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ITLN2_HUMAN
ID   ITLN2_HUMAN             Reviewed;         325 AA.
AC   Q8WWU7; Q17RR2; Q5VYI0;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Intelectin-2;
DE   AltName: Full=Endothelial lectin HL-2;
DE   Flags: Precursor;
GN   Name=ITLN2; ORFNames=UNQ2789/PRO7179;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Small intestine;
RX   PubMed=11181563; DOI=10.1093/glycob/11.1.65;
RA   Lee J.K., Schnee J., Pang M., Wolfert M., Baum L.G., Moremen K.W.,
RA   Pierce M.;
RT   "Human homologs of the Xenopus oocyte cortical granule lectin XL35.";
RL   Glycobiology 11:65-73(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT HIS-103.
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: May play a role in the defense system against pathogens.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8WWU7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8WWU7-2; Sequence=VSP_055093;
CC   -!- TISSUE SPECIFICITY: Expressed only in the small intestine.
CC       {ECO:0000269|PubMed:11181563}.
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DR   EMBL; AY065973; AAL58074.1; -; mRNA.
DR   EMBL; AY358905; AAQ89264.1; -; mRNA.
DR   EMBL; AL354714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL591806; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471121; EAW52685.1; -; Genomic_DNA.
DR   EMBL; BC117225; AAI17226.1; -; mRNA.
DR   EMBL; BC143341; AAI43342.1; -; mRNA.
DR   CCDS; CCDS1212.1; -. [Q8WWU7-1]
DR   RefSeq; NP_543154.1; NM_080878.2. [Q8WWU7-1]
DR   RefSeq; XP_011507512.1; XM_011509210.1. [Q8WWU7-1]
DR   RefSeq; XP_011507513.1; XM_011509211.1.
DR   AlphaFoldDB; Q8WWU7; -.
DR   SMR; Q8WWU7; -.
DR   BioGRID; 126772; 61.
DR   IntAct; Q8WWU7; 3.
DR   STRING; 9606.ENSP00000357008; -.
DR   iPTMnet; Q8WWU7; -.
DR   PhosphoSitePlus; Q8WWU7; -.
DR   BioMuta; ITLN2; -.
DR   DMDM; 55976554; -.
DR   EPD; Q8WWU7; -.
DR   jPOST; Q8WWU7; -.
DR   MassIVE; Q8WWU7; -.
DR   PaxDb; Q8WWU7; -.
DR   PeptideAtlas; Q8WWU7; -.
DR   PRIDE; Q8WWU7; -.
DR   ProteomicsDB; 74936; -. [Q8WWU7-1]
DR   Antibodypedia; 1671; 102 antibodies from 21 providers.
DR   DNASU; 142683; -.
DR   Ensembl; ENST00000368029.4; ENSP00000357008.3; ENSG00000158764.7. [Q8WWU7-1]
DR   GeneID; 142683; -.
DR   KEGG; hsa:142683; -.
DR   MANE-Select; ENST00000368029.4; ENSP00000357008.3; NM_080878.3; NP_543154.1.
DR   UCSC; uc001fxd.4; human. [Q8WWU7-1]
DR   CTD; 142683; -.
DR   GeneCards; ITLN2; -.
DR   HGNC; HGNC:20599; ITLN2.
DR   HPA; ENSG00000158764; Tissue enriched (intestine).
DR   MIM; 609874; gene.
DR   neXtProt; NX_Q8WWU7; -.
DR   OpenTargets; ENSG00000158764; -.
DR   PharmGKB; PA134879128; -.
DR   VEuPathDB; HostDB:ENSG00000158764; -.
DR   eggNOG; ENOG502QU6C; Eukaryota.
DR   GeneTree; ENSGT00940000163851; -.
DR   HOGENOM; CLU_066147_0_0_1; -.
DR   InParanoid; Q8WWU7; -.
DR   OMA; THVKSSC; -.
DR   OrthoDB; 754383at2759; -.
DR   PhylomeDB; Q8WWU7; -.
DR   TreeFam; TF328530; -.
DR   PathwayCommons; Q8WWU7; -.
DR   SignaLink; Q8WWU7; -.
DR   BioGRID-ORCS; 142683; 11 hits in 1059 CRISPR screens.
DR   ChiTaRS; ITLN2; human.
DR   GenomeRNAi; 142683; -.
DR   Pharos; Q8WWU7; Tbio.
DR   PRO; PR:Q8WWU7; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q8WWU7; protein.
DR   Bgee; ENSG00000158764; Expressed in duodenum and 66 other tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070492; F:oligosaccharide binding; IBA:GO_Central.
DR   Gene3D; 3.90.215.10; -; 1.
DR   InterPro; IPR036056; Fibrinogen-like_C.
DR   InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
DR   InterPro; IPR002181; Fibrinogen_a/b/g_C_dom.
DR   SUPFAM; SSF56496; SSF56496; 1.
DR   PROSITE; PS51406; FIBRINOGEN_C_2; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Calcium; Disulfide bond; Lectin; Metal-binding;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..325
FT                   /note="Intelectin-2"
FT                   /id="PRO_0000009149"
FT   DOMAIN          44..267
FT                   /note="Fibrinogen C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00739"
FT   BINDING         98
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT   BINDING         99
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT   BINDING         101
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT   BINDING         104
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT   BINDING         109
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT   BINDING         110
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT   BINDING         145
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT   BINDING         272
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT   BINDING         274..275
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT   BINDING         274
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT   BINDING         294
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT   DISULFID        53..82
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT   DISULFID        106..292
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT   DISULFID        211..271
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT   DISULFID        263..277
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWA0"
FT   VAR_SEQ         26
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_055093"
FT   VARIANT         103
FT                   /note="R -> H (in dbSNP:rs6680969)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_019926"
FT   VARIANT         171
FT                   /note="Q -> R (in dbSNP:rs12090411)"
FT                   /id="VAR_049076"
SQ   SEQUENCE   325 AA;  36212 MW;  283C9A12AED2EBFC CRC64;
     MLSMLRTMTR LCFLLFFSVA TSGCSAAAAS SLEMLSREFE TCAFSFSSLP RSCKEIKERC
     HSAGDGLYFL RTKNGVVYQT FCDMTSGGGG WTLVASVHEN DMRGKCTVGD RWSSQQGNKA
     DYPEGDGNWA NYNTFGSAEA ATSDDYKNPG YYDIQAKDLG IWHVPNKSPM QHWRNSALLR
     YRTNTGFLQR LGHNLFGIYQ KYPVKYRSGK CWNDNGPAIP VVYDFGDAKK TASYYSPYGQ
     REFVAGFVQF RVFNNERAAN ALCAGIKVTG CNTEHHCIGG GGFFPQGKPR QCGDFSAFDW
     DGYGTHVKSS CSREITEAAV LLFYR
 
 
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