CL12A_HUMAN
ID CL12A_HUMAN Reviewed; 265 AA.
AC Q5QGZ9; B2RA16; Q6P4H1; Q6RH77; Q6RH78; Q8TDQ6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=C-type lectin domain family 12 member A;
DE AltName: Full=C-type lectin-like molecule 1;
DE Short=CLL-1;
DE AltName: Full=Dendritic cell-associated lectin 2;
DE Short=DCAL-2;
DE AltName: Full=Myeloid inhibitory C-type lectin-like receptor;
DE Short=MICL;
DE AltName: CD_antigen=CD371;
GN Name=CLEC12A; Synonyms=CLL1, DCAL2, MICL;
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), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=15548716; DOI=10.1158/0008-5472.can-04-1659;
RA Bakker A.B.H., van den Oudenrijn S., Bakker A.Q., Feller N., van Meijer M.,
RA Bia J.A., Jongeneelen M.A.C., Visser T.J., Bijl N., Geuijen C.A.W.,
RA Marissen W.E., Radosevic K., Throsby M., Schuurhuis G.J.,
RA Ossenkoppele G.J., de Kruif J., Goudsmit J., Kruisbeek A.M.;
RT "C-type lectin-like molecule-1: a novel myeloid cell surface marker
RT associated with acute myeloid leukemia.";
RL Cancer Res. 64:8443-8450(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4), FUNCTION, INTERACTION
RP WITH PTPN6 AND PTPN11, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE
RP SPECIFICITY, AND VARIANT GLN-244.
RX PubMed=14739280; DOI=10.1074/jbc.m313127200;
RA Marshall A.S.J., Willment J.A., Lin H.-H., Williams D.L., Gordon S.,
RA Brown G.D.;
RT "Identification and characterization of a novel human myeloid inhibitory C-
RT type lectin-like receptor (MICL) that is predominantly expressed on
RT granulocytes and monocytes.";
RL J. Biol. Chem. 279:14792-14802(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND VARIANT GLN-244.
RX PubMed=16239426; DOI=10.1182/blood-2005-08-3264;
RA Chen C.-H., Floyd H., Olson N.E., Magaletti D., Li C., Draves K.,
RA Clark E.A.;
RT "Dendritic-cell-associated C-type lectin 2 (DCAL-2) alters dendritic-cell
RT maturation and cytokine production.";
RL Blood 107:1459-1467(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT GLN-244.
RA Zhang W., Wan T., Chen T., Cao X.;
RT "Novel human C-type lectin superfamily member CLL-1.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLN-244.
RC TISSUE=Lung;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLN-244.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5), AND VARIANT
RP GLN-244.
RC TISSUE=Blood;
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).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-98.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [10]
RP GLYCOSYLATION, INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16838277; DOI=10.1002/eji.200535628;
RA Marshall A.S.J., Willment J.A., Pyz E., Dennehy K.M., Reid D.M., Dri P.,
RA Gordon S., Wong S.Y.C., Brown G.D.;
RT "Human MICL (CLEC12A) is differentially glycosylated and is down-regulated
RT following cellular activation.";
RL Eur. J. Immunol. 36:2159-2169(2006).
CC -!- FUNCTION: Cell surface receptor that modulates signaling cascades and
CC mediates tyrosine phosphorylation of target MAP kinases.
CC {ECO:0000269|PubMed:14739280, ECO:0000269|PubMed:16239426}.
CC -!- SUBUNIT: Interacts with PTPN6 and PTPN11.
CC {ECO:0000269|PubMed:14739280}.
