GenomeNet

Database: UniProt/SWISS-PROT UniProt/TrEMBL
Entry: TMPS9_HUMAN Q0X0F2_HUMAN
LinkDB: TMPS9_HUMAN Q0X0F2_HUMAN
Original site: TMPS9_HUMAN Q0X0F2_HUMAN 
ID   TMPS9_HUMAN             Reviewed;        1059 AA.
AC   Q7Z410; Q6ZND6; Q7Z411;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 2.
DT   25-OCT-2017, entry version 127.
DE   RecName: Full=Transmembrane protease serine 9;
DE            EC=3.4.21.-;
DE   AltName: Full=Polyserase-I;
DE   AltName: Full=Polyserine protease 1;
DE            Short=Polyserase-1;
DE   Contains:
DE     RecName: Full=Serase-1;
DE   Contains:
DE     RecName: Full=Serase-2;
DE   Contains:
DE     RecName: Full=Serase-3;
GN   Name=TMPRSS9;
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], ENZYME ACTIVITY, ENZYME REGULATION,
RP   CLEAVAGE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=12886014; DOI=10.1073/pnas.1633392100;
RA   Cal S., Quesada V., Garabaya C., Lopez-Otin C.;
RT   "Polyserase-I, a human polyprotease with the ability to generate
RT   independent serine protease domains from a single translation
RT   product.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9185-9190(2003).
RN   [2]
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.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 472-1059, AND VARIANTS
RP   ASN-793 AND LYS-938.
RC   TISSUE=Thalamus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
CC   -!- FUNCTION: Serase-1 and serase-2 are serine proteases that
CC       hydrolyze the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln-
CC       Gly-Arg-AMC. In contrast, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Ala-
CC       Pro-Ala-AMC are not significantly hydrolyzed.
CC   -!- ENZYME REGULATION: Inhibited by serine protease inhibitors PMSF
CC       and 4-(2-aminoethyl)benzenesulfonyl fluoride, but not by EDTA.
CC       {ECO:0000269|PubMed:12886014}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12886014};
CC       Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:12886014}.
CC   -!- TISSUE SPECIFICITY: Expressed in fetal human tissues, such as
CC       kidney, liver, lung and brain, and in a variety of tumor cell
CC       lines. Weakly expressed in adult tissues including skeletal
CC       muscle, liver, placenta and heart. {ECO:0000269|PubMed:12886014}.
CC   -!- DOMAIN: The serine protease 1 and 2 domains are catalytically
CC       active, whereas the serine protease 3 domain lacks the essential
CC       Ser residue of the catalytic triad at position 1009 and is
CC       predicted to be inactive.
CC   -!- PTM: Proteolytically cleaved to generate 3 independent serine
CC       protease chains. The cleaved chains may remain attached to the
CC       membrane thanks to disufide bonds. It is unclear whether cleavage
CC       always takes place. {ECO:0000269|PubMed:12886014}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD18439.1; Type=Frameshift; Positions=776; Evidence={ECO:0000305};
CC       Sequence=CAD35759.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
DR   EMBL; AJ488946; CAD35758.1; -; mRNA.
DR   EMBL; AJ488947; CAD35759.1; ALT_SEQ; mRNA.
DR   EMBL; AC011522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC011542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK131261; BAD18439.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS12088.1; -.
DR   RefSeq; NP_892018.1; NM_182973.2.
DR   UniGene; Hs.465560; -.
DR   ProteinModelPortal; Q7Z410; -.
DR   SMR; Q7Z410; -.
DR   STRING; 9606.ENSP00000330264; -.
DR   MEROPS; S01.969; -.
DR   iPTMnet; Q7Z410; -.
DR   PhosphoSitePlus; Q7Z410; -.
DR   BioMuta; TMPRSS9; -.
DR   DMDM; 61217609; -.
DR   PaxDb; Q7Z410; -.
DR   PeptideAtlas; Q7Z410; -.
DR   PRIDE; Q7Z410; -.
DR   TopDownProteomics; Q7Z410; -.
DR   DNASU; 360200; -.
DR   Ensembl; ENST00000332578; ENSP00000330264; ENSG00000178297.
DR   GeneID; 360200; -.
