KIFA3_HUMAN
ID KIFA3_HUMAN Reviewed; 792 AA.
AC Q92845; B1AKU4; B1AKU5; B2RDL1; B7Z8A3; F5H591; Q8NHU7; Q9H416;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Kinesin-associated protein 3;
DE Short=KAP-3;
DE Short=KAP3;
DE AltName: Full=Smg GDS-associated protein;
GN Name=KIFAP3; Synonyms=KIF3AP, SMAP;
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), INTERACTION WITH RAP1GDS1, AND
RP PHOSPHORYLATION.
RC TISSUE=Brain;
RX PubMed=8900189; DOI=10.1074/jbc.271.43.27013;
RA Shimizu K., Kawabe H., Minami S., Honda T., Takaishi K., Shirataki H.,
RA Takai Y.;
RT "SMAP, an Smg GDS-associating protein having arm repeats and phosphorylated
RT by src tyrosine kinase.";
RL J. Biol. Chem. 271:27013-27017(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Brain, Placenta, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 [5]
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 [6]
RP IDENTIFICATION IN A COMPLEX WITH SMC3 AND KIF3B.
RX PubMed=9506951; DOI=10.1074/jbc.273.12.6591;
RA Shimizu K., Shirataki H., Honda T., Minami S., Takai Y.;
RT "Complex formation of SMAP/KAP3, a KIF3A/B ATPase motor-associated protein,
RT with a human chromosome-associated polypeptide.";
RL J. Biol. Chem. 273:6591-6594(1998).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Involved in tethering the chromosomes to the spindle pole and
CC in chromosome movement. Binds to the tail domain of the KIF3A/KIF3B
CC heterodimer to form a heterotrimeric KIF3 complex and may regulate the
CC membrane binding of this complex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterotrimer of KIFAP3, KIF3A and KIF3B. Interacts with
CC RAP1GDS1/SMG GDS. Interacts with SMC3 subunit of the cohesin complex.
CC {ECO:0000269|PubMed:8900189, ECO:0000269|PubMed:9506951}.
CC -!- INTERACTION:
CC Q92845; Q9H6X5-2: C19orf44; NbExp=3; IntAct=EBI-954040, EBI-12061599;
CC Q92845; P09067: HOXB5; NbExp=3; IntAct=EBI-954040, EBI-3893317;
CC Q92845; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-954040, EBI-2556193;
CC Q92845; Q9Y496: KIF3A; NbExp=7; IntAct=EBI-954040, EBI-1104844;
CC Q92845; O15066: KIF3B; NbExp=7; IntAct=EBI-954040, EBI-3931791;
CC Q92845; P00540: MOS; NbExp=3; IntAct=EBI-954040, EBI-1757866;
CC Q92845; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-954040, EBI-2858213;
CC Q92845; P41227: NAA10; NbExp=7; IntAct=EBI-954040, EBI-747693;
CC Q92845; Q9BSU3: NAA11; NbExp=3; IntAct=EBI-954040, EBI-2585120;
CC Q92845; P19878: NCF2; NbExp=14; IntAct=EBI-954040, EBI-489611;
CC Q92845; Q14D33: RTP5; NbExp=3; IntAct=EBI-954040, EBI-10217913;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q92845-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92845-2; Sequence=VSP_044505;
CC Name=3;
CC IsoId=Q92845-3; Sequence=VSP_047133;
CC Name=4;
CC IsoId=Q92845-4; Sequence=VSP_047132;
CC -!- PTM: Phosphorylated on tyrosine residues by SRC in vitro; this reduces
CC the binding affinity of the protein for RAP1GDS1.
CC {ECO:0000269|PubMed:8900189}.
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DR EMBL; U59919; AAC50788.1; -; mRNA.
DR EMBL; AK297368; BAH12562.1; -; mRNA.
DR EMBL; AK303052; BAH13889.1; -; mRNA.
DR EMBL; AK315586; BAG37958.1; -; mRNA.
DR EMBL; AL356475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121714; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90872.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW90873.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW90871.1; -; Genomic_DNA.
DR EMBL; BC028679; AAH28679.1; -; mRNA.
