TEFF2_HUMAN
ID TEFF2_HUMAN Reviewed; 374 AA.
AC Q9UIK5; Q2FA44; Q4ZFW4; Q53H90; Q53RE1; Q8N2R5; Q9NR15; Q9NSS5; Q9P2Y9;
AC Q9UK65;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Tomoregulin-2;
DE Short=TR-2;
DE AltName: Full=Hyperplastic polyposis protein 1;
DE AltName: Full=Transmembrane protein with EGF-like and two follistatin-like domains;
DE Flags: Precursor;
GN Name=TMEFF2; Synonyms=HPP1, TENB2, TPEF; ORFNames=UNQ178/PRO204;
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), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10903839; DOI=10.1006/geno.2000.6228;
RA Horie M., Mitsumoto Y., Kyushiki H., Kanemoto N., Watanabe A.,
RA Taniguchi Y., Nishino N., Okamoto T., Kondo M., Mori T., Noguchi K.,
RA Nakamura Y., Takahashi E., Tanigami A.;
RT "Identification and characterization of TMEFF2, a novel survival factor for
RT hippocampal and mesencephalic neurons.";
RL Genomics 67:146-152(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA]
RP OF 1-57, INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10987305;
RA Liang G., Robertson K.D., Talmadge C., Sumegi J., Jones P.A.;
RT "The gene for a novel transmembrane protein containing epidermal growth
RT factor and follistatin domains is frequently hypermethylated in human tumor
RT cells.";
RL Cancer Res. 60:4907-4912(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Prostatic carcinoma;
RX PubMed=11668495; DOI=10.1002/ijc.1450;
RA Glynne-Jones E., Harper M.E., Seery L.T., James R., Anglin I., Morgan H.E.,
RA Taylor K.M., Gee J.M., Nicholson R.I.;
RT "TENB2, a proteoglycan identified in prostate cancer that is associated
RT with disease progression and androgen independence.";
RL Int. J. Cancer 94:178-184(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RX PubMed=16439095; DOI=10.1016/j.ygeno.2005.12.004;
RA Quayle S.N., Sadar M.D.;
RT "A truncated isoform of TMEFF2 encodes a secreted protein in prostate
RT cancer cells.";
RL Genomics 87:633-637(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-360.
RX PubMed=10600548; DOI=10.1006/bbrc.1999.1873;
RA Uchida T., Wada K., Akamatsu T., Yonezawa M., Noguchi H., Mizoguchi A.,
RA Kasuga M., Sakamoto C.;
RT "A novel epidermal growth factor-like molecule containing two follistatin
RT modules stimulates tyrosine phosphorylation of erbB-4 in MKN28 gastric
RT cancer cells.";
RL Biochem. Biophys. Res. Commun. 266:593-602(1999).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57, TISSUE SPECIFICITY, AND
RP INDUCTION.
RC TISSUE=Colon;
RX PubMed=11120884; DOI=10.1073/pnas.98.1.265;
RA Young J., Biden K.G., Simms L.A., Huggard P., Karamatic R., Eyre H.J.,
RA Sutherland G.R., Herath N., Barker M., Anderson G.J., Fitzpatrick D.R.,
RA Ramm G.A., Jass J.R., Leggett B.A.;
RT "HPP1: a transmembrane protein-encoding gene commonly methylated in
RT colorectal polyps and cancers.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:265-270(2001).
RN [14]
RP PROTEIN SEQUENCE OF 41-55.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [15]
RP TISSUE SPECIFICITY.
RX PubMed=16805794; DOI=10.1111/j.1471-4159.2006.03801.x;
RA Siegel D.A., Davies P., Dobrenis K., Huang M.;
RT "Tomoregulin-2 is found extensively in plaques in Alzheimer's disease
RT brain.";
RL J. Neurochem. 98:34-44(2006).
RN [16]
RP CLEAVAGE, AND FUNCTION.
