CLTRN_HUMAN
ID CLTRN_HUMAN Reviewed; 222 AA.
AC Q9HBJ8; B2R9M1; Q6UW07;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Collectrin {ECO:0000303|PubMed:21907142};
DE AltName: Full=Transmembrane protein 27;
DE Flags: Precursor;
GN Name=CLTRN {ECO:0000312|HGNC:HGNC:29437};
GN Synonyms=TMEM27 {ECO:0000303|PubMed:22628310}; ORFNames=UNQ679/PRO1312;
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], AND TISSUE SPECIFICITY.
RX PubMed=11278314; DOI=10.1074/jbc.m006723200;
RA Zhang H., Wada J., Hida K., Tsuchiyama Y., Hiragushi K., Shikata K.,
RA Wang H., Lin S., Kanwar Y.S., Makino H.;
RT "Collectrin, a collecting duct-specific transmembrane glycoprotein, is a
RT novel homolog of ACE2 and is developmentally regulated in embryonic
RT kidneys.";
RL J. Biol. Chem. 276:17132-17139(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
RC TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Colon, and Kidney;
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 [7]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH SNAPIN.
RX PubMed=16330323; DOI=10.1016/j.cmet.2005.11.003;
RA Fukui K., Yang Q., Cao Y., Takahashi N., Hatakeyama H., Wang H., Wada J.,
RA Zhang Y., Marselli L., Nammo T., Yoneda K., Onishi M., Higashiyama S.,
RA Matsuzawa Y., Gonzalez F.J., Weir G.C., Kasai H., Shimomura I.,
RA Miyagawa J., Wollheim C.B., Yamagata K.;
RT "The HNF-1 target collectrin controls insulin exocytosis by SNARE complex
RT formation.";
RL Cell Metab. 2:373-384(2005).
RN [8]
RP SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING IN BETA CELLS, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21907142; DOI=10.1016/j.cmet.2011.06.018;
RA Esterhazy D., Stuetzer I., Wang H., Rechsteiner M.P., Beauchamp J.,
RA Doebeli H., Hilpert H., Matile H., Prummer M., Schmidt A., Lieske N.,
RA Boehm B., Marselli L., Bosco D., Kerr-Conte J., Aebersold R., Spinas G.A.,
RA Moch H., Migliorini C., Stoffel M.;
RT "Bace2 is a beta cell-enriched protease that regulates pancreatic beta cell
RT function and mass.";
RL Cell Metab. 14:365-377(2011).
RN [9]
RP SUBCELLULAR LOCATION, SUBUNIT, PROTEOLYTIC PROCESSING IN BETA CELLS,
RP GLYCOSYLATION, AND MUTAGENESIS OF CYS-75; ASN-76; ASN-93; 115-ALA--ASN-119;
RP 123-LEU--ILE-128; CYS-152 AND CYS-186.
RX PubMed=22628310; DOI=10.1515/hsz-2012-0104;
RA Esterhazy D., Akpinar P., Stoffel M.;
RT "Tmem27 dimerization, deglycosylation, plasma membrane depletion, and the
RT extracellular Phe-Phe motif are negative regulators of cleavage by Bace2.";
RL Biol. Chem. 393:473-484(2012).
CC -!- FUNCTION: Plays an important role in amino acid transport by acting as
CC binding partner of amino acid transporters SLC6A18 and SLC6A19,
CC regulating their trafficking on the cell surface and their amino acid
CC transporter activity (By similarity). May also play a role in
CC trafficking of amino acid transporters SLC3A1 and SLC7A9 to the renal
CC cortical cell membrane (By similarity). Regulator of SNARE complex
CC function (PubMed:16330323). Stimulator of beta cell replication
CC (PubMed:16330323). {ECO:0000250|UniProtKB:Q9ESG4,
CC ECO:0000269|PubMed:16330323}.
CC -!- SUBUNIT: Monomer (PubMed:22628310). Homodimer; dimerization prevents
CC CLTRN cleavage by BACE2 (PubMed:22628310). Interacts with SLC6A18; this
CC interaction regulates the trafficking of SLC6A18 to the cell membrane
CC and its amino acid transporter activity (By similarity). Interacts with
CC SLC6A19; this interaction regulates the trafficking of SLC6A19 to the
CC cell membrane and its amino acid transporter activity (By similarity).
CC Interacts with SNAPIN (PubMed:16330323). {ECO:0000250|UniProtKB:Q9ESG4,
CC ECO:0000269|PubMed:16330323, ECO:0000269|PubMed:22628310}.
