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ITIH5_PONAB
ID   ITIH5_PONAB             Reviewed;         940 AA.
AC   Q5RER0;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Inter-alpha-trypsin inhibitor heavy chain H5;
DE            Short=ITI heavy chain H5;
DE            Short=ITI-HC5;
DE            Short=Inter-alpha-inhibitor heavy chain 5;
DE   Flags: Precursor;
GN   Name=ITIH5;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as a tumor suppressor. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ITIH family. {ECO:0000305}.
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DR   EMBL; CR857457; CAH89747.1; -; mRNA.
DR   RefSeq; NP_001124799.1; NM_001131327.1.
DR   AlphaFoldDB; Q5RER0; -.
DR   SMR; Q5RER0; -.
DR   GeneID; 100171653; -.
DR   KEGG; pon:100171653; -.
DR   CTD; 80760; -.
DR   eggNOG; ENOG502QPS2; Eukaryota.
DR   InParanoid; Q5RER0; -.
DR   OrthoDB; 955432at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030212; P:hyaluronan metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.410; -; 1.
DR   InterPro; IPR010600; ITI_HC_C.
DR   InterPro; IPR013694; VIT.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF06668; ITI_HC_C; 1.
DR   Pfam; PF08487; VIT; 1.
DR   Pfam; PF00092; VWA; 1.
DR   SMART; SM00609; VIT; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   PROSITE; PS51468; VIT; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Protease inhibitor; Reference proteome; Secreted;
KW   Serine protease inhibitor; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..940
FT                   /note="Inter-alpha-trypsin inhibitor heavy chain H5"
FT                   /id="PRO_0000331410"
FT   DOMAIN          35..161
FT                   /note="VIT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00801"
FT   DOMAIN          295..478
FT                   /note="VWFA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00219"
FT   REGION          117..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..227
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          541..571
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        405..423
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        508
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        774
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        793
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        860
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   940 AA;  105177 MW;  1B4399590E763799 CRC64;
     MLLLLGLCLG LSQCVGSQEE AQSWGHSSEQ DGLRVPRQVR LLQRLKTKPL MTEFSVKSTI
     ISRYAFTTVS CRMLNRASED QDVEFQMQIP AAAFITNFTM LIGEKVYQGE ITEREKKSGD
     RVKEKRNKTT EENGEKGTEI FRASAVIPSK DKAAFFLSYE ELLQRRLGKY EHSISVRPQQ
     LSGRLSVDVN ILESAGIASL EVLPLRNSRQ RGSGRGEDDS GPPPSTVINQ NETFANIIFK
     PTVVQQARIA QNGILGDFII RYDVNREQSI GDIQVLNGYF VHYFAPKDLP PLPKNVVFVL
     DSSASMVGTK LRQTKDALFT ILHDLRPQDH FSIIGFSNRI KVWKDHFDIS HSRQHQGWQS
     VHSPYVAHWR HRHQRGLAEG HQAPQQVRGP QWHWRPERVP HCLPDGWEAH GRGDAHPQDP
     QQHPRGRPRP SLHLHIGIGN DVDFRLLEKL SLENCGLTRR VHEEEDAGSQ LIGFYDEIRT
     PLLSDIRIDY PPSSVVQATK TLFPNYFNGS EIIIAGKLVD RKLDHLHVEV TASNSKKFVI
     PKTDVPVGPQ KAGKDVTGSP RPGGDGERNP NHIERLWSYL TTKELLSSWL QSDDEPEKER
     LRQRAQALAV SYRFLTPFTS MKLRGPVPRT DGLKEAHGMS AAMGPEPVVQ SVRGAGTQPG
     PLLKKPYQPR IKISKTSVDG DPHFVVDFPL SKLTVCFNID GQPGDILRLV SDHMDSGVTV
     NGELIGAPPN GHKKQRTYFR TITILINKPE RSYLEITPSR VILDGGDRLV LPCNQSVVVG
     SRGLEVSVSA NANVTVTIQG SIAFVIPIHL YKKPAPFQRH HLGFYIANSE GLSSNCHGLL
     GQFLNQDARL TEDPAGPSQN LTHSLLLQVG EGPEAVLTVK GRQVPVVWKQ RKIYNGEEQI
     DCWFARNNAA KLIDGEYKDY LASHPFDTGM TLGRGMSREL
 
 
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