AP180_HUMAN
ID AP180_HUMAN Reviewed; 907 AA.
AC O60641; A8K0L7; E5RI02; Q5JX13; Q68DL9; Q6P9D3; Q9NTY7;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1999, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Clathrin coat assembly protein AP180;
DE AltName: Full=91 kDa synaptosomal-associated protein;
DE AltName: Full=Clathrin coat-associated protein AP180;
DE AltName: Full=Phosphoprotein F1-20;
GN Name=SNAP91; Synonyms=KIAA0656;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 794-907.
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH AP2B1.
RX PubMed=16903783; DOI=10.1371/journal.pbio.0040262;
RA Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y.,
RA Mills I.G., Benmerah A., McMahon H.T.;
RT "Role of the AP2 beta-appendage hub in recruiting partners for clathrin-
RT coated vesicle assembly.";
RL PLoS Biol. 4:E262-E262(2006).
CC -!- FUNCTION: Adaptins are components of the adapter complexes which link
CC clathrin to receptors in coated vesicles. Clathrin-associated protein
CC complexes are believed to interact with the cytoplasmic tails of
CC membrane proteins, leading to their selection and concentration.
CC Binding of AP180 to clathrin triskelia induces their assembly into 60-
CC 70 nm coats (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds AP2A2. Interacts with AP2B1; clathrin competes with
CC SNAP91 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O60641; Q9CR95: Necap1; Xeno; NbExp=2; IntAct=EBI-1105187, EBI-7592476;
CC O60641-3; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-12854506, EBI-11096309;
CC O60641-3; P55040: GEM; NbExp=3; IntAct=EBI-12854506, EBI-744104;
CC O60641-3; Q53GS7: GLE1; NbExp=3; IntAct=EBI-12854506, EBI-1955541;
CC O60641-3; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-12854506, EBI-2548751;
CC O60641-3; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-12854506, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}. Membrane, coated pit
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Component of the coat surrounding the
CC cytoplasmic face of coated vesicles in the plasma membrane.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O60641-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60641-2; Sequence=VSP_020997;
CC Name=3;
CC IsoId=O60641-3; Sequence=VSP_020998, VSP_020999, VSP_021000;
CC Name=4;
CC IsoId=O60641-4; Sequence=VSP_020999, VSP_047049;
CC -!- DOMAIN: Possesses a three domain structure: the N-terminal 300 residues
CC harbor a clathrin binding site, an acidic middle domain 450 residues,
CC interrupted by an Ala-rich segment, and the C-terminal domain (166
CC residues).
CC -!- PTM: Thr-310 can be modified by the addition of N-acetylglucosamine
CC which can be further phosphorylated. There is no evidence for direct
CC Thr-310 phosphorylation (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PICALM/SNAP91 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31631.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAH18201.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AB014556; BAA31631.2; ALT_INIT; mRNA.
DR EMBL; AK289582; BAF82271.1; -; mRNA.
DR EMBL; CR749348; CAH18201.1; ALT_SEQ; mRNA.
DR EMBL; AL109915; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF054993; AAC09352.1; -; mRNA.
DR EMBL; BC060818; AAH60818.1; -; mRNA.
DR CCDS; CCDS47455.1; -. [O60641-1]
DR CCDS; CCDS56437.1; -. [O60641-3]
DR CCDS; CCDS56438.1; -. [O60641-4]
DR RefSeq; NP_001229721.1; NM_001242792.1. [O60641-1]
DR RefSeq; NP_001229722.1; NM_001242793.1. [O60641-4]
DR RefSeq; NP_001229723.1; NM_001242794.1. [O60641-3]
DR RefSeq; NP_001243646.1; NM_001256717.1.
DR RefSeq; NP_001243647.1; NM_001256718.1.
DR RefSeq; NP_055656.1; NM_014841.2. [O60641-1]
DR RefSeq; XP_005248827.1; XM_005248770.4. [O60641-1]
DR RefSeq; XP_006715678.1; XM_006715615.1. [O60641-1]
DR RefSeq; XP_011534567.1; XM_011536265.1. [O60641-1]
DR RefSeq; XP_011534568.1; XM_011536266.1. [O60641-1]
DR AlphaFoldDB; O60641; -.