RX PubMed=17942404; DOI=10.1074/jbc.m702170200;
RA Ali N., Knaeuper V.;
RT "Phorbol ester-induced shedding of the prostate cancer marker transmembrane
RT protein with epidermal growth factor and two follistatin motifs 2 is
RT mediated by the disintegrin and metalloproteinase-17.";
RL J. Biol. Chem. 282:37378-37388(2007).
RN [17]
RP GLYCOSYLATION AT ASN-204.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
CC -!- FUNCTION: May be a survival factor for hippocampal and mesencephalic
CC neurons. The shedded form up-regulates cancer cell proliferation,
CC probably by promoting ERK1/2 phosphorylation.
CC {ECO:0000269|PubMed:10903839, ECO:0000269|PubMed:17942404}.
CC -!- INTERACTION:
CC Q9UIK5; PRO_0000000090 [P05067]: APP; NbExp=3; IntAct=EBI-11423693, EBI-21194918;
CC Q9UIK5; O75031: HSF2BP; NbExp=3; IntAct=EBI-11423693, EBI-7116203;
CC Q9UIK5; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-11423693, EBI-22310682;
CC Q9UIK5; Q7Z5B4-5: RIC3; NbExp=3; IntAct=EBI-11423693, EBI-12375429;
CC Q9UIK5; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-11423693, EBI-10982110;
CC Q9UIK5; P34981: TRHR; NbExp=3; IntAct=EBI-11423693, EBI-18055230;
CC Q9UIK5; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-11423693, EBI-2819725;
CC Q9UIK5; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-11423693, EBI-12837904;
CC Q9UIK5-2; P55212: CASP6; NbExp=3; IntAct=EBI-25835153, EBI-718729;
CC Q9UIK5-2; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-25835153, EBI-5280197;
CC Q9UIK5-2; P62826: RAN; NbExp=3; IntAct=EBI-25835153, EBI-286642;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Membrane {ECO:0000305}; Single-pass
CC type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Membrane {ECO:0000305}; Single-pass
CC type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UIK5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UIK5-2; Sequence=VSP_014312, VSP_014313;
CC Name=3; Synonyms=TMEFF2-S;
CC IsoId=Q9UIK5-3; Sequence=VSP_024973, VSP_024974;
CC -!- TISSUE SPECIFICITY: Highly expressed in adult and fetal brain, spinal
CC cord and prostate. Expressed in all brain regions except the pituitary
CC gland, with highest levels in amygdala and corpus callosum. Expressed
CC in the pericryptal myofibroblasts and other stromal cells of normal
CC colonic mucosa. Expressed in prostate carcinoma. Down-regulated in
CC colorectal cancer. Present in Alzheimer disease plaques (at protein
CC level). Isoform 3 is expressed weakly in testis and at high levels in
CC normal and cancerous prostate. {ECO:0000269|PubMed:10903839,
CC ECO:0000269|PubMed:10987305, ECO:0000269|PubMed:11120884,
CC ECO:0000269|PubMed:11668495, ECO:0000269|PubMed:16439095,
CC ECO:0000269|PubMed:16805794}.
CC -!- INDUCTION: Down-regulated in tumor cell lines in response to a high
CC level of methylation in the 5' region. The CpG island methylation
CC correlates with TMEFF2 silencing in tumor cell lines.
CC {ECO:0000269|PubMed:10987305, ECO:0000269|PubMed:11120884}.
CC -!- PTM: N-glycosylated. Contains chondroitin sulfate glycosaminoglycans.
CC {ECO:0000269|PubMed:11668495, ECO:0000269|PubMed:19139490}.
CC -!- PTM: A soluble form (TMEFF2-ECD) is produced by proteolytic shedding.
CC This shedding can be induced by phorbol ester or pro-inflammatory
CC cytokines such as TNFalpha, and is mediated by ADAM17.
CC -!- SIMILARITY: Belongs to the tomoregulin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA90820.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Mitochondrial contamination starting in position 361.; Evidence={ECO:0000305};
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DR EMBL; AB017269; BAA87897.1; -; mRNA.
