NIN_MOUSE
ID NIN_MOUSE Reviewed; 2113 AA.
AC Q61043; A0A1Y7VJL5; B2RQ73; B7ZMZ9; E9Q488; E9Q4S3; Q674R4; Q6ZPM7;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-APR-2018, sequence version 4.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Ninein {ECO:0000303|PubMed:8834802};
GN Name=Nin {ECO:0000312|MGI:MGI:105108};
GN Synonyms=Kiaa1565 {ECO:0000312|MGI:MGI:105108};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Neonatal macrophage;
RX PubMed=8834802; DOI=10.1242/jcs.109.1.179;
RA Bouckson-Castaing V., Moudjou M., Ferguson D.J.P., Mucklow S., Belkaid Y.,
RA Milon G., Crocker P.R.;
RT "Molecular characterisation of ninein, a new coiled-coil protein of the
RT centrosome.";
RL J. Cell Sci. 109:179-190(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TUBGCP3 AND GAMMA
RP TUBULIN, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAS87211.1};
RX PubMed=15784680; DOI=10.1242/jcs.02302;
RA Delgehyr N., Sillibourne J., Bornens M.;
RT "Microtubule nucleation and anchoring at the centrosome are independent
RT processes linked by ninein function.";
RL J. Cell Sci. 118:1565-1575(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain {ECO:0000312|EMBL:AAI37790.1};
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 FUNCTION.
RX PubMed=10934040; DOI=10.1242/jcs.113.17.3013;
RA Mogensen M.M., Malik A., Piel M., Bouckson-Castaing V., Bornens M.;
RT "Microtubule minus-end anchorage at centrosomal and non-centrosomal sites:
RT the role of ninein.";
RL J. Cell Sci. 113:3013-3023(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-269 AND SER-1826, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP IDENTIFICATION OF ISOFORM 4, INTERACTION WITH CEP170 AND CEP250,
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 4), AND DEVELOPMENTAL STAGE (ISOFORM
RP 4).
RX PubMed=27565344; DOI=10.1016/j.cell.2016.07.025;
RA Zhang X., Chen M.H., Wu X., Kodani A., Fan J., Doan R., Ozawa M., Ma J.,
RA Yoshida N., Reiter J.F., Black D.L., Kharchenko P.V., Sharp P.A.,
RA Walsh C.A.;
RT "Cell-type-specific alternative splicing governs cell fate in the
RT developing cerebral cortex.";
RL Cell 166:1147-1162(2016).
CC -!- FUNCTION: Centrosomal protein required for the positioning and
CC anchorage of the microtubule minus-end in epithelial cells
CC (PubMed:15784680, PubMed:10934040). May also act as a centrosome
CC maturation factor (By similarity). May play a role in microtubule
CC nucleation, by recruiting the gamma-tubulin ring complex to the
CC centrosome (PubMed:15784680). Overexpression does not perturb
CC nucleation or elongation of microtubules but suppresses release of
CC microtubules (By similarity). Required for centriole organization and
CC microtubule anchoring at the mother centriole (By similarity).
CC {ECO:0000250|UniProtKB:Q8N4C6, ECO:0000269|PubMed:10934040,
CC ECO:0000269|PubMed:15784680}.
CC -!- SUBUNIT: Homooligomer (By similarity). Interacts with GSK3B/GSK3-beta
CC via its C-terminal domain (By similarity). Interacts with C14ORF166,
CC such interaction may prevent its phosphorylation by GSK3B (By
CC similarity). Interacts with AUNIP (via N-terminus) (By similarity).
CC Identified in a complex with AUNIP and AURKA (By similarity). Interacts
CC with CCDC120 (By similarity). Interacts (via C-terminus) with CEP250
CC (PubMed:27565344). Interacts with CEP170 (PubMed:27565344). Interacts
CC (via N-terminus) with the gamma-tubulin ring complex component TUBGCP3
CC (PubMed:15784680). Interacts with gamma-tubulin (PubMed:15784680).
CC Isoform 4 does not interact with CEP170 or CEP250 (PubMed:27565344).
CC {ECO:0000250|UniProtKB:Q8N4C6, ECO:0000269|PubMed:15784680,
CC ECO:0000269|PubMed:27565344}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:27565344,
CC ECO:0000269|PubMed:8834802}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:15784680}.
CC Note=Component of the core centrosome. Arranged in a tubular
CC conformation with an open and a closed end within the centrosome. In
CC the mother centrosome, it localizes at both ends of the centrosome
CC tube, including the site of centrosome duplication, while in the
CC daughter centrosome it is present only at the closed end. Requires PCM1
CC for centrosome localization. Localizes to the subdistal appendage
CC region of the centriole in a DCTN1-dependent manner.
