NCKP1_HUMAN
ID NCKP1_HUMAN Reviewed; 1128 AA.
AC Q9Y2A7; O60329; Q53QN5; Q53S94; Q53Y35;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Nck-associated protein 1;
DE Short=NAP 1;
DE AltName: Full=Membrane-associated protein HEM-2;
DE AltName: Full=p125Nap1;
GN Name=NCKAP1; Synonyms=HEM2, KIAA0587, NAP1;
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).
RC TISSUE=Brain;
RX PubMed=10673335; DOI=10.1006/geno.1999.6053;
RA Suzuki T., Nishiyama K., Yamamoto A., Inazawa J., Iwaki T., Yamada T.,
RA Kanazawa I., Sakaki Y.;
RT "Molecular cloning of a novel apoptosis-related gene, human Nap1 (NCKAP1),
RT and its possible relation to Alzheimer disease.";
RL Genomics 63:246-254(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
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 MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Uterus;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL135 (MICROBIAL INFECTION).
RX PubMed=25121749; DOI=10.1016/j.chom.2014.07.005;
RA Stanton R.J., Prod'homme V., Purbhoo M.A., Moore M., Aicheler R.J.,
RA Heinzmann M., Bailer S.M., Haas J., Antrobus R., Weekes M.P., Lehner P.J.,
RA Vojtesek B., Miners K.L., Man S., Wilkie G.S., Davison A.J., Wang E.C.,
RA Tomasec P., Wilkinson G.W.;
RT "HCMV pUL135 remodels the actin cytoskeleton to impair immune recognition
RT of infected cells.";
RL Cell Host Microbe 16:201-214(2014).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF WAVE1 COMPLEX, AND SUBUNIT.
RX PubMed=21107423; DOI=10.1038/nature09623;
RA Chen Z., Borek D., Padrick S.B., Gomez T.S., Metlagel Z., Ismail A.M.,
RA Umetani J., Billadeau D.D., Otwinowski Z., Rosen M.K.;
RT "Structure and control of the actin regulatory WAVE complex.";
RL Nature 468:533-538(2010).
RN [11]
RP VARIANT GLU-1094--1128-ALA DEL, AND TISSUE SPECIFICITY.
RX PubMed=28940097; DOI=10.1007/s00439-017-1843-2;
RA Anazi S., Maddirevula S., Salpietro V., Asi Y.T., Alsahli S., Alhashem A.,
RA Shamseldin H.E., AlZahrani F., Patel N., Ibrahim N., Abdulwahab F.M.,
RA Hashem M., Alhashmi N., Al Murshedi F., Al Kindy A., Alshaer A.,
RA Rumayyan A., Al Tala S., Kurdi W., Alsaman A., Alasmari A., Banu S.,
RA Sultan T., Saleh M.M., Alkuraya H., Salih M.A., Aldhalaan H., Ben-Omran T.,
RA Al Musafri F., Ali R., Suleiman J., Tabarki B., El-Hattab A.W., Bupp C.,
RA Alfadhel M., Al Tassan N., Monies D., Arold S.T., Abouelhoda M.,
RA Lashley T., Houlden H., Faqeih E., Alkuraya F.S.;
RT "Expanding the genetic heterogeneity of intellectual disability.";
RL Hum. Genet. 136:1419-1429(2017).
RN [12]
RP ERRATUM OF PUBMED:28940097.
RX PubMed=29288388; DOI=10.1007/s00439-017-1859-7;
RA Anazi S., Maddirevula S., Salpietro V., Asi Y.T., Alsahli S., Alhashem A.,
RA Shamseldin H.E., AlZahrani F., Patel N., Ibrahim N., Abdulwahab F.M.,
RA Hashem M., Alhashmi N., Al Murshedi F., Al Kindy A., Alshaer A.,
RA Rumayyan A., Al Tala S., Kurdi W., Alsaman A., Alasmari A., Banu S.,
RA Sultan T., Saleh M.M., Alkuraya H., Salih M.A., Aldhalaan H., Ben-Omran T.,
RA Al Musafri F., Ali R., Suleiman J., Tabarki B., El-Hattab A.W., Bupp C.,
RA Alfadhel M., Al Tassan N., Monies D., Arold S.T., Abouelhoda M.,
RA Lashley T., Houlden H., Faqeih E., Alkuraya F.S.;
RT "Correction to: Expanding the genetic heterogeneity of intellectual
RT disability.";
RL Hum. Genet. 137:105-109(2018).