DR CCDS; CCDS1288.1; -. [Q92845-1]
DR CCDS; CCDS55659.1; -. [Q92845-4]
DR CCDS; CCDS55660.1; -. [Q92845-3]
DR CCDS; CCDS55661.1; -. [Q92845-2]
DR RefSeq; NP_001191443.1; NM_001204514.1. [Q92845-4]
DR RefSeq; NP_001191445.1; NM_001204516.1. [Q92845-2]
DR RefSeq; NP_001191446.1; NM_001204517.1. [Q92845-3]
DR RefSeq; NP_055785.2; NM_014970.3. [Q92845-1]
DR AlphaFoldDB; Q92845; -.
DR SMR; Q92845; -.
DR BioGRID; 116582; 101.
DR ComplexPortal; CPX-3200; KIF3 complex variant AC-KAP3.
DR ComplexPortal; CPX-3201; KIF3 complex variant AB-KAP3.
DR IntAct; Q92845; 78.
DR MINT; Q92845; -.
DR STRING; 9606.ENSP00000354560; -.
DR iPTMnet; Q92845; -.
DR PhosphoSitePlus; Q92845; -.
DR BioMuta; KIFAP3; -.
DR DMDM; 73920216; -.
DR EPD; Q92845; -.
DR jPOST; Q92845; -.
DR MassIVE; Q92845; -.
DR MaxQB; Q92845; -.
DR PaxDb; Q92845; -.
DR PeptideAtlas; Q92845; -.
DR PRIDE; Q92845; -.
DR ProteomicsDB; 26809; -.
DR ProteomicsDB; 3111; -.
DR ProteomicsDB; 3112; -.
DR ProteomicsDB; 75540; -. [Q92845-1]
DR Antibodypedia; 20546; 185 antibodies from 26 providers.
DR DNASU; 22920; -.
DR Ensembl; ENST00000361580.7; ENSP00000354560.2; ENSG00000075945.13. [Q92845-1]
DR Ensembl; ENST00000367765.5; ENSP00000356739.1; ENSG00000075945.13. [Q92845-3]
DR Ensembl; ENST00000367767.5; ENSP00000356741.1; ENSG00000075945.13. [Q92845-2]
DR Ensembl; ENST00000538366.5; ENSP00000444622.1; ENSG00000075945.13. [Q92845-4]
DR GeneID; 22920; -.
DR KEGG; hsa:22920; -.
DR MANE-Select; ENST00000361580.7; ENSP00000354560.2; NM_014970.4; NP_055785.2.
DR UCSC; uc001ggv.4; human. [Q92845-1]
DR CTD; 22920; -.
DR DisGeNET; 22920; -.
DR GeneCards; KIFAP3; -.
DR HGNC; HGNC:17060; KIFAP3.
DR HPA; ENSG00000075945; Low tissue specificity.
DR MIM; 601836; gene.
DR neXtProt; NX_Q92845; -.
DR OpenTargets; ENSG00000075945; -.
DR PharmGKB; PA30111; -.
DR VEuPathDB; HostDB:ENSG00000075945; -.
DR eggNOG; KOG1222; Eukaryota.
DR GeneTree; ENSGT00390000003574; -.
DR HOGENOM; CLU_009879_1_0_1; -.
DR InParanoid; Q92845; -.
DR OMA; NFVEFVG; -.
DR OrthoDB; 535512at2759; -.
DR PhylomeDB; Q92845; -.
DR TreeFam; TF314964; -.
DR PathwayCommons; Q92845; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q92845; -.
DR BioGRID-ORCS; 22920; 11 hits in 1082 CRISPR screens.
DR ChiTaRS; KIFAP3; human.
DR GeneWiki; KIFAP3; -.
DR GenomeRNAi; 22920; -.
DR Pharos; Q92845; Tbio.
DR PRO; PR:Q92845; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q92845; protein.
DR Bgee; ENSG00000075945; Expressed in cortical plate and 197 other tissues.
DR Genevisible; Q92845; HS.
DR GO; GO:0005930; C:axoneme; IBA:GO_Central.
DR GO; GO:0005813; C:centrosome; IDA:BHF-UCL.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR GO; GO:0035869; C:ciliary transition zone; IBA:GO_Central.
DR GO; GO:0005929; C:cilium; TAS:Reactome.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016939; C:kinesin II complex; IDA:BHF-UCL.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:BHF-UCL.