DR   KEGG; hsa:360200; -.
DR   UCSC; uc010xgx.3; human.
DR   CTD; 360200; -.
DR   DisGeNET; 360200; -.
DR   EuPathDB; HostDB:ENSG00000178297.12; -.
DR   GeneCards; TMPRSS9; -.
DR   HGNC; HGNC:30079; TMPRSS9.
DR   HPA; HPA051483; -.
DR   MIM; 610477; gene.
DR   neXtProt; NX_Q7Z410; -.
DR   OpenTargets; ENSG00000178297; -.
DR   PharmGKB; PA134967594; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00900000140784; -.
DR   HOGENOM; HOG000154654; -.
DR   HOVERGEN; HBG079270; -.
DR   InParanoid; Q7Z410; -.
DR   KO; K09640; -.
DR   OMA; PDCGLAP; -.
DR   OrthoDB; EOG091G0DF7; -.
DR   PhylomeDB; Q7Z410; -.
DR   TreeFam; TF330647; -.
DR   GenomeRNAi; 360200; -.
DR   PRO; PR:Q7Z410; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; ENSG00000178297; -.
DR   CleanEx; HS_TMPRSS9; -.
DR   ExpressionAtlas; Q7Z410; baseline and differential.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd00112; LDLa; 1.
DR   CDD; cd00190; Tryp_SPc; 3.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR017324; Tmprss9.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF00089; Trypsin; 3.
DR   PIRSF; PIRSF037931; TMPRSS9_polyserase-1; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00020; Tryp_SPc; 3.
DR   SUPFAM; SSF50494; SSF50494; 3.
DR   SUPFAM; SSF57424; SSF57424; 1.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 3.
DR   PROSITE; PS00134; TRYPSIN_HIS; 3.
DR   PROSITE; PS00135; TRYPSIN_SER; 2.
PE   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
KW   Hydrolase; Membrane; Polymorphism; Protease; Reference proteome;
KW   Repeat; Serine protease; Signal-anchor; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN         1   1059       Transmembrane protease serine 9.
FT                                {ECO:0000255}.
FT                                /FTId=PRO_0000027867.
FT   CHAIN       203    503       Serase-1. {ECO:0000255}.
FT                                /FTId=PRO_0000027868.
FT   CHAIN       504    826       Serase-2. {ECO:0000255}.
FT                                /FTId=PRO_0000027869.
FT   CHAIN       827   1059       Serase-3. {ECO:0000255}.
FT                                /FTId=PRO_0000027870.
FT   TOPO_DOM      1     29       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     30     50       Helical; Signal-anchor for type II
FT                                membrane protein. {ECO:0000255}.
FT   TOPO_DOM     51   1059       Extracellular. {ECO:0000255}.
FT   DOMAIN      153    190       LDL-receptor class A.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN      203    436       Peptidase S1 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   DOMAIN      504    736       Peptidase S1 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   DOMAIN      827   1058       Peptidase S1 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    243    243       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    292    292       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    387    387       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    544    544       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    592    592       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    687    687       Charge relay system. {ECO:0000250}.
FT   SITE        202    203       Cleavage. {ECO:0000255}.
FT   SITE        503    504       Cleavage. {ECO:0000255}.
FT   SITE        826    827       Cleavage. {ECO:0000255}.
FT   CARBOHYD    547    547       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    638    638       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    663    663       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    786    786       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    154    166       {ECO:0000250}.
FT   DISULFID    161    180       {ECO:0000250}.
FT   DISULFID    174    189       {ECO:0000250}.
FT   DISULFID    228    244       {ECO:0000250}.
FT   DISULFID    326    393       {ECO:0000250}.
FT   DISULFID    358    372       {ECO:0000250}.
FT   DISULFID    383    412       {ECO:0000250}.
FT   DISULFID    529    545       {ECO:0000250}.
FT   DISULFID    626    693       {ECO:0000250}.
FT   DISULFID    658    672       {ECO:0000250}.
FT   DISULFID    683    712       {ECO:0000250}.
FT   DISULFID    853    869       {ECO:0000250}.
FT   DISULFID    949   1015       {ECO:0000250}.
FT   DISULFID    980    994       {ECO:0000250}.
