ID IPSP_HUMAN Reviewed; 406 AA. AC P05154; Q07616; Q9UG30; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 2. DT 20-JAN-2009, entry version 113. DE RecName: Full=Plasma serine protease inhibitor; DE AltName: Full=Serpin A5; DE AltName: Full=Protein C inhibitor; DE Short=PCI; DE AltName: Full=Plasminogen activator inhibitor 3; DE Short=PAI-3; DE Short=PAI3; DE AltName: Full=Acrosomal serine protease inhibitor; DE Flags: Precursor; GN Name=SERPINA5; Synonyms=PCI, PLANH3, PROCI; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=87109153; PubMed=3027058; RA Suzuki K., Deyashiki Y., Nishioka J., Kurachi K., Akira M., RA Yamamoto S., Hashimoto S.; RT "Characterization of a cDNA for human protein C inhibitor. A new RT member of the plasma serine protease inhibitor superfamily."; RL J. Biol. Chem. 262:611-616(1987). RN [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=91048502; PubMed=2173165; DOI=10.1016/0049-3848(90)90142-Y; RA Meijers J.C.M., Chung D.W.; RT "Evidence for a glycine residue at position 316 in human protein C RT inhibitor."; RL Thromb. Res. 59:389-393(1990). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=91332018; PubMed=1714450; RA Meijers J.C.M., Chung D.W.; RT "Organization of the gene coding for human protein C inhibitor RT (plasminogen activator inhibitor-3). Assignment of the gene to RT chromosome 14."; RL J. Biol. Chem. 266:15028-15034(1991). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=94198434; PubMed=8148499; RA Hayashi T., Suzuki K.; RT "Gene organization of human protein C inhibitor, a member of SERPIN RT family proteins encoded in five exons."; RL Int. J. Hematol. 58:213-224(1993). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-55 AND GLU-105. RC TISSUE=Liver; RX PubMed=8713781; RA Radtke K.-P., Greengard J.S., Fernandez J.A., Villoutreix B.O., RA Griffin J.H.; RT "A two-allele polymorphism in protein C inhibitor with varying RT frequencies in different ethnic populations."; RL Thromb. Haemost. 75:62-69(1996). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLY-44; VAL-55; RP SER-64; VAL-94; GLU-105; PRO-115 AND ARG-217. RG SeattleSNPs variation discovery resource; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 27-406. RC TISSUE=Testis; RX MEDLINE=93229000; PubMed=8471250; RA Moore A., Penfold L.M., Johnson J.L., Latchman D.S., Moore H.D.; RT "Human sperm-egg binding is inhibited by peptides corresponding to RT core region of an acrosomal serine protease inhibitor."; RL Mol. Reprod. Dev. 34:280-291(1993). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-406. RC TISSUE=Testis; RG The German cDNA consortium; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [10] RP PROTEIN SEQUENCE OF 20-39. RX MEDLINE=90085156; PubMed=2556811; RA Laurell M., Stenflo J.; RT "Protein C inhibitor from human plasma: characterization of native and RT cleaved inhibitor and demonstration of inhibitor complexes with plasma RT kallikrein."; RL Thromb. Haemost. 62:885-891(1989). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-249, AND MASS RP SPECTROMETRY. RC TISSUE=Plasma; RX PubMed=14760718; DOI=10.1002/pmic.200300556; RA Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; RT "Screening for N-glycosylated proteins by liquid chromatography mass RT spectrometry."; RL Proteomics 4:454-465(2004). RN [12] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-262 AND ASN-338, AND MASS RP SPECTROMETRY. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [13] RP 3D-STRUCTURE MODELING. RX MEDLINE=91046026; PubMed=2172989; RA Kuhn L.A., Griffin J.H., Fisher C.L., Greengard J.S., Bouma B.N., RA Espana F., Tainer J.A.; RT "Elucidating the structural chemistry of glycosaminoglycan recognition RT by protein C inhibitor."; RL Proc. Natl. Acad. Sci. U.S.A. 87:8506-8510(1990). RN [14] RP VARIANTS VAL-55; SER-64; GLU-105; ALA-121 AND ARG-217. RX MEDLINE=99318093; PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions RT of human genes."; RL Nat. Genet. 22:231-238(1999). RN [15] RP ERRATUM. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). CC -!- FUNCTION: Inhibits activated protein C as well as plasminogen CC activators. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. CC -!- SIMILARITY: Belongs to the serpin family. