ID   TPC11_HUMAN             Reviewed;        1133 AA.
AC   Q7Z392; A4QPB8; B2RCD6; Q5U5I7; Q6FI73; Q86T25; Q9H0L1; Q9H5K9; Q9H8Q1;
AC   Q9H9I7;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   28-JAN-2026, entry version 152.
DE   RecName: Full=Trafficking protein particle complex subunit 11;
GN   Name=TRAPPC11; Synonyms=C4orf41;
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] (ISOFORMS 1 AND 4).
RC   TISSUE=Colon epithelium, and Endometrium;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 199-1133 (ISOFORM 1).
RC   TISSUE=Ovary, and Trachea;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 319-1133 (ISOFORM 1).
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 298-1133 (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA   Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA   Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA   Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA   Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA   Klein M., Poustka A.;
RT   "Towards a catalog of human genes and proteins: sequencing and analysis of
RT   500 novel complete protein coding human cDNAs.";
RL   Genome Res. 11:422-435(2001).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-245, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [7]
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   [8]
RP   FUNCTION, AND IDENTIFICATION IN TRAPP COMPLEX.
RX   PubMed=21525244; DOI=10.1091/mbc.e10-11-0873;
RA   Scrivens P.J., Noueihed B., Shahrzad N., Hul S., Brunet S., Sacher M.;
RT   "C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early
RT   stage in ER-to-Golgi trafficking.";
RL   Mol. Biol. Cell 22:2083-2093(2011).
RN   [9]
RP   VARIANT LGMDR18 ARG-980.
RX   PubMed=23830518; DOI=10.1016/j.ajhg.2013.05.028;
RA   Boegershausen N., Shahrzad N., Chong J.X., von Kleist-Retzow J.C.,
RA   Stanga D., Li Y., Bernier F.P., Loucks C.M., Wirth R., Puffenberger E.G.,
RA   Hegele R.A., Schreml J., Lapointe G., Keupp K., Brett C.L., Anderson R.,
RA   Hahn A., Innes A.M., Suchowersky O., Mets M.B., Nuernberg G., McLeod D.R.,
RA   Thiele H., Waggoner D., Altmueller J., Boycott K.M., Schoser B.,
RA   Nuernberg P., Ober C., Heller R., Parboosingh J.S., Wollnik B., Sacher M.,
RA   Lamont R.E.;
RT   "Recessive TRAPPC11 mutations cause a disease spectrum of limb girdle
RT   muscular dystrophy and myopathy with movement disorder and intellectual
RT   disability.";
RL   Am. J. Hum. Genet. 93:181-190(2013).
RN   [10]
RP   VARIANTS ALA-381 AND ALA-1104, INVOLVEMENT IN DISEASE, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=27862579; DOI=10.1002/humu.23145;
RA   Matalonga L., Bravo M., Serra-Peinado C., Garcia-Pelegri E., Ugarteburu O.,
RA   Vidal S., Llambrich M., Quintana E., Fuster-Jorge P., Gonzalez-Bravo M.N.,
RA   Beltran S., Dopazo J., Garcia-Garcia F., Foulquier F., Matthijs G.,
RA   Mills P., Ribes A., Egea G., Briones P., Tort F., Giros M.;
RT   "Mutations in TRAPPC11 are associated with a congenital disorder of
RT   glycosylation.";
RL   Hum. Mutat. 38:148-151(2017).
RN   [11]
RP   VARIANT LGMDR18 PRO-284.
RX   PubMed=29855340; DOI=10.1186/s13395-018-0163-0;
RA   Larson A.A., Baker P.R. II, Milev M.P., Press C.A., Sokol R.J., Cox M.O.,
RA   Lekostaj J.K., Stence A.A., Bossler A.D., Mueller J.M., Prematilake K.,
RA   Tadjo T.F., Williams C.A., Sacher M., Moore S.A.;
RT   "TRAPPC11 and GOSR2 mutations associate with hypoglycosylation of alpha-
RT   dystroglycan and muscular dystrophy.";
RL   Skelet. Muscle 8:17-17(2018).