DR EMBL; AF242221; AAG49451.1; -; Genomic_DNA.
DR EMBL; AF242222; AAG49452.1; -; mRNA.
DR EMBL; AF179274; AAD55776.2; -; mRNA.
DR EMBL; DQ133599; AAZ43216.1; -; mRNA.
DR EMBL; AY358907; AAQ89266.1; -; mRNA.
DR EMBL; AK074507; BAC11030.1; -; mRNA.
DR EMBL; CR457390; CAG33671.1; -; mRNA.
DR EMBL; AK222691; BAD96411.1; -; mRNA.
DR EMBL; AL157430; CAB75654.1; -; mRNA.
DR EMBL; AC092644; AAY14874.1; -; Genomic_DNA.
DR EMBL; AC098617; AAX88893.1; -; Genomic_DNA.
DR EMBL; BC008973; AAH08973.1; -; mRNA.
DR EMBL; AB004064; BAA90820.1; ALT_TERM; mRNA.
DR EMBL; AF264150; AAF91397.1; -; Genomic_DNA.
DR CCDS; CCDS2314.1; -. [Q9UIK5-1]
DR CCDS; CCDS82547.1; -. [Q9UIK5-3]
DR CCDS; CCDS82548.1; -. [Q9UIK5-2]
DR PIR; T46914; T46914.
DR RefSeq; NP_001292063.1; NM_001305134.1. [Q9UIK5-2]
DR RefSeq; NP_001292074.1; NM_001305145.1. [Q9UIK5-3]
DR RefSeq; NP_057276.2; NM_016192.3. [Q9UIK5-1]
DR AlphaFoldDB; Q9UIK5; -.
DR SMR; Q9UIK5; -.
DR BioGRID; 117189; 12.
DR IntAct; Q9UIK5; 14.
DR MINT; Q9UIK5; -.
DR STRING; 9606.ENSP00000272771; -.
DR MEROPS; I01.969; -.
DR MEROPS; I01.978; -.
DR GlyGen; Q9UIK5; 3 sites.
DR iPTMnet; Q9UIK5; -.
DR PhosphoSitePlus; Q9UIK5; -.
DR BioMuta; TMEFF2; -.
DR DMDM; 71153590; -.
DR MassIVE; Q9UIK5; -.
DR PaxDb; Q9UIK5; -.
DR PeptideAtlas; Q9UIK5; -.
DR PRIDE; Q9UIK5; -.
DR ProteomicsDB; 84539; -. [Q9UIK5-1]
DR ProteomicsDB; 84540; -. [Q9UIK5-2]
DR ProteomicsDB; 84541; -. [Q9UIK5-3]
DR Antibodypedia; 2895; 369 antibodies from 31 providers.
DR DNASU; 23671; -.
DR Ensembl; ENST00000272771.10; ENSP00000272771.5; ENSG00000144339.12. [Q9UIK5-1]
DR Ensembl; ENST00000392314.5; ENSP00000376128.1; ENSG00000144339.12. [Q9UIK5-2]
DR Ensembl; ENST00000409056.3; ENSP00000386871.3; ENSG00000144339.12. [Q9UIK5-3]
DR GeneID; 23671; -.
DR KEGG; hsa:23671; -.
DR MANE-Select; ENST00000272771.10; ENSP00000272771.5; NM_016192.4; NP_057276.2.
DR UCSC; uc002utc.4; human. [Q9UIK5-1]
DR CTD; 23671; -.
DR DisGeNET; 23671; -.
DR GeneCards; TMEFF2; -.
DR HGNC; HGNC:11867; TMEFF2.
DR HPA; ENSG00000144339; Tissue enhanced (brain, prostate, seminal vesicle).
DR MIM; 605734; gene.
DR neXtProt; NX_Q9UIK5; -.
DR OpenTargets; ENSG00000144339; -.
DR PharmGKB; PA36568; -.
DR VEuPathDB; HostDB:ENSG00000144339; -.