CC -!- FUNCTION: Part of the WAVE complex that regulates lamellipodia
CC formation. The WAVE complex regulates actin filament reorganization via
CC its interaction with the Arp2/3 complex. Actin remodeling activity is
CC regulated by RAC1. As component of the WAVE1 complex, required for
CC BDNF-NTRK2 endocytic trafficking and signaling from early endosomes.
CC {ECO:0000250|UniProtKB:P28660}.
CC -!- SUBUNIT: Component of the WAVE1 complex composed of ABI2, CYFIP1 or
CC CYFIP2, BRK1, NCKAP1 and WASF1/WAVE1. Within the complex, a heterodimer
CC containing NCKAP1 and CYFIP1 interacts with a heterotrimer formed by
CC WAVE1, ABI2 and BRK1. Component of the WAVE2 complex composed of ABI1,
CC CYFIP1/SRA1, NCKAP1/NAP1 and WASF2/WAVE2. CYFIP2 binds to activated
CC RAC1 which causes the complex to dissociate, releasing activated WASF1.
CC The complex can also be activated by NCK1. Associates preferentially
CC with the first SH3 domain of NCK. Interacts with NYAP1, NYAP2 and MYO16
CC (By similarity). {ECO:0000250|UniProtKB:P28660}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus
CC protein UL135. {ECO:0000269|PubMed:25121749}.
CC -!- INTERACTION:
CC Q9Y2A7; Q8IZP0: ABI1; NbExp=5; IntAct=EBI-389845, EBI-375446;
CC Q9Y2A7; Q92870-2: APBB2; NbExp=3; IntAct=EBI-389845, EBI-21535880;
CC Q9Y2A7; Q7L576: CYFIP1; NbExp=5; IntAct=EBI-389845, EBI-1048143;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P28660};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:P28660};
CC Cytoplasmic side {ECO:0000250|UniProtKB:P28660}. Cell projection,
CC lamellipodium membrane {ECO:0000250|UniProtKB:P28660}; Single-pass
CC membrane protein {ECO:0000250|UniProtKB:P28660}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P28660}. Note=At the interface between the
CC lamellipodial actin meshwork and the membrane.
CC {ECO:0000250|UniProtKB:P28660}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y2A7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y2A7-2; Sequence=VSP_036558;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined except peripheral
CC blood leukocytes, with highest expression in brain, heart, and skeletal
CC muscle. Expressed in cells of various brain regions including Purkinje
CC cells and dentate nucleus of the cerebellum, CA4 region and dentate
CC gyrus of the hippocampus, and in frontal gray and white matter
CC (PubMed:28940097). {ECO:0000269|PubMed:28940097}.
CC -!- SIMILARITY: Belongs to the HEM-1/HEM-2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25513.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AB014509; BAA77295.1; -; mRNA.
DR EMBL; AB011159; BAA25513.2; ALT_INIT; mRNA.
DR EMBL; AK292914; BAF85603.1; -; mRNA.
DR EMBL; BT007033; AAP35681.1; -; mRNA.
DR EMBL; AC108514; AAX93118.1; -; Genomic_DNA.
DR EMBL; AC064871; AAY24196.1; -; Genomic_DNA.
DR EMBL; BC015025; AAH15025.1; -; mRNA.
DR CCDS; CCDS2287.1; -. [Q9Y2A7-1]
DR CCDS; CCDS2288.1; -. [Q9Y2A7-2]
DR RefSeq; NP_038464.1; NM_013436.4. [Q9Y2A7-1]
DR RefSeq; NP_995314.1; NM_205842.2. [Q9Y2A7-2]
DR PDB; 3P8C; X-ray; 2.29 A; B=1-1128.
DR PDB; 4N78; X-ray; 2.43 A; B=1-1128.
DR PDBsum; 3P8C; -.
DR PDBsum; 4N78; -.
DR AlphaFoldDB; Q9Y2A7; -.
DR SMR; Q9Y2A7; -.
DR BioGRID; 116003; 113.
DR CORUM; Q9Y2A7; -.
DR DIP; DIP-31119N; -.
