BICD1_HUMAN
ID BICD1_HUMAN Reviewed; 975 AA.
AC Q96G01; A8K2C3; F8W113; O43892; O43893;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 3.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Protein bicaudal D homolog 1;
DE Short=Bic-D 1;
GN Name=BICD1;
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), AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 702-975 (ISOFORM 3).
RX PubMed=9367685; DOI=10.1006/geno.1997.4971;
RA Baens M., Marynen P.;
RT "A human homologue (BICD1) of the Drosophila bicaudal-D gene.";
RL Genomics 45:601-606(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP ALA-778.
RC TISSUE=Cerebellum, and Thalamus;
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=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skin;
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 CHARACTERIZATION.
RX PubMed=12447383; DOI=10.1038/ncb891;
RA Matanis T., Akhmanova A., Wulf P., Del Nery E., Weide T., Stepanova T.,
RA Galjart N., Grosveld F., Goud B., De Zeeuw C.I., Barnekow A.,
RA Hoogenraad C.C.;
RT "Bicaudal-D regulates COPI-independent Golgi-ER transport by recruiting the
RT dynein-dynactin motor complex.";
RL Nat. Cell Biol. 4:986-992(2002).
RN [7]
RP INTERACTION WITH RAB6B.
RX PubMed=17707369; DOI=10.1016/j.yexcr.2007.05.032;
RA Wanschers B.F.J.F., van de Vorstenbosch R., Schlager M.A., Splinter D.,
RA Akhmanova A., Hoogenraad C.C., Wieringa B., Fransen J.A.;
RT "A role for the Rab6B Bicaudal-D1 interaction in retrograde transport in
RT neuronal cells.";
RL Exp. Cell Res. 313:3408-3420(2007).
RN [8]
RP INTERACTION WITH HHV-5 PROTEIN UL32 (MICROBIAL INFECTION).
RX PubMed=20089649; DOI=10.1128/jvi.01776-09;
RA Indran S.V., Ballestas M.E., Britt W.J.;
RT "Bicaudal D1-dependent trafficking of human cytomegalovirus tegument
RT protein pp150 in virus-infected cells.";
RL J. Virol. 84:3162-3177(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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).
CC -!- FUNCTION: Regulates coat complex coatomer protein I (COPI)-independent
CC Golgi-endoplasmic reticulum transport by recruiting the dynein-dynactin
CC motor complex.
CC -!- SUBUNIT: Interacts with RAB6A. Interacts (via C-terminus) with RAB6B
CC (GTP-bound); the interaction is direct. Interacts with CLIP-115 and
CC KIFC2 (By similarity). {ECO:0000250, ECO:0000269|PubMed:17707369}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human
CC cytomegalovirus/HHV-5 protein UL32. {ECO:0000269|PubMed:20089649}.
CC -!- INTERACTION:
CC Q96G01; P49841: GSK3B; NbExp=7; IntAct=EBI-1104509, EBI-373586;
CC Q96G01; P40763: STAT3; NbExp=2; IntAct=EBI-1104509, EBI-518675;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q96G01-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96G01-2; Sequence=VSP_007961, VSP_007962;
CC Name=3;
CC IsoId=Q96G01-3; Sequence=VSP_007963, VSP_007964;
CC Name=4;
CC IsoId=Q96G01-4; Sequence=VSP_045637, VSP_045638;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, heart and skeletal muscle.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Due to intron retention. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the BicD family. {ECO:0000305}.
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DR EMBL; U90028; AAB94805.1; -; mRNA.
DR EMBL; U90030; AAB94806.1; -; mRNA.
DR EMBL; AK290188; BAF82877.1; -; mRNA.
DR EMBL; AK313430; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC016954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC026356; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC048344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087245; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471116; EAW88534.1; -; Genomic_DNA.
DR EMBL; BC010091; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS44859.1; -. [Q96G01-4]
DR CCDS; CCDS8726.1; -. [Q96G01-1]
DR RefSeq; NP_001003398.1; NM_001003398.1. [Q96G01-4]
DR RefSeq; NP_001705.2; NM_001714.2. [Q96G01-1]
DR AlphaFoldDB; Q96G01; -.
DR SMR; Q96G01; -.
DR BioGRID; 107105; 223.
DR IntAct; Q96G01; 23.
DR MINT; Q96G01; -.
DR STRING; 9606.ENSP00000281474; -.
DR iPTMnet; Q96G01; -.
DR PhosphoSitePlus; Q96G01; -.
