ID EVA1C_HUMAN Reviewed; 441 AA. AC P58658; A6ND58; Q8IXZ0; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 1. DT 24-JAN-2024, entry version 166. DE RecName: Full=Protein eva-1 homolog C; DE AltName: Full=Protein FAM176C; DE AltName: Full=SUE21; DE Flags: Precursor; GN Name=EVA1C; Synonyms=C21orf63, C21orf64, FAM176C; GN ORFNames=PRED34, UNQ2504/PRO5993; 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] (ISOFORMS 1 AND 2). RX PubMed=11707072; DOI=10.1006/geno.2001.6640; RA Reymond A., Friedli M., Neergaard Henrichsen C., Chapot F., Deutsch S., RA Ucla C., Rossier C., Lyle R., Guipponi M., Antonarakis S.E.; RT "From PREDs and open reading frames to cDNA isolation: revisiting the human RT chromosome 21 transcription map."; RL Genomics 78:46-54(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=10830953; DOI=10.1038/35012518; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U., RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). 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 3). RC TISSUE=Hippocampus; 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 [6] RP TISSUE SPECIFICITY, AND FUNCTION. RX PubMed=19470522; DOI=10.1093/jb/mvp079; RA Mitsunaga K., Harada-Itadani J., Shikanai T., Tateno H., Ikehara Y., RA Hirabayashi J., Narimatsu H., Angata T.; RT "Human C21orf63 is a heparin-binding protein."; RL J. Biochem. 146:369-373(2009). CC -!- FUNCTION: Binds heparin. {ECO:0000269|PubMed:19470522}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I CC membrane protein {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P58658-1; Sequence=Displayed; CC Name=2; CC IsoId=P58658-2; Sequence=VSP_003103, VSP_003104; CC Name=3; CC IsoId=P58658-3; Sequence=VSP_055198; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:19470522}. CC -!- SIMILARITY: Belongs to the EVA1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF358258; AAL40411.1; -; mRNA. DR EMBL; AY040087; AAK74135.1; -; mRNA. DR EMBL; AY358787; AAQ89147.1; -; mRNA. DR EMBL; AP000269; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000270; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000271; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP000272; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471079; EAX09872.1; -; Genomic_DNA. DR EMBL; BC038710; AAH38710.1; -; mRNA. DR CCDS; CCDS13614.1; -. [P58658-1] DR CCDS; CCDS68186.1; -. [P58658-3] DR RefSeq; NP_001273485.1; NM_001286556.1. [P58658-3] DR RefSeq; NP_478067.2; NM_058187.4. [P58658-1] DR AlphaFoldDB; P58658; -. DR SMR; P58658; -. DR BioGRID; 121863; 74. DR IntAct; P58658; 29. DR STRING; 9606.ENSP00000300255; -. DR GlyCosmos; P58658; 2 sites, No reported glycans. DR GlyGen; P58658; 2 sites. DR iPTMnet; P58658; -. DR PhosphoSitePlus; P58658; -. DR BioMuta; EVA1C; -. DR EPD; P58658; -. DR MassIVE; P58658; -. DR PaxDb; 9606-ENSP00000300255; -. DR PeptideAtlas; P58658; -. DR ProteomicsDB; 57094; -. [P58658-1] DR ProteomicsDB; 882; -. DR Antibodypedia; 2587; 69 antibodies from 13 providers. DR DNASU; 59271; -. DR Ensembl; ENST00000300255.7; ENSP00000300255.2; ENSG00000166979.13. [P58658-1] DR Ensembl; ENST00000382699.7; ENSP00000372146.3; ENSG00000166979.13. [P58658-3] DR GeneID; 59271; -. DR KEGG; hsa:59271; -. DR MANE-Select; ENST00000300255.7; ENSP00000300255.2; NM_058187.5; NP_478067.2. DR UCSC; uc002ypr.3; human. [P58658-1] DR AGR; HGNC:13239; -. DR CTD; 59271; -. DR DisGeNET; 59271; -. DR GeneCards; EVA1C; -. DR