DR IntAct; Q9Y2A7; 60.
DR MINT; Q9Y2A7; -.
DR STRING; 9606.ENSP00000354251; -.
DR GlyGen; Q9Y2A7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2A7; -.
DR MetOSite; Q9Y2A7; -.
DR PhosphoSitePlus; Q9Y2A7; -.
DR SwissPalm; Q9Y2A7; -.
DR BioMuta; NCKAP1; -.
DR DMDM; 12643947; -.
DR EPD; Q9Y2A7; -.
DR jPOST; Q9Y2A7; -.
DR MassIVE; Q9Y2A7; -.
DR MaxQB; Q9Y2A7; -.
DR PaxDb; Q9Y2A7; -.
DR PeptideAtlas; Q9Y2A7; -.
DR PRIDE; Q9Y2A7; -.
DR ProteomicsDB; 85712; -. [Q9Y2A7-1]
DR ProteomicsDB; 85713; -. [Q9Y2A7-2]
DR Antibodypedia; 19761; 212 antibodies from 32 providers.
DR DNASU; 10787; -.
DR Ensembl; ENST00000360982.2; ENSP00000354251.2; ENSG00000061676.15. [Q9Y2A7-2]
DR Ensembl; ENST00000361354.9; ENSP00000355348.3; ENSG00000061676.15. [Q9Y2A7-1]
DR GeneID; 10787; -.
DR KEGG; hsa:10787; -.
DR MANE-Select; ENST00000361354.9; ENSP00000355348.3; NM_013436.5; NP_038464.1.
DR UCSC; uc002upb.5; human. [Q9Y2A7-1]
DR CTD; 10787; -.
DR DisGeNET; 10787; -.
DR GeneCards; NCKAP1; -.
DR HGNC; HGNC:7666; NCKAP1.
DR HPA; ENSG00000061676; Low tissue specificity.
DR MalaCards; NCKAP1; -.
DR MIM; 604891; gene.
DR neXtProt; NX_Q9Y2A7; -.
DR OpenTargets; ENSG00000061676; -.
DR PharmGKB; PA31468; -.
DR VEuPathDB; HostDB:ENSG00000061676; -.
DR eggNOG; KOG1917; Eukaryota.
DR GeneTree; ENSGT00390000016619; -.
DR HOGENOM; CLU_004450_0_0_1; -.
DR InParanoid; Q9Y2A7; -.
DR OMA; XSIVGMT; -.
DR OrthoDB; 138196at2759; -.
DR PhylomeDB; Q9Y2A7; -.
DR TreeFam; TF313683; -.
DR PathwayCommons; Q9Y2A7; -.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013404; RAC2 GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; Q9Y2A7; -.
DR SIGNOR; Q9Y2A7; -.
DR BioGRID-ORCS; 10787; 401 hits in 1087 CRISPR screens.
DR ChiTaRS; NCKAP1; human.
DR EvolutionaryTrace; Q9Y2A7; -.
DR GeneWiki; NCKAP1; -.
DR GenomeRNAi; 10787; -.
DR Pharos; Q9Y2A7; Tbio.
DR PRO; PR:Q9Y2A7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9Y2A7; protein.
DR Bgee; ENSG00000061676; Expressed in seminal vesicle and 209 other tissues.
DR Genevisible; Q9Y2A7; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; ISS:BHF-UCL.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030027; C:lamellipodium; ISS:BHF-UCL.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; ISS:BHF-UCL.
DR GO; GO:0031209; C:SCAR complex; IDA:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0030031; P:cell projection assembly; IBA:GO_Central.
DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:BHF-UCL.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:UniProtKB.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IDA:ARUK-UCL.
DR GO; GO:0016601; P:Rac protein signal transduction; IDA:UniProtKB.
DR InterPro; IPR019137; Nck-associated_protein-1.
DR PANTHER; PTHR12093; PTHR12093; 1.