DR BioMuta; BICD1; -.
DR DMDM; 209572759; -.
DR EPD; Q96G01; -.
DR jPOST; Q96G01; -.
DR MassIVE; Q96G01; -.
DR MaxQB; Q96G01; -.
DR PaxDb; Q96G01; -.
DR PeptideAtlas; Q96G01; -.
DR PRIDE; Q96G01; -.
DR ProteomicsDB; 29543; -.
DR ProteomicsDB; 76577; -. [Q96G01-1]
DR ProteomicsDB; 76578; -. [Q96G01-2]
DR ProteomicsDB; 76579; -. [Q96G01-3]
DR Antibodypedia; 24706; 65 antibodies from 22 providers.
DR DNASU; 636; -.
DR Ensembl; ENST00000548411.5; ENSP00000446793.1; ENSG00000151746.15. [Q96G01-4]
DR Ensembl; ENST00000551848.1; ENSP00000448933.1; ENSG00000151746.15. [Q96G01-2]
DR Ensembl; ENST00000652176.1; ENSP00000498700.1; ENSG00000151746.15. [Q96G01-1]
DR GeneID; 636; -.
DR KEGG; hsa:636; -.
DR MANE-Select; ENST00000652176.1; ENSP00000498700.1; NM_001714.4; NP_001705.2.
DR UCSC; uc001rku.4; human. [Q96G01-1]
DR CTD; 636; -.
DR DisGeNET; 636; -.
DR GeneCards; BICD1; -.
DR HGNC; HGNC:1049; BICD1.
DR HPA; ENSG00000151746; Tissue enhanced (brain).
DR MIM; 602204; gene.
DR neXtProt; NX_Q96G01; -.
DR OpenTargets; ENSG00000151746; -.
DR PharmGKB; PA25352; -.
DR VEuPathDB; HostDB:ENSG00000151746; -.
DR eggNOG; KOG0999; Eukaryota.
DR GeneTree; ENSGT00940000154471; -.
DR HOGENOM; CLU_2399043_0_0_1; -.
DR InParanoid; Q96G01; -.
DR OMA; AHHISLG; -.
DR OrthoDB; 542877at2759; -.
DR PhylomeDB; Q96G01; -.
DR TreeFam; TF323833; -.
DR PathwayCommons; Q96G01; -.
DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR SignaLink; Q96G01; -.
DR SIGNOR; Q96G01; -.
DR BioGRID-ORCS; 636; 10 hits in 1078 CRISPR screens.
DR ChiTaRS; BICD1; human.
DR GeneWiki; BICD1; -.
DR GenomeRNAi; 636; -.
DR Pharos; Q96G01; Tbio.
DR PRO; PR:Q96G01; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96G01; protein.
DR Bgee; ENSG00000151746; Expressed in ventricular zone and 181 other tissues.
DR ExpressionAtlas; Q96G01; baseline and differential.
DR Genevisible; Q96G01; HS.
DR GO; GO:0005813; C:centrosome; IMP:ARUK-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:BHF-UCL.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0099503; C:secretory vesicle; IDA:BHF-UCL.
DR GO; GO:0005802; C:trans-Golgi network; IDA:BHF-UCL.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IDA:BHF-UCL.
DR GO; GO:0034452; F:dynactin binding; IDA:BHF-UCL.
DR GO; GO:0070840; F:dynein complex binding; IDA:BHF-UCL.
DR GO; GO:0045505; F:dynein intermediate chain binding; IDA:ARUK-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL.
DR GO; GO:0031871; F:proteinase activated receptor binding; ISS:BHF-UCL.
DR GO; GO:0031267; F:small GTPase binding; IPI:BHF-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR GO; GO:0008298; P:intracellular mRNA localization; NAS:UniProtKB.
DR GO; GO:0072393; P:microtubule anchoring at microtubule organizing center; ISS:BHF-UCL.
DR GO; GO:0072385; P:minus-end-directed organelle transport along microtubule; IMP:BHF-UCL.
DR GO; GO:1900275; P:negative regulation of phospholipase C activity; ISS:BHF-UCL.
DR GO; GO:1900737; P:negative regulation of phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:1904781; P:positive regulation of protein localization to centrosome; IGI:ARUK-UCL.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:BHF-UCL.
DR GO; GO:0033365; P:protein localization to organelle; IDA:BHF-UCL.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IGI:ARUK-UCL.
