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Database: UniProt
Entry: D2HEC6_AILME
LinkDB: D2HEC6_AILME
Original site: D2HEC6_AILME 
ID   D2HEC6_AILME            Unreviewed;       431 AA.
AC   D2HEC6;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   06-JUL-2016, entry version 49.
DE   SubName: Full=Putative uncharacterized protein {ECO:0000313|EMBL:EFB13223.1};
DE   Flags: Fragment;
GN   ORFNames=PANDA_009140 {ECO:0000313|EMBL:EFB13223.1};
OS   Ailuropoda melanoleuca (Giant panda).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae;
OC   Ailuropoda.
OX   NCBI_TaxID=9646;
RN   [1] {ECO:0000313|EMBL:EFB13223.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20010809; DOI=10.1038/nature08696;
RA   Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q.,
RA   Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H.,
RA   Jian M., Li J., Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z.,
RA   Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X.,
RA   Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W.,
RA   Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q.,
RA   Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H.,
RA   Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z.,
RA   Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G.,
RA   Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W.,
RA   Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N.,
RA   Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N.,
RA   Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y.,
RA   Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X.,
RA   Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA   Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H.,
RA   Wang J., Wang J.;
RT   "The sequence and de novo assembly of the giant panda genome.";
RL   Nature 463:311-317(2010).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|SAAS:SAAS00558208}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|SAAS:SAAS00559343}.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
CC       {ECO:0000256|RuleBase:RU363034}.
CC   -!- SIMILARITY: Contains Gla (gamma-carboxy-glutamate) domain.
CC       {ECO:0000256|SAAS:SAAS00522319}.
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DR   EMBL; GL192750; EFB13223.1; -; Genomic_DNA.
DR   STRING; 9646.ENSAMEP00000017115; -.
DR   MEROPS; S01.214; -.
DR   eggNOG; ENOG410IGPV; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000251821; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR   Gene3D; 4.10.740.10; -; 1.
DR   InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
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; 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   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; 2.
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   3: Inferred from homology;
KW   Calcium {ECO:0000256|SAAS:SAAS00433206};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS00037407};
KW   EGF-like domain {ECO:0000256|RuleBase:RU000459,
KW   ECO:0000256|SAAS:SAAS00602928};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034,
KW   ECO:0000256|SAAS:SAAS00524687};
KW   Protease {ECO:0000256|RuleBase:RU363034,
KW   ECO:0000256|SAAS:SAAS00524999};
KW   Secreted {ECO:0000256|SAAS:SAAS00526105};
KW   Serine protease {ECO:0000256|RuleBase:RU363034}.
FT   DOMAIN       19     65       Gla (gamma-carboxy-glutamate).
FT                                {ECO:0000259|PROSITE:PS50998}.
FT   DOMAIN       65    101       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      197    429       Peptidase S1. {ECO:0000259|PROSITE:
FT                                PS50240}.
FT   ACT_SITE    237    237       Charge relay system. {ECO:0000256|PIRSR:
FT                                PIRSR001143-1}.
FT   ACT_SITE    285    285       Charge relay system. {ECO:0000256|PIRSR:
FT                                PIRSR001143-1}.
FT   ACT_SITE    381    381       Charge relay system. {ECO:0000256|PIRSR:
FT                                PIRSR001143-1}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:EFB13223.1}.
FT   NON_TER     431    431       {ECO:0000313|EMBL:EFB13223.1}.
SQ   SEQUENCE   431 AA;  48660 MW;  1791A3F770D667C9 CRC64;
     SVFLDHENAT KILNRPKRYN SGKLEEFVRG NLERECLEEK CSFEEAREVF ENTEKTTEFW
     KQYVDGDQCE SDPCLNGGIC KDDINSYECW CQAGFEGKNC ELDVTCNIKN GRCKQFCKLG
     ADNKVVCSCT AGYQLAEDQR SCEPAVPFPC GRVSVPHIST TRTRAETFFS NMDYENSTEV
     EKNFENLTQP LNDLTRVVGG KDAKPGQFPW QVLLTRKVDA FCGGSIINEK WVVTAAHCIE
     PDVKITVVAG EHNTQVSEHT EQKRNVIRTI LHHSYNATIN KYNHDIALLE LDEPLTFNSY
     VTPICVADRE YTNIFLKFGS GYVSGWGRVF HRGRSASILQ YLKVPLVDRA TCLRSTKFTI
     YNNMFCAGFH EGGKDSCQGD SGGPHVTEVE GISFLTGIIS WGEECATKGK YGIYTKVSRY
     VNWIKEKTKL T
//
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