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/serpina5/"; 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; J02639; AAA35688.1; -; mRNA. DR EMBL; M68516; AAA02811.1; -; Genomic_DNA. DR EMBL; S69366; AAB30461.1; -; Genomic_DNA. DR EMBL; S69364; AAB30461.1; JOINED; Genomic_DNA. DR EMBL; S69574; AAB30461.1; JOINED; Genomic_DNA. DR EMBL; S69365; AAB30461.1; JOINED; Genomic_DNA. DR EMBL; U35464; AAB60386.1; -; mRNA. DR EMBL; AF361796; AAK27240.1; -; Genomic_DNA. DR EMBL; BC008915; AAH08915.1; -; mRNA. DR EMBL; S58545; AAB26244.2; -; mRNA. DR EMBL; AL080185; CAB45766.1; -; mRNA. DR PIR; A39339; A39339. DR UniGene; Hs.510334; -. DR PDB; 1LQ8; X-ray; 2.40 A; A/C/E/G=30-375, B/D/F/H=376-406. DR PDB; 1PAI; Model; -; A=20-373, B=374-406. DR PDB; 2HI9; X-ray; 2.30 A; A/B/C=44-406. DR PDB; 2PAI; Model; -; A=20-373, B=374-406. DR PDBsum; 1LQ8; -. DR PDBsum; 1PAI; -. DR PDBsum; 2HI9; -. DR PDBsum; 2PAI; -. DR IntAct; P05154; 1. DR MEROPS; I04.004; -. DR PRIDE; P05154; -. DR Ensembl; ENSG00000188488; Homo sapiens. DR KEGG; hsa:5104; -. DR GeneCards; GC14P094117; -. DR H-InvDB; HIX0079547; -. DR HGNC; HGNC:8723; SERPINA5. DR MIM; 601841; gene. DR PharmGKB; PA35505; -. DR HOGENOM; P05154; -. DR HOVERGEN; P05154; -. DR DrugBank; DB00055; Drotrecogin alfa. DR DrugBank; DB00013; Urokinase. DR LinkHub; P05154; -. DR NextBio; 19698; -. DR ArrayExpress; P05154; -. DR CleanEx; HS_SERPINA5; -. DR GermOnline; ENSG00000188488; Homo sapiens. DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0043234; C:protein complex; IDA:UniProtKB. DR GO; GO:0032190; F:acrosin binding; IPI:UniProtKB. DR GO; GO:0008201; F:heparin binding; TAS:UniProtKB. DR GO; GO:0002020; F:protease binding; IPI:UniProtKB. DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IDA:UniProtKB. DR GO; GO:0007342; P:fusion of sperm to egg plasma membrane; NAS:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR InterPro; IPR000215; Protease_inhib_I4_serpin. DR PANTHER; PTHR11461; Prot_inh_serpin; 1. DR Pfam; PF00079; Serpin; 1. DR SMART; SM00093; SERPIN; 1. DR PROSITE; PS00284; SERPIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Glycoprotein; Polymorphism; KW Protease inhibitor; Secreted; Serine protease inhibitor; Signal. FT SIGNAL 1 19 FT CHAIN 20 406 Plasma serine protease inhibitor. FT /FTId=PRO_0000032427. FT SITE 373 374 Reactive bond. FT CARBOHYD 249 249 N-linked (GlcNAc...). FT CARBOHYD 262 262 N-linked (GlcNAc...). FT CARBOHYD 338 338 N-linked (GlcNAc...). FT VARIANT 44 44 S -> G (in dbSNP:rs2069975). FT /FTId=VAR_013080. FT VARIANT 55 55 A -> V (in allele PCI*B; dbSNP:rs6118). FT /FTId=VAR_007100. FT VARIANT 64 64 N -> S (in dbSNP:rs6115). FT /FTId=VAR_013081. FT VARIANT 94 94 G -> V (in dbSNP:rs2069976). FT /FTId=VAR_013082. FT VARIANT 105 105 K -> E (in allele PCI*B; dbSNP:rs6119). FT /FTId=VAR_007101. FT VARIANT 115 115 L -> P (in dbSNP:rs2069999). FT /FTId=VAR_013083. FT VARIANT 121 121 P -> A (in dbSNP:rs6120). FT /FTId=VAR_013900. FT VARIANT 217 217 G -> R (in dbSNP:rs6114). FT /FTId=VAR_013084. FT CONFLICT 28 28 K -> E (in Ref. 9; CAB45766). FT CONFLICT 221 221 Q -> L (in Ref. 8; AAB26244). FT CONFLICT 335 335 G -> R (in Ref. 1; AAA35688 and 8; FT AAB26244). FT CONFLICT 384 384 F -> S (in Ref. 8; AAB26244). FT HELIX 48 59 FT STRAND 65 67 FT HELIX 69 79 FT HELIX 80 82 FT HELIX 85 95 FT STRAND 99 102 FT HELIX 105 116 FT STRAND 123 136 FT HELIX 143 151 FT STRAND 156 160 FT HELIX 165 179 FT TURN 180 182 FT STRAND 193 211 FT HELIX 215 217 FT STRAND 219 228 FT STRAND 230 244 FT TURN 248 251 FT STRAND 252 262 FT STRAND 264 270 FT HELIX 275 281 FT HELIX 284 293 FT STRAND 295 304 FT STRAND 306 313 FT HELIX 314 317 FT HELIX 318 321 FT HELIX 325 327 FT TURN 334 336 FT STRAND 337 339 FT STRAND 343 355 FT STRAND 357 371 FT STRAND 380 383 FT STRAND 388 404 SQ SEQUENCE 406 AA; 45702 MW; 0B9D1A519341B8C9 CRC64; MQLFLLLCLV LLSPQGASLH RHHPREMKKR VEDLHVGATV APSSRRDFTF DLYRALASAA PSQNIFFSPV SISMSLAMLS LGAGSSTKMQ ILEGLGLNLQ KSSEKELHRG FQQLLQELNQ PRDGFQLSLG NALFTDLVVD LQDTFVSAMK TLYLADTFPT NFRDSAGAMK QINDYVAKQT KGKIVDLLKN LDSNAVVIMV NYIFFKAKWE TSFNHKGTQE QDFYVTSETV VRVPMMSRED QYHYLLDRNL SCRVVGVPYQ GNATALFILP SEGKMQQVEN GLSEKTLRKW LKMFKKRQLE LYLPKFSIEG SYQLEKVLPS LGISNVFTSH ADLSGISNHS NIQVSEMVHK AVVEVDESGT RAAAATGTIF TFRSARLNSQ RLVFNRPFLM FIVDNNILFL GKVNRP //