KCND1_HUMAN
ID KCND1_HUMAN Reviewed; 647 AA.
AC Q9NSA2; A6NEF1; B2RCG0; O75671;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Potassium voltage-gated channel subfamily D member 1;
DE AltName: Full=Voltage-gated potassium channel subunit Kv4.1;
GN Name=KCND1;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Embryonic kidney;
RX PubMed=10729221; DOI=10.1006/geno.2000.6117;
RA Isbrandt D., Leicher T., Waldschuetz R., Zhu X.-R., Luhmann U., Michel U.,
RA Sauter K., Pongs O.;
RT "Gene structures and expression profiles of three human KCND (Kv4)
RT potassium channels mediating A-type currents I(TO) and I(SA).";
RL Genomics 64:144-154(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RA Makita N., Shirai N., Sawa H., Sasaki K., Nagashima K., Yoshida M.C.,
RA Kitabatake A.;
RT "Homo sapiens mRNA for shal-type potassium channel KCND1 (Kv4.1).";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A.,
RA Meindl A.;
RT "Transcription map in Xp11.23.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum;
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 [5]
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [8]
RP INTERACTION WITH DPP10.
RX PubMed=15454437; DOI=10.1529/biophysj.104.042358;
RA Jerng H.H., Qian Y., Pfaffinger P.J.;
RT "Modulation of Kv4.2 channel expression and gating by dipeptidyl peptidase
RT 10 (DPP10).";
RL Biophys. J. 87:2380-2396(2004).
CC -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated rapidly
CC inactivating A-type potassium channels. May contribute to I(To) current
CC in heart and I(Sa) current in neurons. Channel properties are modulated
CC by interactions with other alpha subunits and with regulatory subunits.
CC -!- SUBUNIT: Homotetramer or heterotetramer with KCND2 and/or KCND3.
CC Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and
CC KCNIP4 (By similarity). Interacts with DPP10 (Probable). {ECO:0000250,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
CC projection, dendrite {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NSA2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NSA2-2; Sequence=VSP_057040;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in brain, in
CC particular in cerebellum and thalamus; detected at lower levels in the
CC other parts of the brain. {ECO:0000269|PubMed:10729221}.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position.
CC -!- SIMILARITY: Belongs to the potassium channel family. D (Shal) (TC
CC 1.A.1.2) subfamily. Kv4.1/KCND1 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF166003; AAF65516.1; -; mRNA.
DR EMBL; AF166006; AAF65617.1; -; Genomic_DNA.
DR EMBL; AF166004; AAF65617.1; JOINED; Genomic_DNA.
DR EMBL; AF166005; AAF65617.1; JOINED; Genomic_DNA.
DR EMBL; AB021865; BAA96454.1; -; mRNA.
DR EMBL; AJ005898; CAA06755.1; -; mRNA.
DR EMBL; AK094431; BAG52865.1; -; mRNA.
DR EMBL; AK315092; BAG37557.1; -; mRNA.
DR EMBL; AF207550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471224; EAW50720.1; -; Genomic_DNA.
DR EMBL; CH471224; EAW50721.1; -; Genomic_DNA.
DR EMBL; BC045659; AAH45659.1; -; mRNA.
DR CCDS; CCDS14314.1; -. [Q9NSA2-1]
DR RefSeq; NP_004970.3; NM_004979.5. [Q9NSA2-1]
DR RefSeq; XP_011542212.1; XM_011543910.2. [Q9NSA2-1]
DR AlphaFoldDB; Q9NSA2; -.
DR SMR; Q9NSA2; -.
DR BioGRID; 109952; 1.
DR IntAct; Q9NSA2; 1.
DR STRING; 9606.ENSP00000218176; -.
DR ChEMBL; CHEMBL2362996; -.
DR DrugBank; DB06637; Dalfampridine.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB01110; Miconazole.
DR DrugBank; DB01069; Promethazine.
DR DrugCentral; Q9NSA2; -.
DR GuidetoPHARMACOLOGY; 552; -.
DR TCDB; 1.A.1.2.28; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; Q9NSA2; 2 sites.
DR iPTMnet; Q9NSA2; -.
DR PhosphoSitePlus; Q9NSA2; -.
DR BioMuta; KCND1; -.
DR DMDM; 38258256; -.
DR jPOST; Q9NSA2; -.
DR MassIVE; Q9NSA2; -.
DR PaxDb; Q9NSA2; -.
DR PeptideAtlas; Q9NSA2; -.
DR PRIDE; Q9NSA2; -.
DR ProteomicsDB; 82521; -. [Q9NSA2-1]
DR ProteomicsDB; 980; -.
DR Antibodypedia; 370; 263 antibodies from 31 providers.
DR DNASU; 3750; -.
DR Ensembl; ENST00000218176.4; ENSP00000218176.3; ENSG00000102057.10. [Q9NSA2-1]
DR Ensembl; ENST00000376477.5; ENSP00000365660.1; ENSG00000102057.10. [Q9NSA2-2]
DR GeneID; 3750; -.