DR GO; GO:1990075; C:periciliary membrane compartment; IEA:Ensembl.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:Ensembl.
DR GO; GO:0001750; C:photoreceptor outer segment; IEA:Ensembl.
DR GO; GO:0120170; F:intraciliary transport particle B binding; IEA:Ensembl.
DR GO; GO:0019894; F:kinesin binding; IPI:BHF-UCL.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:BHF-UCL.
DR GO; GO:0010659; P:cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0044782; P:cilium organization; IBA:GO_Central.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; ISS:UniProtKB.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IEA:Ensembl.
DR GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR GO; GO:0072383; P:plus-end-directed vesicle transport along microtubule; TAS:BHF-UCL.
DR GO; GO:0046587; P:positive regulation of calcium-dependent cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0008104; P:protein localization; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0070242; P:thymocyte apoptotic process; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR008658; KAP3.
DR PANTHER; PTHR15605; PTHR15605; 1.
DR SMART; SM00185; ARM; 3.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..792
FT /note="Kinesin-associated protein 3"
FT /id="PRO_0000084302"
FT REPEAT 333..373
FT /note="ARM 1"
FT REPEAT 374..412
FT /note="ARM 2"
FT REPEAT 494..533
FT /note="ARM 3"
FT REPEAT 578..620
FT /note="ARM 4"
FT REPEAT 621..662
FT /note="ARM 5"
FT REGION 103..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..106
FT /note="MQGEDARYLKRKVKGGNIDVHPSEKALIVHYEVEATILGEMGDPMLGERKEC
FT QKIIRLKSLNANTDITSLARKVVEECKLIHPSKLNEVEQLLYYLQNRRDSLSGK -> M
FT SIALGNTYRRSLSDSETVSVLQASLCE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047132"
FT VAR_SEQ 1..40
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047133"
FT VAR_SEQ 11..55
FT /note="RKVKGGNIDVHPSEKALIVHYEVEATILGEMGDPMLGERKECQKI -> S
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044505"
FT VARIANT 513
FT /note="S -> A (in dbSNP:rs12075833)"
FT /id="VAR_051081"
FT CONFLICT 91
FT /note="Q -> L (in Ref. 1; AAC50788)"
FT /evidence="ECO:0000305"
FT CONFLICT 734
FT /note="I -> V (in Ref. 2; BAH13889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 792 AA; 91205 MW; 1887A75D811DF56A CRC64;
MQGEDARYLK RKVKGGNIDV HPSEKALIVH YEVEATILGE MGDPMLGERK ECQKIIRLKS
LNANTDITSL ARKVVEECKL IHPSKLNEVE QLLYYLQNRR DSLSGKEKKE KSSKPKDPPP
FEGMEIDEVA NINDMDEYIE LLYEDIPDKV RGSALILQLA RNPDNLEELL LNETALGALA
RVLREDWKQS VELATNIIYI FFCFSSFSQF HGLITHYKIG ALCMNIIDHE LKRHELWQEE
LSKKKKAVDE DPENQTLRKD YEKTFKKYQG LVVKQEQLLR VALYLLLNLA EDTRTELKMR
NKNIVHMLVK ALDRDNFELL ILVVSFLKKL SIFMENKNDM VEMDIVEKLV KMIPCEHEDL
LNITLRLLLN LSFDTGLRNK MVQVGLLPKL TALLGNDNYK QIAMCVLYHI SMDDRFKSMF
AYTDCIPQLM KMLFECSDER IDLELISFCI NLAANKRNVQ LICEGNGLKM LMKRALKFKD
PLLMKMIRNI SQHDGPTKNL FIDYVGDLAA QISNDEEEEF VIECLGTLAN LTIPDLDWEL
VLKEYKLVPY LKDKLKPGAA EDDLVLEVVI MIGTVSMDDS CAALLAKSGI IPALIELLNA
QQEDDEFVCQ IIYVFYQMVF HQATRDVIIK ETQAPAYLID LMHDKNNEIR KVCDNTLDII
AEYDEEWAKK IQSEKFRWHN SQWLEMVESR QMDESEQYLY GDDRIEPYIH EGDILERPDL
FYNSDGLIAS EGAISPDFFN DYHLQNGDVV GQHSFPGSLG MDGFGQPVGI LGRPATAYGF
RPDEPYYYGY GS