CC   -!- FUNCTION: Involved in endoplasmic reticulum to Golgi apparatus
CC       trafficking at a very early stage. {ECO:0000269|PubMed:21525244,
CC       ECO:0000269|PubMed:27862579}.
CC   -!- SUBUNIT: Component of the multisubunit TRAPP (transport protein
CC       particle) complex, which includes at least TRAPPC2, TRAPPC2L, TRAPPC3,
CC       TRAPPC3L, TRAPPC4, TRAPPC5, TRAPPC8, TRAPPC9, TRAPPC10, TRAPPC11 and
CC       TRAPPC12. {ECO:0000269|PubMed:21525244}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:27862579}.
CC       Golgi apparatus, cis-Golgi network {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q7Z392-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z392-2; Sequence=VSP_035095, VSP_035098, VSP_035099;
CC       Name=3;
CC         IsoId=Q7Z392-3; Sequence=VSP_035098, VSP_035099;
CC       Name=4;
CC         IsoId=Q7Z392-4; Sequence=VSP_035096, VSP_035097;
CC   -!- DISEASE: Muscular dystrophy, limb-girdle, autosomal recessive 18
CC       (LGMDR18) [MIM:615356]: A form of limb-girdle muscular dystrophy
CC       characterized by proximal muscle weakness with childhood onset,
CC       resulting in gait abnormalities and scapular winging. Serum creatine
CC       kinase is increased. A subset of patients may show a hyperkinetic
CC       movement disorder with chorea, ataxia, or dystonia and global
CC       developmental delay. {ECO:0000269|PubMed:23830518,
CC       ECO:0000269|PubMed:29855340}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the TRAPPC11 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB14240.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB14556.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB15617.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAG37533.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAB66686.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAD91169.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAD97983.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL833571; CAD91169.1; ALT_INIT; mRNA.
DR   EMBL; BX538044; CAD97983.1; ALT_INIT; mRNA.
DR   EMBL; BC051724; AAH51724.1; -; mRNA.
DR   EMBL; BC139745; AAI39746.1; -; mRNA.
DR   EMBL; AK022778; BAB14240.1; ALT_INIT; mRNA.
DR   EMBL; AK023390; BAB14556.1; ALT_INIT; mRNA.
DR   EMBL; AK026992; BAB15617.1; ALT_SEQ; mRNA.
DR   EMBL; AK315057; BAG37533.1; ALT_INIT; mRNA.
DR   EMBL; CR533553; CAG38584.1; -; mRNA.
DR   EMBL; AL136752; CAB66686.1; ALT_INIT; mRNA.
DR   CCDS; CCDS34112.1; -. [Q7Z392-1]
DR   CCDS; CCDS47166.1; -. [Q7Z392-3]
DR   RefSeq; NP_068761.4; NM_021942.5. [Q7Z392-1]
DR   RefSeq; NP_951008.1; NM_199053.3. [Q7Z392-3]
DR   RefSeq; XP_024309947.1; XM_024454179.2. [Q7Z392-1]
DR   RefSeq; XP_024309948.1; XM_024454180.2. [Q7Z392-1]
DR   RefSeq; XP_054206676.1; XM_054350701.1. [Q7Z392-1]
DR   RefSeq; XP_054206677.1; XM_054350702.1. [Q7Z392-1]
DR   AlphaFoldDB; Q7Z392; -.
DR   SMR; Q7Z392; -.
DR   BioGRID; 121957; 100.
DR   ComplexPortal; CPX-4750; TRAPP III complex, TRAPPC2 variant.
DR   ComplexPortal; CPX-6903; TRAPP III complex, TRAPPC2B variant.
DR   CORUM; Q7Z392; -.
DR   DIP; DIP-48282N; -.
DR   FunCoup; Q7Z392; 3497.
DR   IntAct; Q7Z392; 39.
DR   STRING; 9606.ENSP00000335371; -.
DR   iPTMnet; Q7Z392; -.
DR   PhosphoSitePlus; Q7Z392; -.
DR   BioMuta; TRAPPC11; -.
DR   DMDM; 205696378; -.
DR   jPOST; Q7Z392; -.
DR   MassIVE; Q7Z392; -.