CC {ECO:0000250|UniProtKB:Q8N4C6}.
CC -!- SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm
CC {ECO:0000269|PubMed:27565344}. Note=Seems to have a dominant-negative
CC effect on localization of other isoforms, promoting their dissociation
CC from the centrosome. {ECO:0000269|PubMed:27565344}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=NPC-CT {ECO:0000303|PubMed:27565344};
CC IsoId=Q61043-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61043-2; Sequence=VSP_059555, VSP_059556;
CC Name=3;
CC IsoId=Q61043-1; Sequence=VSP_059552, VSP_059555, VSP_059556;
CC Name=4; Synonyms=Neuron {ECO:0000303|PubMed:27565344};
CC IsoId=Q61043-4; Sequence=VSP_059551, VSP_059553, VSP_059554;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in spleen, bone
CC marrow and skin. Weakly expressed in liver and small intestine.
CC Expressed in brain. {ECO:0000269|PubMed:8834802}.
CC -!- DEVELOPMENTAL STAGE: Associated with the centrosome throughout the cell
CC cycle (PubMed:8834802). During mitosis, it is associated with the
CC centrosome and the mitotic spindle (PubMed:8834802). At anaphase, it is
CC only localized to centrosomes (PubMed:8834802). Isoform 4 is highly
CC expressed in postmitotic cortical neurons during neurogenesis
CC (PubMed:27565344). {ECO:0000269|PubMed:27565344,
CC ECO:0000269|PubMed:8834802}.
CC -!- DOMAIN: There is conflicting information regarding the regions required
CC for centrosomal localization (PubMed:15784680). One study shows that
CC the region 1591-1671 is necessary and sufficient for targeting to the
CC centrosome (By similarity). Another study shows that a separate region
CC within the coiled-coil domain, 1279-1565, is important for centrosomal
CC localization (By similarity). However, a third study shows that the
CC coiled-coil region (373-1874) is not sufficient for centrosomal
CC localization and instead localizes to cytoplasmic speckles
CC (PubMed:15784680). The observed differences might be due to
CC oligomerization of the longer coiled-coil domain-containing sequence,
CC which would mask the shorter centrosomal targeting sequences
CC (PubMed:15784680). {ECO:0000250|UniProtKB:Q8N4C6,
CC ECO:0000269|PubMed:15784680}.
CC -!- DOMAIN: The N-terminal domain is important for targeting to the mother
CC centriole, although it is not sufficient by itself for centrosomal
CC localization. {ECO:0000269|PubMed:8834802}.
CC -!- PTM: Phosphorylated by AURKA/Aurora kinase A and PKA kinases but not
CC CK2 or AURKB/Aurora kinase B.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA83234.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC98204.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=AAA83234.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U40342; AAA83234.1; ALT_SEQ; mRNA.
DR EMBL; AY515727; AAS87211.1; -; mRNA.
DR EMBL; AK129394; BAC98204.1; ALT_INIT; mRNA.
DR EMBL; AC112146; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC137789; AAI37790.1; -; mRNA.
DR EMBL; BC144913; AAI44914.1; -; mRNA.
DR CCDS; CCDS36468.1; -. [Q61043-3]
DR CCDS; CCDS36469.1; -. [Q61043-1]
DR PIR; T30171; T30171.
DR RefSeq; NP_001074922.1; NM_001081453.1. [Q61043-3]
DR RefSeq; NP_001273008.1; NM_001286079.2. [Q61043-1]
DR RefSeq; NP_001273009.1; NM_001286080.2. [Q61043-2]
DR RefSeq; NP_032723.2; NM_008697.4. [Q61043-1]
DR RefSeq; XP_011242311.1; XM_011244009.1. [Q61043-3]
DR AlphaFoldDB; Q61043; -.
DR SMR; Q61043; -.
DR BioGRID; 201772; 4.
DR IntAct; Q61043; 3.
DR MINT; Q61043; -.
DR STRING; 10090.ENSMUSP00000082422; -.
DR iPTMnet; Q61043; -.
DR PhosphoSitePlus; Q61043; -.
DR EPD; Q61043; -.
DR jPOST; Q61043; -.
DR MaxQB; Q61043; -.
DR PaxDb; Q61043; -.
DR PRIDE; Q61043; -.
DR ProteomicsDB; 252836; -. [Q61043-3]
DR ProteomicsDB; 252837; -. [Q61043-2]
DR ProteomicsDB; 312470; -.
