APOR_PIG
ID APOR_PIG Reviewed; 202 AA.
AC Q03472;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 96.
DE RecName: Full=Apolipoprotein R;
DE Short=Apo-R;
DE Flags: Precursor;
GN Name=APOR;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 29-47.
RC TISSUE=Liver;
RX PubMed=1463721; DOI=10.1021/bi00164a006;
RA Cooper S.T., Attie A.D.;
RT "Pig apolipoprotein R: a new member of the short consensus repeat family of
RT proteins.";
RL Biochemistry 31:12328-12336(1992).
CC -!- FUNCTION: May be a lipoprotein-borne regulator of either the
CC coagulation or the complement cascades.
CC -!- SUBUNIT: Forms high molecular weight disulfide-linked complexes.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Plasma. Found on very low-density lipoprotein
CC (VLDL), on chylomicrons, and in the D > 1.21 g/ml fraction of pig
CC plasma. Found in liver, spleen, lung, bone marrow and lymph node.
CC -!- DEVELOPMENTAL STAGE: Terminally differentiated macrophages.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L06820; AAA30994.1; -; mRNA.
DR PIR; A44247; A44247.
DR RefSeq; NP_999107.1; NM_213942.1.
DR AlphaFoldDB; Q03472; -.
DR SMR; Q03472; -.
DR STRING; 9823.ENSSSCP00000016606; -.
DR PaxDb; Q03472; -.
DR PeptideAtlas; Q03472; -.
DR GeneID; 396982; -.
DR KEGG; ssc:396982; -.
DR CTD; 722; -.
DR eggNOG; ENOG502RWWT; Eukaryota.
DR InParanoid; Q03472; -.
DR OrthoDB; 1212292at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR GO; GO:0045959; P:negative regulation of complement activation, classical pathway; IBA:GO_Central.
DR CDD; cd00033; CCP; 2.
DR InterPro; IPR040514; C4bp_oligo.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR Pfam; PF18453; C4bp_oligo; 1.
DR Pfam; PF00084; Sushi; 2.
DR SMART; SM00032; CCP; 2.
DR SUPFAM; SSF57535; SSF57535; 2.
DR PROSITE; PS50923; SUSHI; 2.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Lipid transport;
KW Reference proteome; Repeat; Secreted; Signal; Sushi; Transport.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:1463721"
FT CHAIN 29..202
FT /note="Apolipoprotein R"
FT /id="PRO_0000002063"
FT DOMAIN 29..87
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 88..145
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 30..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 59..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 89..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 116..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 151
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DISULFID 163
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT CONFLICT 44
FT /note="I -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="G -> A (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 22724 MW; EABC951B06A0D80C CRC64;
MPPNLQRIFP ALCLLGVLFL LHCTPVLCGC DNPPVVAHGH HTQIIGLFGM KKDEVVYKCD
EGYTLVGEDR LSCRSSRWSP AAPQCKALCP KPQIDRGKLS VDQDEYIESE NVIVQCGSGY
GLVGPKIITC TEDGTWHPRV PKCEWEYPED CEQVHEGKKL MQCLPNLEEI KLALELYKLS
LETKLLELQI DKEKKAKAKY SI