HGNC; HGNC:13239; EVA1C. DR HPA; ENSG00000166979; Low tissue specificity. DR neXtProt; NX_P58658; -. DR OpenTargets; ENSG00000166979; -. DR PharmGKB; PA25858; -. DR VEuPathDB; HostDB:ENSG00000166979; -. DR eggNOG; KOG4729; Eukaryota. DR GeneTree; ENSGT00940000162103; -. DR HOGENOM; CLU_050537_0_1_1; -. DR InParanoid; P58658; -. DR OMA; LWTRRMN; -. DR OrthoDB; 56324at2759; -. DR PhylomeDB; P58658; -. DR TreeFam; TF328177; -. DR PathwayCommons; P58658; -. DR SignaLink; P58658; -. DR BioGRID-ORCS; 59271; 8 hits in 1134 CRISPR screens. DR ChiTaRS; EVA1C; human. DR GenomeRNAi; 59271; -. DR Pharos; P58658; Tbio. DR PRO; PR:P58658; -. DR Proteomes; UP000005640; Chromosome 21. DR RNAct; P58658; Protein. DR Bgee; ENSG00000166979; Expressed in olfactory segment of nasal mucosa and 167 other cell types or tissues. DR ExpressionAtlas; P58658; baseline and differential. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0008201; F:heparin binding; IMP:UniProtKB. DR CDD; cd22828; Gal_Rha_Lectin_EVA1_EVA1C_rpt1; 1. DR CDD; cd22829; Gal_Rha_Lectin_EVA1_EVA1C_rpt2; 1. DR Gene3D; 2.60.120.740; -; 2. DR InterPro; IPR039500; EVA1_dom. DR InterPro; IPR000922; Lectin_gal-bd_dom. DR InterPro; IPR043159; Lectin_gal-bd_sf. DR PANTHER; PTHR46780; PROTEIN EVA-1; 1. DR PANTHER; PTHR46780:SF4; PROTEIN EVA-1 HOMOLOG C; 1. DR Pfam; PF14851; FAM176; 1. DR Pfam; PF02140; Gal_Lectin; 2. DR PROSITE; PS50228; SUEL_LECTIN; 2. DR Genevisible; P58658; HS. PE 2: Evidence at transcript level; KW Alternative splicing; Glycoprotein; Lectin; Membrane; Reference proteome; KW Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..48 FT /evidence="ECO:0000255" FT CHAIN 49..441 FT /note="Protein eva-1 homolog C" FT /id="PRO_0000017671" FT TOPO_DOM 49..322 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 323..343 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 344..441 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 67..159 FT /note="SUEL-type lectin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260" FT DOMAIN 168..260 FT /note="SUEL-type lectin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00260" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 362..390 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 368..385 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 62 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 165 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 54..69 FT /note="GYLTKLLQNHTTYACD -> EGAGRMPEPAGLPPPG (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11707072" FT /id="VSP_003103" FT VAR_SEQ 70..441 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11707072" FT /id="VSP_003104" FT VAR_SEQ 285..287 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_055198" FT CONFLICT 19 FT /note="P -> H (in Ref. 5; AAH38710)" FT /evidence="ECO:0000305" FT CONFLICT 284..286 FT /note="Missing (in Ref. 5; AAH38710)" FT /evidence="ECO:0000305" SQ SEQUENCE 441 AA; 49483 MW; 31B2C9C12915ACD4 CRC64; MLLPGRARQP PTPQPVQHPG LRRQVEPPGQ LLRLFYCTVL VCSKEISALT DFSGYLTKLL QNHTTYACDG DYLNLQCPRH STISVQSAFY GQDYQMCSSQ KPASQREDSL TCVAATTFQK VLDECQNQRA CHLLVNSRVF GPDLCPGSSK YLLVSFKCQP NELKNKTVCE DQELKLHCHE SKFLNIYSAT YGRRTQERDI CSSKAERLPP FDCLSYSALQ VLSRRCYGKQ RCKIIVNNHH FGSPCLPGVK KYLTVTYACV PKNILTAIDP AIANLKPSLK QKDGEYGINF DPSGSKVLRK DGILVSNSLA AFAYIRAHPE RAALLFVSSV CIGLALTLCA LVIRESCAKD FRDLQLGREQ LVPGSDKVEE DSEDEEEEED PSESDFPGEL SGFCRTSYPI YSSIEAAELA ERIERREQII QEIWMNSGLD TSLPRNMGQF Y //