DR eggNOG; KOG3649; Eukaryota.
DR GeneTree; ENSGT00940000156056; -.
DR HOGENOM; CLU_048579_1_0_1; -.
DR InParanoid; Q9UIK5; -.
DR OMA; XCDAGYT; -.
DR OrthoDB; 1517641at2759; -.
DR PhylomeDB; Q9UIK5; -.
DR TreeFam; TF330868; -.
DR PathwayCommons; Q9UIK5; -.
DR SignaLink; Q9UIK5; -.
DR BioGRID-ORCS; 23671; 7 hits in 1017 CRISPR screens.
DR ChiTaRS; TMEFF2; human.
DR GeneWiki; TMEFF2; -.
DR GenomeRNAi; 23671; -.
DR Pharos; Q9UIK5; Tbio.
DR PRO; PR:Q9UIK5; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UIK5; protein.
DR Bgee; ENSG00000144339; Expressed in middle temporal gyrus and 146 other tissues.
DR Genevisible; Q9UIK5; HS.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0030336; P:negative regulation of cell migration; IDA:MGI.
DR GO; GO:0045720; P:negative regulation of integrin biosynthetic process; IMP:MGI.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IDA:MGI.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IBA:GO_Central.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR GO; GO:0044319; P:wound healing, spreading of cells; IDA:MGI.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR Pfam; PF07648; Kazal_2; 2.
DR SMART; SM00280; KAZAL; 2.
DR SUPFAM; SSF100895; SSF100895; 2.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS51465; KAZAL_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..40
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 41..374
FT /note="Tomoregulin-2"
FT /id="PRO_0000016587"
FT TOPO_DOM 41..320
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 85..137
FT /note="Kazal-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 176..229
FT /note="Kazal-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 261..301
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 303..320
FT /note="Required for shedding"
FT REGION 353..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 355..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) (complex) asparagine; atypical"
FT /evidence="ECO:0000269|PubMed:19139490"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 91..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 95..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 103..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 182..213
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 186..206
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 195..227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 265..278
FT /evidence="ECO:0000250"
FT DISULFID 273..289
FT /evidence="ECO:0000250"
FT DISULFID 291..300
FT /evidence="ECO:0000250"
FT VAR_SEQ 147..175
FT /note="VHEGSGETSQKETSTCDICQFGAECDEDA -> GRSCLFTYLKIYWWILLCI
FT FTYVCSISDI (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16439095"
FT /id="VSP_024973"
FT VAR_SEQ 176..374
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16439095"
FT /id="VSP_024974"
FT VAR_SEQ 344..346
FT /note="KCP -> AKL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.7"
FT /id="VSP_014312"
FT VAR_SEQ 347..374
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.7"
FT /id="VSP_014313"
FT CONFLICT 28
FT /note="M -> V (in Ref. 8; BAD96411)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="E -> G (in Ref. 6; BAC11030)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="M -> T (in Ref. 8; BAD96411)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="L -> H (in Ref. 8; BAD96411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 374 AA; 41428 MW; 44452F680FEBDCDB CRC64;
MVLWESPRQC SSWTLCEGFC WLLLLPVMLL IVARPVKLAA FPTSLSDCQT PTGWNCSGYD
DRENDLFLCD TNTCKFDGEC LRIGDTVTCV CQFKCNNDYV PVCGSNGESY QNECYLRQAA
CKQQSEILVV SEGSCATDAG SGSGDGVHEG SGETSQKETS TCDICQFGAE CDEDAEDVWC
VCNIDCSQTN FNPLCASDGK SYDNACQIKE ASCQKQEKIE VMSLGRCQDN TTTTTKSEDG
HYARTDYAEN ANKLEESARE HHIPCPEHYN GFCMHGKCEH SINMQEPSCR CDAGYTGQHC
EKKDYSVLYV VPGPVRFQYV LIAAVIGTIQ IAVICVVVLC ITRKCPRSNR IHRQKQNTGH
YSSDNTTRAS TRLI