FT   DISULFID   1005   1034       {ECO:0000250}.
FT   VARIANT       4      4       T -> A (in dbSNP:rs8100709).
FT                                /FTId=VAR_051845.
FT   VARIANT      30     30       S -> T (in dbSNP:rs891174).
FT                                /FTId=VAR_021508.
FT   VARIANT      73     73       R -> W (in dbSNP:rs17685098).
FT                                /FTId=VAR_033650.
FT   VARIANT     456    456       A -> T (in dbSNP:rs10153474).
FT                                /FTId=VAR_051846.
FT   VARIANT     659    659       S -> T (in dbSNP:rs60568869).
FT                                /FTId=VAR_061774.
FT   VARIANT     793    793       S -> N (in dbSNP:rs735911).
FT                                {ECO:0000269|PubMed:14702039}.
FT                                /FTId=VAR_021509.
FT   VARIANT     938    938       E -> K (in dbSNP:rs7247162).
FT                                {ECO:0000269|PubMed:14702039}.
FT                                /FTId=VAR_021510.
FT   CONFLICT    657    657       T -> P (in Ref. 3; BAD18439).
FT                                {ECO:0000305}.
FT   CONFLICT    899    899       A -> V (in Ref. 3; BAD18439).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1059 AA;  114021 MW;  17D27A2D99F2A264 CRC64;
     MEPTVADVHL VPRTTKEVPA LDAACCRAAS IGVVATSLVV LTLGVLLAFL STQGFHVDHT
     AELRGIRWTS SLRRETSDYH RTLTPTLEAL LHFLLRPLQT LSLGLEEELL QRGIRARLRE
     HGISLAAYGT IVSAELTGRH KGPLAERDFK SGRCPGNSFS CGNSQCVTKV NPECDDQEDC
     SDGSDEAHCE CGLQPAWRMA GRIVGGMEAS PGEFPWQASL RENKEHFCGA AIINARWLVS
     AAHCFNEFQD PTKWVAYVGA TYLSGSEAST VRAQVVQIVK HPLYNADTAD FDVAVLELTS
     PLPFGRHIQP VCLPAATHIF PPSKKCLISG WGYLKEDFLV KPEVLQKATV ELLDQALCAS
     LYGHSLTDRM VCAGYLDGKV DSCQGDSGGP LVCEEPSGRF FLAGIVSWGI GCAEARRPGV
     YARVTRLRDW ILEATTKASM PLAPTMAPAP AAPSTAWPTS PESPVVSTPT KSMQALSTVP
     LDWVTVPKLQ ECGARPAMEK PTRVVGGFGA ASGEVPWQVS LKEGSRHFCG ATVVGDRWLL
     SAAHCFNHTK VEQVRAHLGT ASLLGLGGSP VKIGLRRVVL HPLYNPGILD FDLAVLELAS
     PLAFNKYIQP VCLPLAIQKF PVGRKCMISG WGNTQEGNAT KPELLQKASV GIIDQKTCSV
     LYNFSLTDRM ICAGFLEGKV DSCQGDSGGP LACEEAPGVF YLAGIVSWGI GCAQVKKPGV
     YTRITRLKGW ILEIMSSQPL PMSPPSTTRM LATTSPRTTA GLTVPGATPS RPTPGAASRV
     TGQPANSTLS AVSTTARGQT PFPDAPEATT HTQLPDCGLA PAALTRIVGG SAAGRGEWPW
     QVSLWLRRRE HRCGAVLVAE RWLLSAAHCF DVYGDPKQWA AFLGTPFLSG AEGQLERVAR
     IYKHPFYNLY TLDYDVALLE LAGPVRRSRL VRPICLPEPA PRPPDGTRCV ITGWGSVREG
     GSMARQLQKA AVRLLSEQTC RRFYPVQISS RMLCAGFPQG GVDSCSGDAG GPLACREPSG
     RWVLTGVTSW GYGCGRPHFP GVYTRVAAVR GWIGQHIQE
//
  All links  
Ontology (2)   
   GO (2)   
Disease (1)   
   OMIM (1)   
Gene (8)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
   HGNC (1)   
   ENSEMBL-UP (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (5)   
   EMBL (5)   
Protein domain (17)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (5)   
   SMART (2)   
Literature (3)   
   PubMed (3)   
All databases (37)   

Download RDF
ID   Q0X0F2_HUMAN            Unreviewed;       531 AA.