DR SMR; O60641; -.
DR BioGRID; 115222; 54.
DR ELM; O60641; -.
DR IntAct; O60641; 18.
DR MINT; O60641; -.
DR STRING; 9606.ENSP00000400459; -.
DR GlyConnect; 64; 1 O-Linked glycan.
DR GlyGen; O60641; 8 sites, 1 O-linked glycan (8 sites).
DR iPTMnet; O60641; -.
DR PhosphoSitePlus; O60641; -.
DR SwissPalm; O60641; -.
DR BioMuta; SNAP91; -.
DR EPD; O60641; -.
DR jPOST; O60641; -.
DR MassIVE; O60641; -.
DR MaxQB; O60641; -.
DR PaxDb; O60641; -.
DR PeptideAtlas; O60641; -.
DR PRIDE; O60641; -.
DR ProteomicsDB; 16144; -.
DR ProteomicsDB; 49493; -. [O60641-1]
DR ProteomicsDB; 49494; -. [O60641-2]
DR ProteomicsDB; 49495; -. [O60641-3]
DR Antibodypedia; 4056; 112 antibodies from 23 providers.
DR DNASU; 9892; -.
DR Ensembl; ENST00000369694.7; ENSP00000358708.2; ENSG00000065609.15. [O60641-1]
DR Ensembl; ENST00000439399.6; ENSP00000400459.2; ENSG00000065609.15. [O60641-1]
DR Ensembl; ENST00000520213.5; ENSP00000428026.1; ENSG00000065609.15. [O60641-3]
DR Ensembl; ENST00000520302.5; ENSP00000428511.1; ENSG00000065609.15. [O60641-4]
DR Ensembl; ENST00000521743.5; ENSP00000428215.1; ENSG00000065609.15. [O60641-1]
DR GeneID; 9892; -.
DR KEGG; hsa:9892; -.
DR MANE-Select; ENST00000369694.7; ENSP00000358708.2; NM_001242792.2; NP_001229721.1.
DR UCSC; uc003pkc.4; human. [O60641-1]
DR CTD; 9892; -.
DR DisGeNET; 9892; -.
DR GeneCards; SNAP91; -.
DR HGNC; HGNC:14986; SNAP91.
DR HPA; ENSG00000065609; Group enriched (brain, pituitary gland, retina).
DR MIM; 607923; gene.
DR neXtProt; NX_O60641; -.
DR OpenTargets; ENSG00000065609; -.
DR PharmGKB; PA37956; -.
DR VEuPathDB; HostDB:ENSG00000065609; -.
DR eggNOG; KOG0251; Eukaryota.
DR GeneTree; ENSGT00950000183068; -.
DR HOGENOM; CLU_014080_3_0_1; -.
DR InParanoid; O60641; -.
DR OMA; CNEGVIN; -.
DR OrthoDB; 1592722at2759; -.
DR PhylomeDB; O60641; -.
DR TreeFam; TF314861; -.
DR PathwayCommons; O60641; -.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR SignaLink; O60641; -.
DR SIGNOR; O60641; -.
DR BioGRID-ORCS; 9892; 20 hits in 1063 CRISPR screens.
DR ChiTaRS; SNAP91; human.
DR GeneWiki; SNAP91; -.
DR GenomeRNAi; 9892; -.
DR Pharos; O60641; Tbio.
DR PRO; PR:O60641; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O60641; protein.
DR Bgee; ENSG00000065609; Expressed in middle temporal gyrus and 141 other tissues.
DR ExpressionAtlas; O60641; baseline and differential.
DR Genevisible; O60641; HS.
DR GO; GO:0005905; C:clathrin-coated pit; IBA:GO_Central.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0098894; C:extrinsic component of presynaptic endocytic zone membrane; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IBA:GO_Central.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0032050; F:clathrin heavy chain binding; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0048268; P:clathrin coat assembly; IEA:InterPro.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:2000369; P:regulation of clathrin-dependent endocytosis; IMP:MGI.
