EVA1C_MOUSE
ID EVA1C_MOUSE Reviewed; 440 AA.
AC P58659; A2RSZ2; Q497W3; Q9D4L3;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein eva-1 homolog C;
DE AltName: Full=Protein FAM176C;
DE Flags: Precursor;
GN Name=Eva1c; Synonyms=Fam176c;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 3).
RC STRAIN=C57BL/6J; TISSUE=Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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: Binds heparin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P58659-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P58659-2; Sequence=VSP_026601;
CC Name=3;
CC IsoId=P58659-3; Sequence=VSP_026600;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
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; AF358257; AAL40410.1; -; mRNA.
DR EMBL; AK016443; BAB30238.1; -; mRNA.
DR EMBL; BC100350; AAI00351.1; -; mRNA.
DR EMBL; BC132305; AAI32306.1; -; mRNA.
DR CCDS; CCDS28319.1; -. [P58659-2]
DR CCDS; CCDS57038.1; -. [P58659-1]
DR CCDS; CCDS84261.1; -. [P58659-3]
DR RefSeq; NP_001186139.1; NM_001199210.2. [P58659-1]
DR RefSeq; NP_001303689.1; NM_001316760.1. [P58659-3]
DR RefSeq; NP_001303690.1; NM_001316761.1.
DR RefSeq; NP_081903.1; NM_027627.3. [P58659-2]
DR RefSeq; XP_017172620.1; XM_017317131.1. [P58659-3]
DR RefSeq; XP_017172621.1; XM_017317132.1. [P58659-3]
DR AlphaFoldDB; P58659; -.
DR SMR; P58659; -.
DR GlyGen; P58659; 3 sites.
DR iPTMnet; P58659; -.
DR PhosphoSitePlus; P58659; -.
DR MaxQB; P58659; -.
DR PaxDb; P58659; -.
DR PRIDE; P58659; -.
DR ProteomicsDB; 275897; -. [P58659-1]
DR ProteomicsDB; 275898; -. [P58659-2]
DR ProteomicsDB; 275899; -. [P58659-3]
DR Antibodypedia; 2587; 58 antibodies from 12 providers.
DR Ensembl; ENSMUST00000037539; ENSMUSP00000036695; ENSMUSG00000039903. [P58659-1]
DR Ensembl; ENSMUST00000099543; ENSMUSP00000097141; ENSMUSG00000039903. [P58659-2]
DR GeneID; 70967; -.
DR KEGG; mmu:70967; -.
DR UCSC; uc007zwp.2; mouse. [P58659-1]
DR UCSC; uc007zwq.2; mouse. [P58659-2]
DR CTD; 59271; -.
DR MGI; MGI:1918217; Eva1c.
DR VEuPathDB; HostDB:ENSMUSG00000039903; -.
DR GeneTree; ENSGT00940000162103; -.
DR HOGENOM; CLU_050537_0_1_1; -.
DR InParanoid; P58659; -.
DR OMA; LWTRRMN; -.
DR OrthoDB; 548674at2759; -.
DR PhylomeDB; P58659; -.
DR TreeFam; TF328177; -.
DR BioGRID-ORCS; 70967; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Eva1c; mouse.
DR PRO; PR:P58659; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P58659; protein.
DR Bgee; ENSMUSG00000039903; Expressed in lumbar dorsal root ganglion and 114 other tissues.
DR ExpressionAtlas; P58659; baseline and differential.
DR Genevisible; P58659; MM.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; ISO:MGI.
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 Pfam; PF14851; FAM176; 1.
DR Pfam; PF02140; Gal_Lectin; 2.
DR PROSITE; PS50228; SUEL_LECTIN; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Glycoprotein; Lectin; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..48
FT /evidence="ECO:0000255"
FT CHAIN 49..440
FT /note="Protein eva-1 homolog C"
FT /id="PRO_0000017672"
FT TOPO_DOM 49..321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..440
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 364..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..383
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 109
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 1..95
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026600"
FT VAR_SEQ 212..259
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026601"
FT CONFLICT 347
FT /note="T -> R (in Ref. 3; AAI32306)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="A -> S (in Ref. 1; AAL40410)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="Q -> E (in Ref. 3; AAI32306)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 440 AA; 49287 MW; AD4782A666D90EF0 CRC64;
MLLPGHPRPP PAPQSAQNQG LRRQVEPPGQ LLRLFYCTVL VCSKETSALT DFSGYLTKLL
QNHTAYACDG DYLNLQCPRH STISVQSAFY GQDYQMCSSQ EPISQREDNL TCVASTTLQK
VLDECQNQRA CHLLVNSRVF GPDLCPGSSK YLLVSFKCQP NELKNKTVCE NQELKLHCHE
SKFLNIYSAA YGRRTQQRDI CSSGAELLPP FDCLSYTALQ VLSRRCYGKQ RCKVLVDNYH
FGSPCLPGVK KYLTVAYACV PKNILTAVDP AVANLNPSLK KDDEHGITFN PSGSRVVRKD
GVIVSNSLAA FAYIRAHPER AALLFMSSVC IGLLLTLCAL VIRVSCTKDF RELRQGREHL
VLGSDKAEED SEEDLEEEDS SDSQFPEELS RFCRTSYPAY SSIEAAELAE RIERREQVIQ
EIWMNSGLDS SLPRNVGHFY