DR ProteomicsDB; 333011; -.
DR Antibodypedia; 23688; 151 antibodies from 24 providers.
DR DNASU; 18080; -.
DR Ensembl; ENSMUST00000021468; ENSMUSP00000021468; ENSMUSG00000021068. [Q61043-1]
DR Ensembl; ENSMUST00000085314; ENSMUSP00000082422; ENSMUSG00000021068. [Q61043-3]
DR Ensembl; ENSMUST00000095666; ENSMUSP00000093327; ENSMUSG00000021068. [Q61043-1]
DR Ensembl; ENSMUST00000169074; ENSMUSP00000129648; ENSMUSG00000021068. [Q61043-1]
DR Ensembl; ENSMUST00000220689; ENSMUSP00000152530; ENSMUSG00000021068. [Q61043-4]
DR Ensembl; ENSMUST00000222237; ENSMUSP00000152240; ENSMUSG00000021068. [Q61043-3]
DR GeneID; 18080; -.
DR KEGG; mmu:18080; -.
DR UCSC; uc007ntf.1; mouse.
DR UCSC; uc007ntg.2; mouse. [Q61043-3]
DR UCSC; uc007nth.2; mouse. [Q61043-2]
DR CTD; 51199; -.
DR MGI; MGI:105108; Nin.
DR VEuPathDB; HostDB:ENSMUSG00000021068; -.
DR eggNOG; ENOG502QZCC; Eukaryota.
DR GeneTree; ENSGT00660000095541; -.
DR HOGENOM; CLU_001462_1_1_1; -.
DR InParanoid; Q61043; -.
DR OMA; QKVELLX; -.
DR OrthoDB; 95801at2759; -.
DR TreeFam; TF325139; -.
DR BioGRID-ORCS; 18080; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Nin; mouse.
DR PRO; PR:Q61043; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q61043; protein.
DR Bgee; ENSMUSG00000021068; Expressed in cortical plate and 234 other tissues.
DR ExpressionAtlas; Q61043; baseline and differential.
DR Genevisible; Q61043; MM.
DR GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0044295; C:axonal growth cone; IDA:MGI.
DR GO; GO:0120103; C:centriolar subdistal appendage; ISO:MGI.
DR GO; GO:0005814; C:centriole; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0097539; C:ciliary transition fiber; IDA:MGI.
DR GO; GO:0005881; C:cytoplasmic microtubule; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000242; C:pericentriolar material; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0019900; F:kinase binding; IPI:MGI.
DR GO; GO:0051011; F:microtubule minus-end binding; IDA:MGI.
DR GO; GO:0010457; P:centriole-centriole cohesion; ISO:MGI.
DR GO; GO:0051642; P:centrosome localization; IMP:MGI.
DR GO; GO:0090222; P:centrosome-templated microtubule nucleation; IMP:MGI.
DR GO; GO:0048668; P:collateral sprouting; IGI:MGI.
DR GO; GO:0021540; P:corpus callosum morphogenesis; IGI:MGI.
DR GO; GO:0021957; P:corticospinal tract morphogenesis; IGI:MGI.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; IMP:MGI.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IGI:MGI.
DR GO; GO:0008104; P:protein localization; ISO:MGI.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR029664; NIN.
