ID   Q6P163_HUMAN            Unreviewed;        72 AA.
AC   Q6P163;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=Apolipoprotein C-II {ECO:0000256|ARBA:ARBA00013947, ECO:0000256|RuleBase:RU368054};
DE            Short=Apo-CII {ECO:0000256|RuleBase:RU368054};
DE            Short=ApoC-II {ECO:0000256|RuleBase:RU368054};
DE   AltName: Full=Apolipoprotein C2 {ECO:0000256|ARBA:ARBA00031176, ECO:0000256|RuleBase:RU368054};
GN   Name=APOC2 {ECO:0000313|EMBL:AAH65270.1,
GN   ECO:0000313|Ensembl:ENSP00000465001.1};
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 {ECO:0000313|EMBL:AAH65270.1};
RN   [1] {ECO:0000313|EMBL:AAH65270.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin {ECO:0000313|EMBL:AAH65270.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2] {ECO:0000313|Ensembl:ENSP00000465001.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [3] {ECO:0007829|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [4] {ECO:0000313|Ensembl:ENSP00000465001.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Component of chylomicrons, very low-density lipoproteins
CC       (VLDL), low-density lipoproteins (LDL), and high-density lipoproteins
CC       (HDL) in plasma. Plays an important role in lipoprotein metabolism as
CC       an activator of lipoprotein lipase. {ECO:0000256|RuleBase:RU368054}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC       ECO:0000256|RuleBase:RU368054}.
CC   -!- PTM: Proapolipoprotein C-II is synthesized as a sialic acid containing
CC       glycoprotein which is subsequently desialylated prior to its
CC       proteolytic processing. {ECO:0000256|RuleBase:RU368054}.
CC   -!- PTM: Proapolipoprotein C-II, the major form found in plasma undergoes
CC       proteolytic cleavage of its N-terminal hexapeptide to generate
CC       apolipoprotein C-II, which occurs as the minor form in plasma.
CC       {ECO:0000256|RuleBase:RU368054}.
CC   -!- SIMILARITY: Belongs to the apolipoprotein C2 family.
CC       {ECO:0000256|ARBA:ARBA00007221, ECO:0000256|RuleBase:RU368054}.
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DR   EMBL; AC011481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC065270; AAH65270.1; -; mRNA.
DR   Antibodypedia; 31235; 176 antibodies from 22 providers.
DR   Ensembl; ENST00000585786.1; ENSP00000465001.1; ENSG00000234906.11.
DR   UCSC; uc060zuy.1; human.
DR   HGNC; HGNC:609; APOC2.
DR   VEuPathDB; HostDB:ENSG00000234906; -.
DR   GeneTree; ENSGT00390000007913; -.
DR   OMA; GTHEPQE; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; ENSG00000234906; Expressed in right lobe of liver and 97 other cell types or tissues.
DR   GO; GO:0042627; C:chylomicron; IEA:UniProtKB-UniRule.
DR   GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-UniRule.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:UniProtKB-UniRule.
DR   GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1440.10; Apolipoprotein C-II; 1.
DR   InterPro; IPR008019; Apo-CII.
DR   InterPro; IPR023121; ApoC-II_dom_sf.
DR   PANTHER; PTHR16566; APOLIPOPROTEIN C-II; 1.
DR   PANTHER; PTHR16566:SF0; APOLIPOPROTEIN C-II; 1.
DR   Pfam; PF05355; Apo-CII; 1.
PE   1: Evidence at protein level;
KW   Chylomicron {ECO:0000256|ARBA:ARBA00022513, ECO:0000256|RuleBase:RU368054};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00022981};
KW   HDL {ECO:0000256|ARBA:ARBA00022850, ECO:0000256|RuleBase:RU368054};
KW   LDL {ECO:0000256|ARBA:ARBA00022710, ECO:0000256|RuleBase:RU368054};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW   ECO:0000256|RuleBase:RU368054};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU368054};
KW   Lipid transport {ECO:0000256|ARBA:ARBA00023055,
KW   ECO:0000256|RuleBase:RU368054};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:Q6P163};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU368054};
KW   Sialic acid {ECO:0000256|ARBA:ARBA00022981};
KW   Signal {ECO:0000256|RuleBase:RU368054, ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU368054};
KW   VLDL {ECO:0000256|ARBA:ARBA00023313, ECO:0000256|RuleBase:RU368054}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..72
FT                   /note="Apolipoprotein C-II"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014310576"
SQ   SEQUENCE   72 AA;  8146 MW;  74A78BF8E68CDC26 CRC64;
     MGTRLLPALF LVLLVLGFEV QGTQQPQQDE MPSPTFLTQV KESLSSYWES AKTAAQNLYE
     KTYLPAVDEK LR
//