CC -!- INTERACTION:
CC Q9HBJ8; Q6UX06: OLFM4; NbExp=3; IntAct=EBI-3924906, EBI-2804156;
CC Q9HBJ8; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-3924906, EBI-8640191;
CC Q9HBJ8; Q9Y385: UBE2J1; NbExp=3; IntAct=EBI-3924906, EBI-988826;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22628310};
CC Single-pass type I membrane protein {ECO:0000255}. Note=Localizes to
CC the brush border membranes of cells in the proximal tubules of kidney
CC (By similarity). Colocalizes with SLC6A19 in the early proximal S1
CC tubule (By similarity). {ECO:0000250|UniProtKB:Q9ESG4}.
CC -!- TISSUE SPECIFICITY: Kidney; collecting ducts. Pancreas; beta cells of
CC islets. {ECO:0000269|PubMed:11278314, ECO:0000269|PubMed:16330323}.
CC -!- DOMAIN: The cleavage site containing the double Phe-Phe motif acts as
CC negative regulator of shedding by BACE2. {ECO:0000269|PubMed:22628310}.
CC -!- PTM: Glycosylated. Glycosylation is required for plasma membrane
CC localization and for its cleavage by BACE2.
CC {ECO:0000269|PubMed:22628310}.
CC -!- PTM: Proteolytically processed in pancreatic beta cells by BACE2
CC leading to the generation and extracellular release of soluble CLTRN,
CC and a corresponding cell-associated C-terminal fragment which is later
CC cleaved by gamma-secretase. This shedding process inactivates CLTRN (By
CC similarity). Three cleavage sites have been identified for BACE2, two
CC clustered sites after Phe-116 and Leu-118 and a more membrane proximal
CC site at Phe-125; the preferred BACE2 cleavage site seems to be between
CC Phe-125 and Leu-126, Phe-116 and Leu-118 act as alternative sites
CC (PubMed:21907142, PubMed:22628310). {ECO:0000250|UniProtKB:Q9ESG4,
CC ECO:0000269|PubMed:21907142, ECO:0000269|PubMed:22628310}.
CC -!- SIMILARITY: Belongs to the CLTRN family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ89419.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF229179; AAG09466.1; -; mRNA.
DR EMBL; AY359060; AAQ89419.1; ALT_FRAME; mRNA.
DR EMBL; AK313835; BAG36568.1; -; mRNA.
DR EMBL; AC003669; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471074; EAW98894.1; -; Genomic_DNA.
DR EMBL; BC014317; AAH14317.1; -; mRNA.
DR EMBL; BC015099; AAH15099.1; -; mRNA.
DR EMBL; BC050606; AAH50606.1; -; mRNA.
DR CCDS; CCDS14170.1; -.
DR RefSeq; NP_065716.1; NM_020665.5.
DR AlphaFoldDB; Q9HBJ8; -.
DR SMR; Q9HBJ8; -.
DR BioGRID; 121500; 5.
DR IntAct; Q9HBJ8; 5.
DR STRING; 9606.ENSP00000369699; -.
DR MEROPS; M02.M01; -.
DR TCDB; 2.A.22.6.3; the neurotransmitter:sodium symporter (nss) family.
DR GlyGen; Q9HBJ8; 2 sites.
DR iPTMnet; Q9HBJ8; -.
DR PhosphoSitePlus; Q9HBJ8; -.
DR BioMuta; TMEM27; -.
DR DMDM; 74734254; -.
DR jPOST; Q9HBJ8; -.
DR MassIVE; Q9HBJ8; -.
DR PaxDb; Q9HBJ8; -.
DR PeptideAtlas; Q9HBJ8; -.
DR PRIDE; Q9HBJ8; -.
DR ProteomicsDB; 81565; -.
DR Antibodypedia; 23955; 179 antibodies from 19 providers.
DR DNASU; 57393; -.
DR Ensembl; ENST00000380342.4; ENSP00000369699.3; ENSG00000147003.7.
DR GeneID; 57393; -.
DR KEGG; hsa:57393; -.
DR MANE-Select; ENST00000380342.4; ENSP00000369699.3; NM_020665.6; NP_065716.1.
DR UCSC; uc004cxc.4; human.
DR CTD; 57393; -.
DR DisGeNET; 57393; -.
DR GeneCards; CLTRN; -.
DR HGNC; HGNC:29437; CLTRN.
DR HPA; ENSG00000147003; Tissue enriched (kidney).
DR MalaCards; CLTRN; -.
DR MIM; 300631; gene.
DR neXtProt; NX_Q9HBJ8; -.
DR OpenTargets; ENSG00000147003; -.