DR GO; GO:1900276; P:regulation of proteinase activated receptor activity; ISS:BHF-UCL.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR GO; GO:0034063; P:stress granule assembly; ISS:BHF-UCL.
DR GO; GO:0016032; P:viral process; IMP:BHF-UCL.
DR InterPro; IPR018477; BICD.
DR PANTHER; PTHR31233; PTHR31233; 1.
DR Pfam; PF09730; BicD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Golgi apparatus; Host-virus interaction;
KW Reference proteome.
FT CHAIN 1..975
FT /note="Protein bicaudal D homolog 1"
FT /id="PRO_0000205357"
FT REGION 383..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..803
FT /note="Interaction with RAB6A"
FT REGION 800..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 836..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..265
FT /evidence="ECO:0000255"
FT COILED 319..496
FT /evidence="ECO:0000255"
FT COILED 663..803
FT /evidence="ECO:0000255"
FT COMPBIAS 385..403
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 72..93
FT /note="AFGQSFSIHRKVAEDGETREET -> VSCLSPLPFLALTPPTRKAHSS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007961"
FT VAR_SEQ 94..975
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007962"
FT VAR_SEQ 821..835
FT /note="VSGEASVTVPTIDTY -> IVSSLLPPYRHSAHN (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045637"
FT VAR_SEQ 836..975
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045638"
FT VAR_SEQ 858..873
FT /note="QFSPSLCDQSRPRTSG -> YACSDLHSTVQWPDFS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9367685"
FT /id="VSP_007963"
FT VAR_SEQ 874..975
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9367685"
FT /id="VSP_007964"
FT VARIANT 778
FT /note="T -> A (in dbSNP:rs200845476)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_069060"
FT CONFLICT 588
FT /note="A -> P (in Ref. 1; AAB94805)"
FT /evidence="ECO:0000305"
FT CONFLICT 746
FT /note="A -> T (in Ref. 1; AAB94805)"
FT /evidence="ECO:0000305"
FT CONFLICT 796
FT /note="D -> G (in Ref. 1; AAB94806)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 975 AA; 110750 MW; CCF0FB12013AA294 CRC64;
MAAEEVLQTV DHYKTEIERL TKELTETTHE KIQAAEYGLV VLEEKLTLKQ QYDELEAEYD
SLKQELEQLK EAFGQSFSIH RKVAEDGETR EETLLQESAS KEAYYLGKIL EMQNELKQSR
AVVTNVQAEN ERLTAVVQDL KENNEMVELQ RIRMKDEIRE YKFREARLLQ DYTELEEENI
TLQKLVSTLK QNQVEYEGLK HEIKRFEEET VLLNSQLEDA IRLKEIAEHQ LEEALETLKN
EREQKNNLRK ELSQYISLND NHISISVDGL KFAEDGSEPN NDDKMNGHIH GPLVKLNGDY
RTPTLRKGES LNPVSDLFSE LNISEIQKLK QQLMQVEREK AILLANLQES QTQLEHTKGA
LTEQHERVHR LTEHVNAMRG LQSSKELKAE LDGEKGRDSG EEAHDYEVDI NGLEILECKY
RVAVTEVIDL KAEIKALKEK YNKSVENYTD EKAKYESKIQ MYDEQVTSLE KTTKESGEKM
AHMEKELQKM TSIANENHST LNTAQDELVT FSEELAQLYH HVCLCNNETP NRVMLDYYRQ
SRVTRSGSLK GPDDPRGLLS PRLARRGVSS PVETRTSSEP VAKESTEASK EPSPTKTPTI
SPVITAPPSS PVLDTSDIRK EPMNIYNLNA IIRDQIKHLQ KAVDRSLQLS RQRAAARELA
PMIDKDKEAL MEEILKLKSL LSTKREQIAT LRAVLKANKQ TAEVALANLK NKYENEKAMV
TETMTKLRNE LKALKEDAAT FSSLRAMFAT RCDEYVTQLD EMQRQLAAAE DEKKTLNTLL
RMAIQQKLAL TQRLEDLEFD HEQSRRSKGK LGKSKIGSPK VSGEASVTVP TIDTYLLHSQ
GPQTPNIRVS SGTQRKRQFS PSLCDQSRPR TSGASYLQNL LRVPPDPTST ESFLLKGPPS
MSEFIQGHRL SKEKRLTVAP PDCQQPAASV PPQCSQLAGR QDCPTVSPDT ALPEEQPHSS
SQCAPLHCLS KPPHP