DR   PaxDb; 9606-ENSP00000335371; -.
DR   PeptideAtlas; Q7Z392; -.
DR   ProteomicsDB; 69012; -. [Q7Z392-1]
DR   ProteomicsDB; 69013; -. [Q7Z392-2]
DR   ProteomicsDB; 69014; -. [Q7Z392-3]
DR   ProteomicsDB; 69015; -. [Q7Z392-4]
DR   Pumba; Q7Z392; -.
DR   Antibodypedia; 55746; 31 antibodies from 8 providers.
DR   DNASU; 60684; -.
DR   Ensembl; ENST00000334690.11; ENSP00000335371.6; ENSG00000168538.17. [Q7Z392-1]
DR   Ensembl; ENST00000357207.8; ENSP00000349738.4; ENSG00000168538.17. [Q7Z392-3]
DR   GeneID; 60684; -.
DR   KEGG; hsa:60684; -.
DR   MANE-Select; ENST00000334690.11; ENSP00000335371.6; NM_021942.6; NP_068761.4.
DR   UCSC; uc003ivw.3; human. [Q7Z392-1]
DR   AGR; HGNC:25751; -.
DR   ClinPGx; PA162379849; -.
DR   CTD; 60684; -.
DR   DisGeNET; 60684; -.
DR   GeneCards; TRAPPC11; -.
DR   HGNC; HGNC:25751; TRAPPC11.
DR   HPA; ENSG00000168538; Low tissue specificity.
DR   MalaCards; TRAPPC11; -.
DR   MIM; 614138; gene.
DR   MIM; 615356; phenotype.
DR   OpenTargets; ENSG00000168538; -.
DR   Orphanet; 369847; Intellectual disability-hyperkinetic movement-truncal ataxia syndrome.
DR   Orphanet; 369840; TRAPPC11-related limb-girdle muscular dystrophy R18.
DR   Orphanet; 869; Triple A syndrome.
DR   VEuPathDB; HostDB:ENSG00000168538; -.
DR   eggNOG; KOG4386; Eukaryota.
DR   GeneTree; ENSGT00390000006550; -.
DR   HOGENOM; CLU_003649_0_0_1; -.
DR   InParanoid; Q7Z392; -.
DR   OMA; CVEYYRD; -.
DR   OrthoDB; 6278596at2759; -.
DR   PAN-GO; Q7Z392; 0 GO annotations based on evolutionary models.
DR   PhylomeDB; Q7Z392; -.
DR   PathwayCommons; Q7Z392; -.
DR   Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   SignaLink; Q7Z392; -.
DR   Agora; ENSG00000168538; -.
DR   BioGRID-ORCS; 60684; 775 hits in 1165 CRISPR screens.
DR   ChiTaRS; TRAPPC11; human.
DR   GenomeRNAi; 60684; -.
DR   Pharos; Q7Z392; Tbio.
DR   PRO; PR:Q7Z392; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q7Z392; protein.
DR   Bgee; ENSG00000168538; Expressed in calcaneal tendon and 188 other cell types or tissues.
DR   ExpressionAtlas; Q7Z392; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0030008; C:TRAPP complex; IMP:UniProtKB.
DR   GO; GO:1990072; C:TRAPPIII protein complex; NAS:ComplexPortal.
DR   GO; GO:0045054; P:constitutive secretory pathway; IMP:UniProtKB.
DR   GO; GO:0048208; P:COPII vesicle coating; NAS:ComplexPortal.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR   GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR   GO; GO:0061635; P:regulation of protein complex stability; IMP:UniProtKB.
DR   GO; GO:0099022; P:vesicle tethering; NAS:ComplexPortal.
DR   InterPro; IPR021773; TPC11.
DR   InterPro; IPR025876; TRAPPC11_C.
DR   PANTHER; PTHR14374; FOIE GRAS; 1.
DR   PANTHER; PTHR14374:SF0; TRAFFICKING PROTEIN PARTICLE COMPLEX SUBUNIT 11; 1.
DR   Pfam; PF11817; Foie-gras_1; 1.