DR GO; GO:0016185; P:synaptic vesicle budding from presynaptic endocytic zone membrane; IBA:GO_Central.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR Gene3D; 1.20.58.150; -; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR011417; ANTH_dom.
DR InterPro; IPR014712; ANTH_dom_sf.
DR InterPro; IPR030428; AP180.
DR InterPro; IPR045192; AP180-like.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR PANTHER; PTHR22951; PTHR22951; 1.
DR PANTHER; PTHR22951:SF4; PTHR22951:SF4; 1.
DR Pfam; PF07651; ANTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SUPFAM; SSF48464; SSF48464; 1.
DR PROSITE; PS50942; ENTH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coated pit; Glycoprotein; Membrane;
KW Methylation; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..907
FT /note="Clathrin coat assembly protein AP180"
FT /id="PRO_0000193864"
FT DOMAIN 14..145
FT /note="ENTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00243"
FT REGION 285..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05140"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05140"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05140"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61548"
FT MOD_RES 317
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q61548"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05140"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05140"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05140"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05140"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05140"
FT MOD_RES 865
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q61548"
FT MOD_RES 865
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q61548"
FT CARBOHYD 310
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 59..907
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_020997"
FT VAR_SEQ 256..269
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020998"
FT VAR_SEQ 293..295
FT /note="NEG -> K (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020999"
FT VAR_SEQ 381..671
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021000"
FT VAR_SEQ 616..643
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047049"
FT CONFLICT 4
FT /note="Q -> R (in Ref. 5; AAH60818)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 907 AA; 92502 MW; 23959C2B54F5EBF1 CRC64;
MSGQTLTDRI AAAQYSVTGS AVARAVCKAT THEVMGPKKK HLDYLIQATN ETNVNIPQMA
DTLFERATNS SWVVVFKALV TTHHLMVHGN ERFIQYLASR NTLFNLSNFL DKSGSHGYDM
STFIRRYSRY LNEKAFSYRQ MAFDFARVKK GADGVMRTMA PEKLLKSMPI LQGQIDALLE
FDVHPNELTN GVINAAFMLL FKDLIKLFAC YNDGVINLLE KFFEMKKGQC KDALEIYKRF
LTRMTRVSEF LKVAEQVGID KGDIPDLTQA PSSLMETLEQ HLNTLEGKKP GNNEGSGAPS
PLSKSSPATT VTSPNSTPAK TIDTSPPVDL FATASAAVPV STSKPSSDLL DLQPDFSSGG
AAAAAAPAPP PPAGGATAWG DLLGEDSLAA LSSVPSEAQI SDPFAPEPTP PTTTAEIATA
SASASTTTTV TAVTAEVDLF GDAFAASPGE APAASEGAAA PATPTPVAAA LDACSGNDPF
APSEGSAEAA PELDLFAMKP PETSVPVVTP TASTAPPVPA TAPSPAPAVA AAAAATTAAT
AAATTTTTTS AATATTAPPA LDIFGDLFES TPEVAAAPKP DAAPSIDLFS TDAFSSPPQG
ASPVPESSLT ADLLSVDAFA APSPATTASP AKVDSSGVID LFGDAFGSSA SEPQPASQAA
SSSSASADLL AGFGGSFMAP SPSPVTPAQN NLLQPNFEAA FGTTPSTSSS SSFDPSVFDG
LGDLLMPTMA PAGQPAPVSM VPPSPAMAAS KALGSDLDSS LASLVGNLGI SGTTTKKGDL
QWNAGEKKLT GGANWQPKVA PATWSAGVPP SAPLQGAVPP TSSVPPVAGA PSVGQPGAGF
GMPPAGTGMP MMPQQPVMFA QPMMRPPFGA AAVPGTQLSP SPTPASQSPK KPPAKDPLAD
LNIKDFL
