GenomeNet

Database: UniProt
Entry: P16296
LinkDB: P16296
Original site: P16296 
ID   FA9_RAT                 Reviewed;         462 AA.
AC   P16296; F1M1M6;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2015, sequence version 2.
DT   05-JUN-2019, entry version 143.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 173-454.
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   -!- 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-92 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; AABR06108743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06108744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06108745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AABR06108746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH474019; EDL86171.1; -; Genomic_DNA.
DR   EMBL; M26247; AAA41162.1; -; mRNA.
DR   PIR; I84621; I84621.
DR   RefSeq; NP_113728.1; NM_031540.1.
DR   SMR; P16296; -.
DR   STRING; 10116.ENSRNOP00000004559; -.
DR   ChEMBL; CHEMBL4105734; -.
DR   MEROPS; S01.214; -.
DR   PaxDb; P16296; -.
DR   PeptideAtlas; P16296; -.
DR   PRIDE; P16296; -.
DR   Ensembl; ENSRNOT00000004559; ENSRNOP00000004559; ENSRNOG00000003430.
DR   GeneID; 24946; -.
DR   KEGG; rno:24946; -.
DR   CTD; 2158; -.
DR   RGD; 2589; F9.
DR   eggNOG; ENOG410IGPV; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00940000159516; -.
DR   InParanoid; P16296; -.
DR   KO; K01321; -.
DR   OMA; TINKYSH; -.
DR   OrthoDB; 1314811at2759; -.
DR   TreeFam; TF327329; -.
DR   Reactome; R-RNO-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-RNO-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-RNO-159740; Gamma-carboxylation of protein precursors.
DR   Reactome; R-RNO-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR   Reactome; R-RNO-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR   PRO; PR:P16296; -.
DR   Proteomes; UP000002494; Chromosome X.
DR   Bgee; ENSRNOG00000003430; Expressed in 4 organ(s), highest expression level in liver.
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:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IDA:RGD.
DR   GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
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; Complete proteome; Disulfide bond;
KW   EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis;
KW   Hydrolase; Hydroxylation; Magnesium; Metal-binding; Phosphoprotein;
KW   Protease; Reference proteome; Secreted; Serine protease; Signal;
KW   Sulfation; Zymogen.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   PROPEP       22     39       {ECO:0000250|UniProtKB:P00740}.
FT                                /FTId=PRO_0000433111.
FT   CHAIN        40    462       Coagulation factor IX.
FT                                /FTId=PRO_0000088685.
FT   CHAIN        40    185       Coagulation factor IXa light chain.
FT                                /FTId=PRO_0000433112.
FT   PROPEP      186    227       Activation peptide. {ECO:0000250}.
FT                                /FTId=PRO_0000433113.
FT   CHAIN       228    462       Coagulation factor IXa heavy chain.
FT                                /FTId=PRO_0000433114.
FT   DOMAIN       40     86       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       86    122       EGF-like; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      228    460       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    268    268       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   ACT_SITE    316    316       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   ACT_SITE    412    412       Charge relay system.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        40     40       Calcium 1; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        41     41       Calcium 2.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        46     46       Calcium 1; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        46     46       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        47     47       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        47     47       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        54     54       Calcium 4 or magnesium 1; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740,
FT                                ECO:0000250|UniProtKB:P00741}.
FT   METAL        56     56       Calcium 1; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        56     56       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        56     56       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        59     59       Calcium 4 or magnesium 1; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740,
FT                                ECO:0000250|UniProtKB:P00741}.
FT   METAL        60     60       Calcium 1; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        65     65       Calcium 5 or magnesium 2; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740,
FT                                ECO:0000250|UniProtKB:P00741}.
FT   METAL        66     66       Calcium 2; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        66     66       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        69     69       Calcium 3; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        69     69       Calcium 5 or magnesium 2; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        69     69       Calcium 5; via 4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        75     75       Calcium 6 or magnesium 3; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741}.
FT   METAL        79     79       Calcium 6 or magnesium 3; via 4-
FT                                carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741}.
FT   METAL        86     86       Calcium 7.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        87     87       Calcium 7; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL        89     89       Calcium 7.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       103    103       Calcium 7.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       104    104       Calcium 7; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       282    282       Calcium 8.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       284    284       Calcium 8; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       287    287       Calcium 8; via carbonyl oxygen.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       289    289       Calcium 8.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   METAL       292    292       Calcium 8.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   SITE        185    186       Cleavage; by factor XIa.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   SITE        227    228       Cleavage; by factor XIa.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES      46     46       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      47     47       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      56     56       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      59     59       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      60     60       4-carboxyglutamate.
FT                                {ECO:0000250|UniProtKB:P00741,
FT                                ECO:0000255|PROSITE-ProRule:PRU00463}.
FT   MOD_RES      65     65       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      69     69       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      75     75       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     103    103       (3R)-3-hydroxyaspartate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     107    107       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     195    195       Sulfotyrosine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     198    198       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   MOD_RES     199    199       Phosphothreonine; alternate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD     78     78       O-linked (GalNAc...) threonine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD     92     92       O-linked (Glc...) serine; alternate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD     92     92       O-linked (Xyl...) serine; alternate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD    199    199       O-linked (GalNAc...) threonine;
FT                                alternate.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD    208    208       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    214    214       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    216    216       O-linked (GalNAc...) threonine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD    226    226       O-linked (GalNAc...) threonine.
FT                                {ECO:0000250|UniProtKB:P00740}.
FT   CARBOHYD    307    307       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     57     62       {ECO:0000250|UniProtKB:P00741}.
FT   DISULFID     90    101       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID     95    110       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    112    121       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    127    138       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    134    148       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    150    163       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    171    336       Interchain (between light and heavy
FT                                chains). {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    253    269       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    383    397       {ECO:0000250|UniProtKB:P00740}.
FT   DISULFID    408    436       {ECO:0000250|UniProtKB:P00740}.
SQ   SEQUENCE   462 AA;  51808 MW;  6C50A44A8F0945EB CRC64;
     MADAPGLIPI FLLGYLLSTE CAVFLDRENA TKILTRPKRY NSGKLEEFVQ GNLERECIEE
     RCSFEEAREV FENTEKTTEF WKQYVDGDQC ESNPCLNGGI CKDDINSYEC WCQAGFEGRN
     CELDATCSIK NGRCKQFCKN SPDNKIICSC TEGYQLAEDQ KSCEPAVPFP CGRVSVAYNS
     KKITRAETVF SNTDYGNSTE LILDDITNST ILDNLTENSE PINDFTRVVG GENAKPGQIP
     WQVILNGEIE AFCGGAIINE KWIVTAAHCL KPGDKIEVVA GEHNIDEKED TEQRRNVIRT
     IPHHQYNATI NKYSHDIALL ELDKPLILNS YVTPICVANK EYTNIFLKFG SGYVSGWGKV
     FNKGRQASIL QYLRVPLVDR ATCLRSTKFS IYNNMFCAGY REGGKDSCEG DSGGPHVTEV
     EGTSFLTGII SWGEECAMKG KYGIYTKVSR YVNWIKEKTK LT
//
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