DR KEGG; hsa:3750; -.
DR MANE-Select; ENST00000218176.4; ENSP00000218176.3; NM_004979.6; NP_004970.3.
DR UCSC; uc004dlw.1; human. [Q9NSA2-1]
DR CTD; 3750; -.
DR DisGeNET; 3750; -.
DR GeneCards; KCND1; -.
DR HGNC; HGNC:6237; KCND1.
DR HPA; ENSG00000102057; Low tissue specificity.
DR MIM; 300281; gene.
DR neXtProt; NX_Q9NSA2; -.
DR OpenTargets; ENSG00000102057; -.
DR PharmGKB; PA30029; -.
DR VEuPathDB; HostDB:ENSG00000102057; -.
DR eggNOG; KOG4390; Eukaryota.
DR GeneTree; ENSGT00940000162057; -.
DR HOGENOM; CLU_070236_0_0_1; -.
DR InParanoid; Q9NSA2; -.
DR OMA; FPTAFFC; -.
DR OrthoDB; 469107at2759; -.
DR PhylomeDB; Q9NSA2; -.
DR TreeFam; TF313103; -.
DR PathwayCommons; Q9NSA2; -.
DR Reactome; R-HSA-1296072; Voltage gated Potassium channels.
DR Reactome; R-HSA-5576894; Phase 1 - inactivation of fast Na+ channels.
DR SignaLink; Q9NSA2; -.
DR BioGRID-ORCS; 3750; 8 hits in 703 CRISPR screens.
DR ChiTaRS; KCND1; human.
DR GeneWiki; KCND1; -.
DR GenomeRNAi; 3750; -.
DR Pharos; Q9NSA2; Tclin.
DR PRO; PR:Q9NSA2; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9NSA2; protein.
DR Bgee; ENSG00000102057; Expressed in right hemisphere of cerebellum and 93 other tissues.
DR ExpressionAtlas; Q9NSA2; baseline and differential.
DR Genevisible; Q9NSA2; HS.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005250; F:A-type (transient outward) potassium channel activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003975; K_chnl_volt-dep_Kv4.
DR InterPro; IPR004054; K_chnl_volt-dep_Kv4.1.
DR InterPro; IPR024587; K_chnl_volt-dep_Kv4_C.
DR InterPro; IPR021645; Shal-type_N.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF11879; DUF3399; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF11601; Shal-type; 1.
DR PRINTS; PR01516; KV41CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01497; SHALCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Metal-binding; Phosphoprotein; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel; Zinc.
FT CHAIN 1..647
FT /note="Potassium voltage-gated channel subfamily D member
FT 1"
FT /id="PRO_0000054061"
FT TOPO_DOM 1..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..312
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT INTRAMEM 365..385
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..647
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 2..20
FT /note="Interaction with KCNIP2"
FT /evidence="ECO:0000250"
FT REGION 144..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..489
FT /note="Mediates dendritic targeting"
FT /evidence="ECO:0000250"
FT REGION 506..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 372..377
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 509..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03719"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62897"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..377
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057040"
FT CONFLICT 358
FT /note="S -> N (in Ref. 2; BAA96454)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="V -> I (in Ref. 2; BAA96454)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 647 AA; 71330 MW; 8672C299CDB7C5AA CRC64;
MAAGLATWLP FARAAAVGWL PLAQQPLPPA PGVKASRGDE VLVVNVSGRR FETWKNTLDR
YPDTLLGSSE KEFFYDADSG EYFFDRDPDM FRHVLNFYRT GRLHCPRQEC IQAFDEELAF
YGLVPELVGD CCLEEYRDRK KENAERLAED EEAEQAGDGP ALPAGSSLRQ RLWRAFENPH
TSTAALVFYY VTGFFIAVSV IANVVETIPC RGSARRSSRE QPCGERFPQA FFCMDTACVL
IFTGEYLLRL FAAPSRCRFL RSVMSLIDVV AILPYYIGLL VPKNDDVSGA FVTLRVFRVF
RIFKFSRHSQ GLRILGYTLK SCASELGFLL FSLTMAIIIF ATVMFYAEKG TNKTNFTSIP
AAFWYTIVTM TTLGYGDMVP STIAGKIFGS ICSLSGVLVI ALPVPVIVSN FSRIYHQNQR
ADKRRAQQKV RLARIRLAKS GTTNAFLQYK QNGGLEDSGS GEEQALCVRN RSAFEQQHHH
LLHCLEKTTC HEFTDELTFS EALGAVSPGG RTSRSTSVSS QPVGPGSLLS SCCPRRAKRR
AIRLANSTAS VSRGSMQELD MLAGLRRSHA PQSRSSLNAK PHDSLDLNCD SRDFVAAIIS
IPTPPANTPD ESQPSSPGGG GRAGSTLRNS SLGTPCLFPE TVKISSL
