GenomeNet

Database: UniProt
Entry: P16294
LinkDB: P16294
Original site: P16294 
ID   FA9_MOUSE               Reviewed;         471 AA.
AC   P16294; Q3UES1;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 3.
DT   31-JUL-2019, entry version 200.
DE   RecName: Full=Coagulation factor IX;
DE            EC=3.4.21.22 {ECO:0000250|UniProtKB:P00740};
DE   AltName: Full=Christmas factor;
DE   Contains:
DE     RecName: Full=Coagulation factor IXa light chain;
DE   Contains:
DE     RecName: Full=Coagulation factor IXa heavy chain;
DE   Flags: Precursor;
GN   Name=F9; Synonyms=Cf9;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Liver;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-471, AND TISSUE SPECIFICITY.
RX   PubMed=2323576; DOI=10.1016/0378-1119(90)90290-8;
RA   Wu S.-M., Stafford D.W., Ware J.;
RT   "Deduced amino acid sequence of mouse blood-coagulation factor IX.";
RL   Gene 86:275-278(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 180-463.
RX   PubMed=2303254; DOI=10.1016/0888-7543(90)90458-7;
RA   Sarkar G., Koeberl D.D., Sommer S.S.;
RT   "Direct sequencing of the activation peptide and the catalytic domain
RT   of the factor IX gene in six species.";
RL   Genomics 6:133-143(1990).
CC   -!- FUNCTION: Factor IX is a vitamin K-dependent plasma protein that
CC       participates in the intrinsic pathway of blood coagulation by
CC       converting factor X to its active form in the presence of Ca(2+)
CC       ions, phospholipids, and factor VIIIa.
CC       {ECO:0000250|UniProtKB:P00740}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form
CC         factor Xa.; EC=3.4.21.22;
CC         Evidence={ECO:0000250|UniProtKB:P00740};
CC   -!- SUBUNIT: Heterodimer of a light chain and a heavy chain;
CC       disulfide-linked. Interacts with SERPINC1.
CC       {ECO:0000250|UniProtKB:P00740}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00740}.
CC   -!- TISSUE SPECIFICITY: Detected in liver.
CC       {ECO:0000269|PubMed:2323576}.
CC   -!- DOMAIN: Calcium binds to the gamma-carboxyglutamic acid (Gla)
CC       residues in the Gla domain. Calcium can also bind, with stronger
CC       affinity, to another site beyond the Gla domain. Under
CC       physiological ion concentrations, Ca(2+) is displaced by Mg(2+)
CC       from some of the gammaglutamate residues in the N-terminal Gla
CC       domain. This leads to a subtle conformation change that may affect
CC       the interaction with its binding protein.
CC       {ECO:0000250|UniProtKB:P00741}.
CC   -!- PTM: Activated by factor XIa, which excises the activation
CC       peptide. The propeptide can also be removed by snake venom
CC       protease. {ECO:0000250|UniProtKB:P00740}.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000250|UniProtKB:P00740}.
CC   -!- PTM: Predominantly O-glucosylated at Ser-99 by POGLUT1 in vitro.
CC       {ECO:0000250|UniProtKB:P00740}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; AK149372; BAE28840.1; -; mRNA.
DR   EMBL; M23109; AAA37629.1; -; mRNA.
DR   EMBL; M26236; AAA37630.1; -; mRNA.
DR   CCDS; CCDS30158.1; -.
DR   PIR; JQ0419; JQ0419.
DR   RefSeq; NP_001292726.1; NM_001305797.1.
DR   RefSeq; NP_032005.1; NM_007979.2.
DR   STRING; 10090.ENSMUSP00000033477; -.
DR   MEROPS; S01.214; -.
DR   iPTMnet; P16294; -.
DR   PhosphoSitePlus; P16294; -.
DR   CPTAC; non-CPTAC-3415; -.
DR   CPTAC; non-CPTAC-3576; -.
DR   MaxQB; P16294; -.
DR   PaxDb; P16294; -.
DR   PRIDE; P16294; -.
DR   TopDownProteomics; P16294; -.
DR   Ensembl; ENSMUST00000033477; ENSMUSP00000033477; ENSMUSG00000031138.
DR   GeneID; 14071; -.
DR   KEGG; mmu:14071; -.
DR   UCSC; uc009thw.2; mouse.
DR   CTD; 2158; -.
DR   MGI; MGI:88384; F9.
DR   eggNOG; ENOG410IGPV; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00940000159516; -.
DR   HOGENOM; HOG000251821; -.
DR   InParanoid; P16294; -.
DR   KO; K01321; -.
DR   OMA; TINKYSH; -.
DR   OrthoDB; 1314811at2759; -.
DR   PhylomeDB; P16294; -.
DR   TreeFam; TF327329; -.
DR   Reactome; R-MMU-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-MMU-159740; Gamma-carboxylation of protein precursors.
DR   Reactome; R-MMU-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR   Reactome; R-MMU-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR   PRO; PR:P16294; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   Bgee; ENSMUSG00000031138; Expressed in 26 organ(s), highest expression level in liver.