DR Orphanet; 2116; Hartnup disease.
DR PharmGKB; PA134994199; -.
DR VEuPathDB; HostDB:ENSG00000147003; -.
DR eggNOG; ENOG502RWVW; Eukaryota.
DR GeneTree; ENSGT00940000160862; -.
DR HOGENOM; CLU_108544_0_0_1; -.
DR InParanoid; Q9HBJ8; -.
DR OMA; CKPDAQN; -.
DR OrthoDB; 1212584at2759; -.
DR PhylomeDB; Q9HBJ8; -.
DR TreeFam; TF335519; -.
DR PathwayCommons; Q9HBJ8; -.
DR Reactome; R-HSA-264876; Insulin processing.
DR SignaLink; Q9HBJ8; -.
DR BioGRID-ORCS; 57393; 16 hits in 694 CRISPR screens.
DR ChiTaRS; TMEM27; human.
DR GenomeRNAi; 57393; -.
DR Pharos; Q9HBJ8; Tbio.
DR PRO; PR:Q9HBJ8; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9HBJ8; protein.
DR Bgee; ENSG00000147003; Expressed in kidney epithelium and 115 other tissues.
DR ExpressionAtlas; Q9HBJ8; baseline and differential.
DR Genevisible; Q9HBJ8; HS.
DR GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IDA:GO_Central.
DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; IDA:GO_Central.
DR GO; GO:0051957; P:positive regulation of amino acid transport; IBA:GO_Central.
DR GO; GO:1905737; P:positive regulation of L-proline import across plasma membrane; IGI:ARUK-UCL.
DR GO; GO:0022898; P:regulation of transmembrane transporter activity; IGI:ARUK-UCL.
DR GO; GO:0035493; P:SNARE complex assembly; IDA:GO_Central.
DR InterPro; IPR042944; Collectrin.
DR InterPro; IPR031588; Collectrin_dom.
DR PANTHER; PTHR46884; PTHR46884; 1.
DR Pfam; PF16959; Collectrin; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..222
FT /note="Collectrin"
FT /id="PRO_0000245867"
FT TOPO_DOM 15..141
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:22628310"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:22628310"
FT SITE 125..126
FT /note="Cleavage by BACE2"
FT /evidence="ECO:0000269|PubMed:22628310"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESG4"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESG4"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 75
FT /note="C->A: Increased dimerization leading to
FT hyperoligomerized. Abolishes processing by BACE2. Abolishes
FT localization to the cell membrane."
FT /evidence="ECO:0000269|PubMed:22628310"
FT MUTAGEN 76
FT /note="N->I: Loss of localization to the cell membrane.
FT Abolishes processing by BACE2. Loss of localization to the
FT cell membrane; when associated with I-93."
FT /evidence="ECO:0000269|PubMed:22628310"
FT MUTAGEN 93
FT /note="N->I: Loss of localization to the cell membrane.
FT Abolishes processing by BACE2. Loss of localization to the
FT cell membrane; when associated with I-76."
FT /evidence="ECO:0000269|PubMed:22628310"
FT MUTAGEN 115..119
FT /note="AFFLN->GGGGG,AAAAA,TYYLR: Increases processing by
FT BACE2. Decreases of protein abundance."
FT /evidence="ECO:0000269|PubMed:22628310"
FT MUTAGEN 123..128
FT /note="LEFLKI->NTYGKR: Does not affet processing by BACE2."
FT /evidence="ECO:0000269|PubMed:22628310"
FT MUTAGEN 152
FT /note="C->A: Does not affect dimerization. Does not affect
FT cell membrane localization. Abolishes dimerization; when
FT associated with A-186."
FT /evidence="ECO:0000269|PubMed:22628310"
FT MUTAGEN 186
FT /note="C->A: Abolishes dimerization. Does not affect cell
FT membrane localization. Does not affect processing by BACE2.
FT Abolishes dimerization; when associated with A-152."
FT /evidence="ECO:0000269|PubMed:22628310"
SQ SEQUENCE 222 AA; 25235 MW; 52C0ED522134ED05 CRC64;
MLWLLFFLVT AIHAELCQPG AENAFKVRLS IRTALGDKAY AWDTNEEYLF KAMVAFSMRK
VPNREATEIS HVLLCNVTQR VSFWFVVTDP SKNHTLPAVE VQSAIRMNKN RINNAFFLND
QTLEFLKIPS TLAPPMDPSV PIWIIIFGVI FCIIIVAIAL LILSGIWQRR RKNKEPSEVD
DAEDKCENMI TIENGIPSDP LDMKGGHIND AFMTEDERLT PL