CC -!- INTERACTION:
CC Q5QGZ9; Q8NC01: CLEC1A; NbExp=3; IntAct=EBI-13335829, EBI-11996768;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14739280,
CC ECO:0000269|PubMed:15548716, ECO:0000269|PubMed:16239426,
CC ECO:0000269|PubMed:16838277}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:14739280, ECO:0000269|PubMed:15548716,
CC ECO:0000269|PubMed:16239426, ECO:0000269|PubMed:16838277}. Note=Ligand
CC binding leads to internalization.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=2; Synonyms=Alpha;
CC IsoId=Q5QGZ9-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q5QGZ9-1; Sequence=VSP_039854;
CC Name=3; Synonyms=Gamma;
CC IsoId=Q5QGZ9-3; Sequence=VSP_030031, VSP_030032;
CC Name=4; Synonyms=Beta;
CC IsoId=Q5QGZ9-4; Sequence=VSP_030030;
CC Name=5;
CC IsoId=Q5QGZ9-5; Sequence=VSP_030033;
CC -!- TISSUE SPECIFICITY: Detected in normal myeloid cells and in acute
CC myeloid leukemia cells. Detected in neutrophils, eosinophils, monocytes
CC and dendritic cells. Detected in spleen macrophage-rich red pulp and in
CC lymph node (at protein level). Detected in peripheral blood leukocytes,
CC dendritic cells, bone marrow, monocytes, mononuclear leukocytes and
CC macrophages. {ECO:0000269|PubMed:14739280, ECO:0000269|PubMed:15548716,
CC ECO:0000269|PubMed:16239426, ECO:0000269|PubMed:16838277}.
CC -!- INDUCTION: Down-regulated in activated leukocytes recruited to a site
CC of inflammation. {ECO:0000269|PubMed:16838277}.
CC -!- DOMAIN: Contains 1 copy of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
CC -!- PTM: Highly N-glycosylated. Glycosylation varies between cell types.
CC {ECO:0000269|PubMed:14739280, ECO:0000269|PubMed:16335952,
CC ECO:0000269|PubMed:16838277}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
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DR EMBL; AY547296; AAT11783.1; -; mRNA.
DR EMBL; AY498550; AAS00605.1; -; mRNA.
DR EMBL; AY498551; AAS00606.1; -; mRNA.
DR EMBL; AY498552; AAS00607.1; -; mRNA.
DR EMBL; AY426759; AAR84594.1; -; mRNA.
DR EMBL; AF247788; AAL95693.1; -; mRNA.
DR EMBL; AK314001; BAG36713.1; -; mRNA.
DR EMBL; AC091814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96133.1; -; Genomic_DNA.
DR EMBL; BC063424; AAH63424.1; -; mRNA.
DR EMBL; BC126289; AAI26290.1; -; mRNA.
DR EMBL; BC126291; AAI26292.1; -; mRNA.
DR CCDS; CCDS55803.1; -. [Q5QGZ9-1]
DR CCDS; CCDS73442.1; -. [Q5QGZ9-5]
DR CCDS; CCDS8608.1; -. [Q5QGZ9-2]
DR CCDS; CCDS8609.1; -. [Q5QGZ9-4]
DR RefSeq; NP_001193939.1; NM_001207010.1. [Q5QGZ9-1]
DR RefSeq; NP_001287659.1; NM_001300730.1. [Q5QGZ9-5]
DR RefSeq; NP_612210.4; NM_138337.5. [Q5QGZ9-2]
DR RefSeq; NP_963917.2; NM_201623.3. [Q5QGZ9-4]
DR RefSeq; XP_005253381.1; XM_005253324.2. [Q5QGZ9-2]
DR RefSeq; XP_011518872.1; XM_011520570.1. [Q5QGZ9-2]
DR AlphaFoldDB; Q5QGZ9; -.
DR SMR; Q5QGZ9; -.
DR BioGRID; 127754; 34.
DR IntAct; Q5QGZ9; 24.
DR STRING; 9606.ENSP00000347916; -.
DR GuidetoPHARMACOLOGY; 3081; -.
DR TCDB; 1.C.111.1.16; the regiiiGama (regiiiGama) family.
DR GlyGen; Q5QGZ9; 3 sites.
DR iPTMnet; Q5QGZ9; -.
DR PhosphoSitePlus; Q5QGZ9; -.
DR BioMuta; CLEC12A; -.
DR DMDM; 308153619; -.
DR jPOST; Q5QGZ9; -.
DR MassIVE; Q5QGZ9; -.
DR MaxQB; Q5QGZ9; -.
DR PaxDb; Q5QGZ9; -.
DR PeptideAtlas; Q5QGZ9; -.
DR PRIDE; Q5QGZ9; -.
DR ProteomicsDB; 63611; -. [Q5QGZ9-2]
DR ProteomicsDB; 63612; -. [Q5QGZ9-1]
DR ProteomicsDB; 63613; -. [Q5QGZ9-3]
DR ProteomicsDB; 63614; -. [Q5QGZ9-4]
DR ProteomicsDB; 63615; -. [Q5QGZ9-5]
DR ABCD; Q5QGZ9; 13 sequenced antibodies.