DR PANTHER; PTHR18905:SF11; PTHR18905:SF11; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 5.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; GTP-binding;
KW Microtubule; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..2113
FT /note="Ninein"
FT /id="PRO_0000096845"
FT DOMAIN 8..43
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 42..77
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 182..217
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 219..252
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 317..352
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 578..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..1495
FT /note="Important for interaction with CEP170"
FT /evidence="ECO:0000269|PubMed:27565344"
FT REGION 1899..1922
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1988..2008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 358..570
FT /evidence="ECO:0000255"
FT COILED 620..926
FT /evidence="ECO:0000255"
FT COILED 958..1008
FT /evidence="ECO:0000255"
FT COILED 1175..1323
FT /evidence="ECO:0000255"
FT COILED 1425..1806
FT /evidence="ECO:0000255"
FT COILED 1852..1910
FT /evidence="ECO:0000255"
FT COILED 1971..2093
FT /evidence="ECO:0000255"
FT BINDING 245..252
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 300..304
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 420..423
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 152
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N4C6"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1540
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N4C6"
FT MOD_RES 1826
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 797..1503
FT /note="Missing (in isoform 4)"
FT /id="VSP_059551"
FT VAR_SEQ 1940
FT /note="Q -> QVRLDEKLME (in isoform 3)"
FT /id="VSP_059552"
FT VAR_SEQ 1941..1979
FT /note="MQPLRSTVTRSPSSHWDLQLLQQQACPMVPREQFLQLQQ -> VRLDEKLME
FT SSVVGSSRAGRSSVPELACEDAAPEVHCDA (in isoform 4)"
FT /id="VSP_059553"
FT VAR_SEQ 1980..2113
FT /note="Missing (in isoform 4)"
FT /id="VSP_059554"
FT VAR_SEQ 2007..2026
FT /note="GNQEHLVNLMEERMIEVEQK -> ALLLEQRAVHADSCRRIGHL (in
FT isoform 2 and isoform 3)"
FT /id="VSP_059555"
FT VAR_SEQ 2027..2113
FT /note="Missing (in isoform 2 and isoform 3)"
FT /id="VSP_059556"
FT CONFLICT 145..146
FT /note="EH -> DD (in Ref. 1; AAA83234)"
FT /evidence="ECO:0000305"
FT CONFLICT 341..342
FT /note="EL -> DV (in Ref. 1; AAA83234)"
FT /evidence="ECO:0000305"
FT CONFLICT 383..394
FT /note="KEKLRSDLDKAE -> RRAYGRTWTSR (in Ref. 1; AAA83234)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="R -> A (in Ref. 1; AAA83234)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="Y -> H (in Ref. 3; BAC98204)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="E -> K (in Ref. 2; AAS87211)"
FT /evidence="ECO:0000305"
FT CONFLICT 737
FT /note="S -> T (in Ref. 1; AAA83234)"
FT /evidence="ECO:0000305"
FT CONFLICT 862
FT /note="T -> A (in Ref. 1; AAA83234)"
FT /evidence="ECO:0000305"
FT CONFLICT 909
FT /note="K -> E (in Ref. 1; AAA83234, 3; BAC98204, 5;
FT AAI37790/AAI44914 and 2; AAS87211)"
FT /evidence="ECO:0000305"
FT CONFLICT 963..964
FT /note="QQ -> PE (in Ref. 1; AAA83234)"
FT /evidence="ECO:0000305"
FT CONFLICT 1084..1085
FT /note="SR -> YQ (in Ref. 1; AAA83234 and 2; AAS87211)"
FT /evidence="ECO:0000305"
FT CONFLICT 1084
FT /note="S -> Y (in Ref. 3; BAC98204 and 5; AAI37790/
FT AAI44914)"
