; -.
DR STRING; 9601.ENSPPYP00000017873; -.
DR Ensembl; ENSPPYT00000018589; ENSPPYP00000017873; ENSPPYG00000015972.
DR GeneID; 100172887; -.
DR KEGG; pon:100172887; -.
DR CTD; 4238; -.
DR eggNOG; ENOG502QW9J; Eukaryota.
DR GeneTree; ENSGT00390000011576; -.
DR HOGENOM; CLU_056017_0_0_1; -.
DR InParanoid; Q5R9E4; -.
DR OMA; KPHCCLF; -.
DR OrthoDB; 1154642at2759; -.
DR TreeFam; TF333205; -.
DR Proteomes; UP000001595; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013151; Immunoglobulin.
DR InterPro; IPR039696; MFAP3-like.
DR PANTHER; PTHR14340; PTHR14340; 1.
DR Pfam; PF00047; ig; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..362
FT /note="Microfibril-associated glycoprotein 3"
FT /id="PRO_0000014867"
FT TOPO_DOM 20..146
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 45..137
FT /note="Ig-like C2-type"
FT REGION 282..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 73..124
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 362 AA; 40106 MW; E01C8E07A3D1D142 CRC64;
MKLHCCLFTL VASIIVPAAF VLEDVDFNQM VSLEANRSSY NASFPSSFEL SASSHSDDDV
IIAKEGTSVS IECLLTASHY EDVHWHNSKG QQLDGRGRGG KWLVSDNFLN ITNVAFDDRG
LYTCFVTSPI RASYSVTLRV IFTSGDMSVY YMIVCLIAFT ITLILNVTRL CMMSSHLRKT
EKAINEFFRT EGAEKLQKAF EIAKRIPIIT SAKTLELAKV TQFKTMEFAR YIEELARSVP
LPPLILNCRA FVEEMFEAVR VDDPDDLGER IKERPALNAQ GGIYVINPEM GRSNSPGGDS
DDGSLNEQGQ EIAVQVSVHL QSETKSIDTE SQGSSHFSPP DDTGSAESNC NYKDGAYENS
QL