DR Antibodypedia; 11635; 333 antibodies from 32 providers.
DR DNASU; 160364; -.
DR Ensembl; ENST00000304361.9; ENSP00000302804.4; ENSG00000172322.14. [Q5QGZ9-2]
DR Ensembl; ENST00000350667.4; ENSP00000345448.4; ENSG00000172322.14. [Q5QGZ9-4]
DR Ensembl; ENST00000355690.8; ENSP00000347916.4; ENSG00000172322.14. [Q5QGZ9-1]
DR Ensembl; ENST00000434319.6; ENSP00000405244.2; ENSG00000172322.14. [Q5QGZ9-5]
DR GeneID; 160364; -.
DR KEGG; hsa:160364; -.
DR MANE-Select; ENST00000304361.9; ENSP00000302804.4; NM_138337.6; NP_612210.4.
DR UCSC; uc001qwq.3; human. [Q5QGZ9-2]
DR CTD; 160364; -.
DR DisGeNET; 160364; -.
DR GeneCards; CLEC12A; -.
DR HGNC; HGNC:31713; CLEC12A.
DR HPA; ENSG00000172322; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 612088; gene.
DR neXtProt; NX_Q5QGZ9; -.
DR OpenTargets; ENSG00000172322; -.
DR PharmGKB; PA142672094; -.
DR VEuPathDB; HostDB:ENSG00000172322; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000162719; -.
DR InParanoid; Q5QGZ9; -.
DR OMA; TWMWHED; -.
DR OrthoDB; 1201127at2759; -.
DR TreeFam; TF336674; -.
DR PathwayCommons; Q5QGZ9; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q5QGZ9; -.
DR BioGRID-ORCS; 160364; 11 hits in 1059 CRISPR screens.
DR ChiTaRS; CLEC12A; human.
DR GeneWiki; CLEC12A; -.
DR GenomeRNAi; 160364; -.
DR Pharos; Q5QGZ9; Tbio.
DR PRO; PR:Q5QGZ9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q5QGZ9; protein.
DR Bgee; ENSG00000172322; Expressed in monocyte and 110 other tissues.
DR ExpressionAtlas; Q5QGZ9; baseline and differential.
DR Genevisible; Q5QGZ9; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0030545; F:signaling receptor regulator activity; IEA:InterPro.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd03593; CLECT_NK_receptors_like; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR042916; CLEC12A/B.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR033992; NKR-like_CTLD.
DR PANTHER; PTHR47647; PTHR47647; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein; Lectin;
KW Membrane; Receptor; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..265
FT /note="C-type lectin domain family 12 member A"
FT /id="PRO_0000313578"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..265
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 140..249
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MOTIF 5..10
FT /note="ITIM motif"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 227..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT VAR_SEQ 1
FT /note="M -> MWIDFFTYSSM (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15548716"
FT /id="VSP_039854"
FT VAR_SEQ 31..64
FT /note="APPAPSHVWRPAALFLTLLCLLLLIGLGVLASMF -> V (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:14739280"
FT /id="VSP_030030"
FT VAR_SEQ 64..81
FT /note="FHVTLKIEMKKMNKLQNI -> CMYCPCFGQEEVSRISNI (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14739280"
FT /id="VSP_030031"
FT VAR_SEQ 82..265
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14739280"
FT /id="VSP_030032"
FT VAR_SEQ 214..265
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030033"
FT VARIANT 244
FT /note="K -> Q (in dbSNP:rs479499)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:14739280, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16239426, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.7"
FT /id="VAR_037669"
SQ SEQUENCE 265 AA; 30762 MW; 4255FF1EA9F0D4B1 CRC64;
MSEEVTYADL QFQNSSEMEK IPEIGKFGEK APPAPSHVWR PAALFLTLLC LLLLIGLGVL
ASMFHVTLKI EMKKMNKLQN ISEELQRNIS LQLMSNMNIS NKIRNLSTTL QTIATKLCRE
LYSKEQEHKC KPCPRRWIWH KDSCYFLSDD VQTWQESKMA CAAQNASLLK INNKNALEFI
KSQSRSYDYW LGLSPEEDST RGMRVDNIIN SSAWVIRNAP DLNNMYCGYI NRLYVQYYHC
TYKKRMICEK MANPVQLGST YFREA
