LPAL2_HUMAN
ID LPAL2_HUMAN Reviewed; 132 AA.
AC Q16609; E1P5B4;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Putative apolipoprotein(a)-like protein 2;
DE Short=Apo(a)-like protein 2;
DE Short=Lp(a)-liker protein 2;
DE AltName: Full=Apolipoprotein a-related gene C protein;
DE Short=Apo(a)rg-C;
DE Flags: Precursor;
GN Name=LPAL2; Synonyms=APOARGC;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=7749817; DOI=10.1161/01.atv.15.1.65;
RA Byrne C.D., Schwartz K., Lawn R.M.;
RT "Loss of a splice donor site at a 'skipped exon' in a gene homologous to
RT apolipoprotein(a) leads to an mRNA encoding a protein consisting of a
RT single kringle domain.";
RL Arterioscler. Thromb. Vasc. Biol. 15:65-70(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION.
RX PubMed=8148351; DOI=10.1161/01.atv.14.4.534;
RA Byrne C.D., Schwartz K., Meer K., Cheng J.F., Lawn R.M.;
RT "The human apolipoprotein(a)/plasminogen gene cluster contains a novel
RT homologue transcribed in liver.";
RL Arterioscler. Thromb. 14:534-541(1994).
CC -!- INTERACTION:
CC Q16609; P55212: CASP6; NbExp=3; IntAct=EBI-10238012, EBI-718729;
CC Q16609; P06307: CCK; NbExp=3; IntAct=EBI-10238012, EBI-6624398;
CC Q16609; O94985-2: CLSTN1; NbExp=3; IntAct=EBI-10238012, EBI-16041593;
CC Q16609; O00291: HIP1; NbExp=3; IntAct=EBI-10238012, EBI-473886;
CC Q16609; P62826: RAN; NbExp=3; IntAct=EBI-10238012, EBI-286642;
CC Q16609; Q08AM6: VAC14; NbExp=3; IntAct=EBI-10238012, EBI-2107455;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in liver but not in other tissues tested.
CC {ECO:0000269|PubMed:7749817}.
CC -!- DOMAIN: The signal sequence and the kringle domain are highly similar
CC to the apolipoprotein(a) precursor protein. This protein is however
CC much shorter and does not contain any peptidase region.
CC -!- CAUTION: Could be the product of a pseudogene. {ECO:0000305}.
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DR EMBL; U19517; AAA85692.1; -; mRNA.
DR EMBL; U19518; AAA85693.1; -; mRNA.
DR EMBL; CH471051; EAW47597.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW47598.1; -; Genomic_DNA.
DR AlphaFoldDB; Q16609; -.
DR SMR; Q16609; -.
DR IntAct; Q16609; 6.
DR GlyGen; Q16609; 1 site.
DR BioMuta; HGNC:21210; -.
DR DMDM; 74739884; -.
DR MassIVE; Q16609; -.
DR PeptideAtlas; Q16609; -.
DR PRIDE; Q16609; -.
DR GeneCards; LPAL2; -.
DR HGNC; HGNC:21210; LPAL2.
DR MIM; 611682; gene.
DR neXtProt; NX_Q16609; -.
DR InParanoid; Q16609; -.
DR PhylomeDB; Q16609; -.
DR PathwayCommons; Q16609; -.
DR SignaLink; Q16609; -.
DR Pharos; Q16609; Tdark.
DR PRO; PR:Q16609; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q16609; protein.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00108; KR; 1.
DR Gene3D; 2.40.20.10; -; 1.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR Pfam; PF00051; Kringle; 1.
DR SMART; SM00130; KR; 1.
DR SUPFAM; SSF57440; SSF57440; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
PE 5: Uncertain;
KW Disulfide bond; Glycoprotein; Kringle; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..132
FT /note="Putative apolipoprotein(a)-like protein 2"
FT /id="PRO_0000317566"
FT DOMAIN 27..105
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..105
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DISULFID 49..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DISULFID 77..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT VARIANT 91
FT /note="T -> M (in dbSNP:rs7749199)"
FT /id="VAR_051100"
SQ SEQUENCE 132 AA; 14886 MW; 3794AD30A586DBBA CRC64;
MEHKEVVLLL LLFLKSAPTE TGPSVQECYH SNGQSYRGTY FTTVTGRTCQ AWSSMTPHQH
SRTPEKYPND GLISNYCRNP DCSAGPWCYT TDPNVRWEYC NLTRCSDDEG TVFVPLTVIP
VPSLEDSFIQ VA