DR Pfam; PF09735; Nckap1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Cell projection; Host-virus interaction; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..1128
FT /note="Nck-associated protein 1"
FT /id="PRO_0000216172"
FT TRANSMEM 995..1015
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 640..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT VAR_SEQ 36
FT /note="K -> KQGQVWK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9628581"
FT /id="VSP_036558"
FT VARIANT 1094..1128
FT /note="Missing (found in a patient with intellectual
FT disability; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:28940097"
FT /id="VAR_084649"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 13..39
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 51..53
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 83..117
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 127..148
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4N78"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 255..268
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 277..287
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 303..311
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 320..359
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 361..364
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 368..391
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 397..400
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 405..421
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 423..436
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 438..446
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 454..468
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 472..476
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 484..498
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 510..527
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 529..537
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 540..544
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 546..558
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 560..563
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 564..567
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 568..572
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 573..579
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 585..587
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 588..626
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 630..633
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 634..640
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 662..664
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 674..689
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 700..702
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 704..723
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 728..731
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 736..752
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 753..755
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 761..771
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 774..776
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 784..794
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 796..801
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 804..808
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 809..812
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 813..816
FT /evidence="ECO:0007829|PDB:3P8C"
FT STRAND 818..820
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 828..831
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 833..871
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 874..882
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 887..894
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 900..931
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 933..944
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 955..964
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 973..979
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 989..1006
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1007..1012
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1014..1016
FT /evidence="ECO:0007829|PDB:3P8C"
FT TURN 1020..1023
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1029..1031
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1032..1046
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1051..1068
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1069..1071
FT /evidence="ECO:0007829|PDB:4N78"
FT TURN 1075..1080
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1081..1094
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1100..1106
FT /evidence="ECO:0007829|PDB:3P8C"
FT HELIX 1109..1120
FT /evidence="ECO:0007829|PDB:3P8C"
SQ SEQUENCE 1128 AA; 128790 MW; 12D32BAC7080CB5A CRC64;
MSRSVLQPSQ QKLAEKLTIL NDRGVGMLTR LYNIKKACGD PKAKPSYLID KNLESAVKFI
VRKFPAVETR NNNQQLAQLQ KEKSEILKNL ALYYFTFVDV MEFKDHVCEL LNTIDVCQVF
FDITVNFDLT KNYLDLIITY TTLMILLSRI EERKAIIGLY NYAHEMTHGA SDREYPRLGQ
MIVDYENPLK KMMEEFVPHS KSLSDALISL QMVYPRRNLS ADQWRNAQLL SLISAPSTML
NPAQSDTMPC EYLSLDAMEK WIIFGFILCH GILNTDATAL NLWKLALQSS SCLSLFRDEV
FHIHKAAEDL FVNIRGYNKR INDIRECKEA AVSHAGSMHR ERRKFLRSAL KELATVLSDQ
PGLLGPKALF VFMALSFARD EIIWLLRHAD NMPKKSADDF IDKHIAELIF YMEELRAHVR
KYGPVMQRYY VQYLSGFDAV VLNELVQNLS VCPEDESIIM SSFVNTMTSL SVKQVEDGEV
FDFRGMRLDW FRLQAYTSVS KASLGLADHR ELGKMMNTII FHTKMVDSLV EMLVETSDLS
IFCFYSRAFE KMFQQCLELP SQSRYSIAFP LLCTHFMSCT HELCPEERHH IGDRSLSLCN
MFLDEMAKQA RNLITDICTE QCTLSDQLLP KHCAKTISQA VNKKSKKQTG KKGEPEREKP
GVESMRKNRL VVTNLDKLHT ALSELCFSIN YVPNMVVWEH TFTPREYLTS HLEIRFTKSI
VGMTMYNQAT QEIAKPSELL TSVRAYMTVL QSIENYVQID ITRVFNNVLL QQTQHLDSHG
EPTITSLYTN WYLETLLRQV SNGHIAYFPA MKAFVNLPTE NELTFNAEEY SDISEMRSLS
ELLGPYGMKF LSESLMWHIS SQVAELKKLV VENVDVLTQM RTSFDKPDQM AALFKRLSSV
DSVLKRMTII GVILSFRSLA QEALRDVLSY HIPFLVSSIE DFKDHIPRET DMKVAMNVYE
LSSAAGLPCE IDPALVVALS SQKSENISPE EEYKIACLLM VFVAVSLPTL ASNVMSQYSP
AIEGHCNNIH CLAKAINQIA AALFTIHKGS IEDRLKEFLA LASSSLLKIG QETDKTTTRN
RESVYLLLDM IVQESPFLTM DLLESCFPYV LLRNAYHAVY KQSVTSSA