DR   Genevisible; P16294; MM.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0004175; F:endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0008233; F:peptidase activity; IDA:MGI.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR   GO; GO:0006508; P:proteolysis; ISO:MGI.
DR   GO; GO:0031638; P:zymogen activation; ISS:UniProtKB.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 4.10.740.10; -; 1.
DR   InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR   InterPro; IPR035694; Coagulation_factor_IX.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR035972; GLA-like_dom_SF.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24278:SF31; PTHR24278:SF31; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001143; Factor_X; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00001; GLABLOOD.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57630; SSF57630; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 2.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS00011; GLA_1; 1.
DR   PROSITE; PS50998; GLA_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Complete proteome; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase;
KW   Hydroxylation; Magnesium; Metal-binding; Phosphoprotein; Protease;
KW   Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW   Sulfation; Zymogen.
FT   SIGNAL        1     28       {ECO:0000255}.
FT   PROPEP       29     46       {ECO:0000250|UniProtKB:P00740}.
FT                                /FTId=PRO_0000027760.
FT   CHAIN        47    471       Coagulation factor IX.
FT                                /FTId=PRO_0000027761.
FT   CHAIN        47    192       Coagulation factor IXa light chain.
FT                                /FTId=PRO_0000027762.
FT   PROPEP      193    236       Activation peptide. {ECO:0000250}.
FT                                /FTId=PRO_0000027763.
FT   CHAIN       237    471       Coagulation factor IXa heavy chain.
FT                                /FTId=PRO_0000027764.
FT   DOMAIN       47     92       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       93    129       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      130    171       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      237    469       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    277    277       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   ACT_SITE    325    325       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   ACT_SITE    421    421       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        47     47       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        48     48       Calcium 2.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        53     53       Calcium 1; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        53     53       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        54     54       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        54     54       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        61     61       Calcium 4 or magnesium 1; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        63     63       Calcium 1; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        63     63       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        63     63       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        66     66       Calcium 4 or magnesium 1; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        67     67       Calcium 1; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        72     72       Calcium 5 or magnesium 2; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        73     73       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        73     73       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        76     76       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        76     76       Calcium 5 or magnesium 2; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        82     82       Calcium 6 or magnesium 3; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        86     86       Calcium 6 or magnesium 3; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        93     93       Calcium 7.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        94     94       Calcium 7; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        96     96       Calcium 7.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       110    110       Calcium 7.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       111    111       Calcium 7; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       291    291       Calcium 8.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       293    293       Calcium 8; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       298    298       Calcium 8.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       301    301       Calcium 8.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   SITE        192    193       Cleavage; by factor XIa.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   SITE        236    237       Cleavage; by factor XIa.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES      53     53       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      54     54       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      61     61       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      63     63       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      66     66       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      67     67       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      72     72       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      73     73       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      76     76       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      79     79       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      82     82       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      86     86       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES     110    110       (3R)-3-hydroxyaspartate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     114    114       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     202    202       Sulfotyrosine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     205    205       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     206    206       Phosphothreonine; alternate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD     85     85       O-linked (GalNAc...) threonine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD     99     99       O-linked (Glc...) serine; alternate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD     99     99       O-linked (Xyl...) serine; alternate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD    204    204       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    206    206       O-linked (GalNAc...) threonine;
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD    223    223       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    225    225       O-linked (GalNAc...) threonine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD    235    235       O-linked (GalNAc...) threonine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID     64     69       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID     97    108       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    102    117       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    119    128       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    134    145       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    141    155       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    157    170       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    178    345       Interchain (between light and heavy
FT                                chains). {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    262    278       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    392    406       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    417    445       {ECO:0000250|UniProtKB:P00740}.
FT   CONFLICT    375    375       Q -> H (in Ref. 2; AAA37629).
FT                                {ECO:0000305}.
FT   CONFLICT    400    400       I -> T (in Ref. 2; AAA37629).
FT                                {ECO:0000305}.
SQ   SEQUENCE   471 AA;  52978 MW;  05E08E86622397E2 CRC64;
     MKHLNTVMAE SPALITIFLL GYLLSTECAV FLDRENATKI LTRPKRYNSG KLEEFVRGNL
     ERECIEERCS FEEAREVFEN TEKTTEFWKQ YVDGDQCESN PCLNGGICKD DISSYECWCQ
     VGFEGRNCEL DATCNIKNGR CKQFCKNSPD NKVICSCTEG YQLAEDQKSC EPTVPFPCGR
     ASISYSSKKI TRAETVFSNM DYENSTEAVF IQDDITDGAI LNNVTESSES LNDFTRVVGG
     ENAKPGQIPW QVILNGEIEA FCGGAIINEK WIVTAAHCLK PGDKIEVVAG EYNIDKKEDT
     EQRRNVIRTI PHHQYNATIN KYSHDIALLE LDKPLILNSY VTPICVANRE YTNIFLKFGS
     GYVSGWGKVF NKGRQASILQ YLRVPLVDRA TCLRSTTFTI YNNMFCAGYR EGGKDSCEGD
     SGGPHVTEVE GTSFLTGIIS WGEECAMKGK YGIYTKVSRY VNWIKEKTKL T
//
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