FT /evidence="ECO:0000305"
FT CONFLICT 1155
FT /note="E -> K (in Ref. 1; AAA83234 and 2; AAS87211)"
FT /evidence="ECO:0000305"
FT CONFLICT 1182
FT /note="Missing (in Ref. 1; AAA83234)"
FT /evidence="ECO:0000305"
FT CONFLICT 1327
FT /note="A -> P (in Ref. 2; AAS87211)"
FT /evidence="ECO:0000305"
FT CONFLICT 1336..1339
FT /note="LWEA -> SGKP (in Ref. 1; AAA83234)"
FT /evidence="ECO:0000305"
FT CONFLICT 1487..1490
FT /note="DLQI -> PAV (in Ref. 1; AAA83234)"
FT /evidence="ECO:0000305"
FT CONFLICT 1653..1654
FT /note="EV -> RI (in Ref. 1; AAA83234)"
FT /evidence="ECO:0000305"
FT CONFLICT 1687
FT /note="F -> L (in Ref. 1; AAA83234)"
FT /evidence="ECO:0000305"
FT CONFLICT 1694
FT /note="I -> V (in Ref. 1; AAA83234)"
FT /evidence="ECO:0000305"
FT CONFLICT 1759
FT /note="N -> D (in Ref. 1; AAA83234)"
FT /evidence="ECO:0000305"
FT CONFLICT 1788
FT /note="L -> V (in Ref. 1; AAA83234)"
FT /evidence="ECO:0000305"
FT CONFLICT 1841
FT /note="L -> F (in Ref. 5; AAI44914)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2113 AA; 243718 MW; F3A2EEBD3E9FC826 CRC64;
MDEVEEDQHE ARLKELFDSF DTLGTGSLGQ EELTDLCHVL CLEDVGPVLQ QTLLQDNLLG
RVHFDQFKEA LILILSRTLS SEEHFEESDC SPEAQPKYVR GGKRYGRRSL PEFQESGEEI
EEVTVLEPLE EEARSSPIPA GDCGEHWKTQ RSEEYEAEGQ LRFWNPDDLN ASHGGSCPPP
DWIEEKLQEV CEDLGITRDG HLNRKKLVSI CEQYGLQNVD GAMLEEVFLS LDPDGTMSVE
DFFYGLFKTG KSLTPSASTP YRQLKRHLSM QSFDESGRRT ATSSAMTSTI GFRVFSCLDD
GMGQASVERI LDTWQEEGIE NSQEILKALD FSLDGNINLT ELTLALENEL LVTKNGIHQA
ALASFKAEIR HLLERVDQVV REKEKLRSDL DKAEKLKSLM ASEVDDHHAA IERRNEYNLR
KLDEEYKERI AALKNELRQE REQMLQQVGK QRVELEQEIQ KAKTEENYIR DRLALSLKEN
NRLETELLEN AEKLAEYESL TQKLQRSLEN VLAEKFGDLD PSSAEFFLQE ERLAQMRNEY
EQQCRLLQDQ VDELQSELEE YQAQGRVLRL PLKNSLSEEL DGHSGGIEPD QGPGSEECNP
LNMSIEAELV IEQMKEQHHR DLCHLRLELE DKVRHYEKQL DDTRVASEQE QAAMKQKYEQ
GVHTLEKRVS ELRSEIADLE GQAAVLREAH HKASCRHEEE KRQLQMAFDE EKAQLQEELR
QEHERELQAR LQQAAESFRQ EREGLAQAAW TEEKVRGLEQ SYQEQLLSLE EKHALEKEEL
REELSEHHRR ELQEGREEME TECNRRVSQI EAQCQADCEK VTEHCEQTLQ SLEVRHRQEL
RDLLDQHLEE RSQWEFEKDE LTQECTDAQE QLKEALQRER ATAAAMKQEQ EILERTYKDR
LNILSTERKQ LLQDLKDLQN ASESQHGLLS GQILELKRSQ ERELRDQGQA LCQTGVSEQL
ASQQLERLRV EHEQERREMT GKLAALESAH RASLERADQE KAEMSTEICR LQNTVKDMQQ
AASLLMLQGG CQATAGEEAE GDGAMSLLQQ GEQLLEENGD VLISLQRAHE HAVKENAKMA
TEISRLQQRL KKLEPGSVIS SCLEEGTSEI SGSSREQVEP IMKQGPATKH FLSDLGDHEA
RDLASTGTSS VQRQECKTEA SEASLDCFSE LENSEDTRTE SWDLKSQISQ LREQLTVLRA
DCDRASERKQ DLLFDISVLK KKLKMLERLP EASSRYKVLY EDAARENSCL QEELRLVETR
YEESLDSNKE LTAEVYRLQD EMKKMEEVME TFLSLEKSYD EVKVENEELR ALVLRLQGKM
EKVLGRAALQ GDSYALWEAP SENLEVASDE KMLELRQTPK ECTPKVVSMH HIIEECTQET
QCCEQGSTKL LARIKAHEIA WFHRAIKTHP EKPSAQNRVI PEGSAALLGL QDKHLQQEAT
IAELELEKQK LQELTRNLRE RVTALVRQKD APSQGQKEEE LKAMMQDLQI TCGEMQRKVE
LLRYESEKLQ EENSILRNEI TTLNEEDSIS NLKLEELNGS QEELWQKIET IEQEKASIQT
MVEKLKKQVS DLKIKNQQLD SENIELSQKN SQNKEELKTL NQRLAEMLCQ REEPGACTSE
KWEQENASLK EELDHYKVQT STLVSSLEAE LSEVKLQTHV MEQENLLLKD ELERLKQLHR
CPDLSDFQQK MSSILSYNEK LLKEKEVLSE ELKSCADKLA ESSLLEHRIA TMKQEQTAWE
EQSESLKSQL AVSQAKVQNL EDVLQNVNLQ MAEIESDLQV TRQEKEALKQ EVMSLHRQLQ
NAIDKDWVSE TAPHLSGLRG QQRRLSWDKL DHLMNEEPQL LCQESKRLQT VVQNTQADLT
HSREKVRQLE SNLLPTKHQK QLNQPCTVKS TEQEKLTLKR ECEQSQKEQS PTSRKVGQMG
SLERGLETIH LENEGLKKKQ MQPLRSTVTR SPSSHWDLQL LQQQACPMVP REQFLQLQQQ
LLQAEKRSQH LQEELENRTS ETNTPQGNQE HLVNLMEERM IEVEQKLKLV KRLLQEKVNQ
LKEQLCKNTK TDAVVKDLYV ENAQLLKALE MTEQRQKTAE KRNFLLEEKI ASLSTIVRNL
APAPLTSMPP LRS