AC   Q0X0F2;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   25-OCT-2017, entry version 65.
DE   SubName: Full=Serase-1B {ECO:0000313|EMBL:BAF02295.1};
GN   Name=serase-1B {ECO:0000313|EMBL:BAF02295.1};
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 {ECO:0000313|EMBL:BAF02295.1};
RN   [1] {ECO:0000313|EMBL:BAF02295.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16872279; DOI=10.1042/BJ20060212;
RA   Okumura Y., Hayama M., Takahashi E., Fujiuchi M., Shimabukuro A.,
RA   Yano M., Kido H.;
RT   "Serase-1B, a new splice variant of polyserase-1/TMPRSS9, activates
RT   urokinase-type plasminogen activator and the proteolytic activation is
RT   negatively regulated by glycosaminoglycans.";
RL   Biochem. J. 400:551-561(2006).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|SAAS:SAAS00559343}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AB109390; BAF02295.1; -; mRNA.
DR   RefSeq; NP_892018.1; NM_182973.2.
DR   UniGene; Hs.465560; -.
DR   ProteinModelPortal; Q0X0F2; -.
DR   PeptideAtlas; Q0X0F2; -.
DR   GeneID; 360200; -.
DR   KEGG; hsa:360200; -.
DR   CTD; 360200; -.
DR   HOGENOM; HOG000120710; -.
DR   HOVERGEN; HBG082971; -.
DR   KO; K09640; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd00112; LDLa; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 3.30.70.960; -; 1.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR000082; SEA_dom.
DR   InterPro; IPR036364; SEA_dom_sf.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF01390; SEA; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00192; LDLa; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57424; SSF57424; 1.
DR   SUPFAM; SSF82671; SSF82671; 1.
DR   PROSITE; PS50068; LDLRA_2; 1.
DR   PROSITE; PS50024; SEA; 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   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00124,
KW   ECO:0000256|SAAS:SAAS00037407};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     28     50       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       51    164       SEA. {ECO:0000259|PROSITE:PS50024}.
FT   DOMAIN      237    470       Peptidase S1. {ECO:0000259|PROSITE:
FT                                PS50240}.
FT   DISULFID    188    200       {ECO:0000256|PROSITE-ProRule:PRU00124}.
FT   DISULFID    208    223       {ECO:0000256|PROSITE-ProRule:PRU00124}.
SQ   SEQUENCE   531 AA;  57511 MW;  3BC7E03801472D59 CRC64;
     MEPTVADVHL VPRTTKEVPA LDAACCRAAT IGVVATSLVV LTLGVLLAFL STQGFHVDHT
     AELRGIRWTS SLRRETSDYH RTLTPTLEAL FVSSFQKTEL EASCVGCSVL NYRDGNSSVL
     VHFQLHFLLR PLQTLSLGLE EELLQRGIRA RLREHGISLA AYGTIVSAEL TGRHKGPLAE
     RDFKSGRCPG NSFSCGNSQC VTKVNPECDD QEDCSDGSDE AHCECGLQPA WRMAGRIVGG
     MEASPGEFPW QASLRENKEH FCGAAIINAR WLVSAAHCFN EFQDPTKWVA YVGATYLSGS
     EASTVRAQVV QIVKHPLYNA DTADFDVAVL ELTSPLPFGR HIQPVCLPAA THIFPPSKKC
     LISGWGYLKE DFLVKPEVLQ KATVELLDQA LCASLYGHSL TDRMVCAGYL DGKVDSCQGD
     SGGPLVCEEP SGRFFLAGIV SWGIGCAEAR RPGVYARVTR LRDWILEATT KASMPLAPTM
     APAPAAPSTA WPTSPESPVV STPTKSMQAL STVPLDWVTV PKLQGIFGAE R
//
  All links  
Ontology (2)   
   GO (2)   
Gene (4)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
   UniGene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (19)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (5)   
   SMART (2)   
Literature (1)   
   PubMed (1)   
All databases (28)   

Download RDF
DBGET integrated database retrieval system