DR   Pfam; PF12742; Gryzun-like; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Disease variant; ER-Golgi transport;
KW   Golgi apparatus; Limb-girdle muscular dystrophy; Proteomics identification;
KW   Reference proteome; Transport.
FT   CHAIN           1..1133
FT                   /note="Trafficking protein particle complex subunit 11"
FT                   /id="PRO_0000348072"
FT   MOD_RES         245
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   VAR_SEQ         1..656
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035095"
FT   VAR_SEQ         962..1018
FT                   /note="CFCLQCPSLGNIEGGVATGHYIISWKRTSAMENIPIITTVITLPHVIVENIP
FT                   LHVNA -> LYYLLEKDLSNGEYPHHHNCHHSAARDCGEYPSPCECRSAVIWACQRVVT
FT                   CQVSPTE (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_035096"
FT   VAR_SEQ         1019..1133
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_035097"
FT   VAR_SEQ         1067..1086
FT                   /note="RILPGTEQEMLYNFYPLMAG -> PAQAFYTYQYFCQATGSTHG (in
FT                   isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035098"
FT   VAR_SEQ         1087..1133
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_035099"
FT   VARIANT         284
FT                   /note="Q -> P (in LGMDR18; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:29855340"
FT                   /id="VAR_087914"
FT   VARIANT         381
FT                   /note="P -> A (found in a patient with congenital disorder
FT                   of glycosylation; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:27862579"
FT                   /id="VAR_078126"
FT   VARIANT         980
FT                   /note="G -> R (in LGMDR18; dbSNP:rs397509417)"
FT                   /evidence="ECO:0000269|PubMed:23830518"
FT                   /id="VAR_070158"
FT   VARIANT         1104
FT                   /note="T -> A (found in a patient with congenital disorder
FT                   of glycosylation; uncertain significance;
FT                   dbSNP:rs78663235)"
FT                   /evidence="ECO:0000269|PubMed:27862579"
FT                   /id="VAR_078127"
FT   CONFLICT        70
FT                   /note="T -> A (in Ref. 2; AAH51724)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        197
FT                   /note="Q -> L (in Ref. 2; AAH51724)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        312
FT                   /note="S -> F (in Ref. 2; AAH51724)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        397
FT                   /note="W -> R (in Ref. 3; BAG37533)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        467
FT                   /note="K -> E (in Ref. 2; AAH51724)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        544
FT                   /note="N -> K (in Ref. 3; BAB15617)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        660
FT                   /note="V -> L (in Ref. 2; AAH51724)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        661
FT                   /note="P -> L (in Ref. 3; BAB15617)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        697
FT                   /note="R -> K (in Ref. 4; CAG38584)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        723..744
FT                   /note="Missing (in Ref. 3; BAB14556)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        812
FT                   /note="T -> P (in Ref. 1; CAD91169, 4; CAG38584 and 5;
FT                   CAB66686)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        842
FT                   /note="Y -> C (in Ref. 3; BAB15617)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        865
FT                   /note="V -> I (in Ref. 3; BAB14240)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        869
FT                   /note="E -> G (in Ref. 3; BAB14556)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1011
FT                   /note="N -> S (in Ref. 3; BAB14240)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1030
FT                   /note="L -> S (in Ref. 3; BAB14556)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1112
FT                   /note="I -> L (in Ref. 1; CAD97983)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1133 AA;  128881 MW;  6048FB396E946D4A CRC64;
     MSPTQWDFPV ELCCRPMAFV TLTGLDVVYN AVHRAVWDAF CANRRADRVP ISFKVLPGDH
     EYPKCRPKRT SYEWYIPKGI LKTGWMNKHL NLVPALVVVF YELDWDEPQW KEKQSECATR
     VEIVRQSLQG RNTKVAVVLI QKKTPLPPGE DVIASERAAA LCNACELSGK SLFVLPHTDH
     LVGYIIRLEN AFYEHAQTYY YTEIRRVKSH KEFLNKTTHQ LLFVRHQFKI AFFSELKQDT
     QNALKNYRTA YNLVHELRAH ETNILEIKTM AGFINYKICR LCFQHNTPLD AIAQFRKHID
     LCKKKIGSAE LSFEHDAWMS KQFQAFGDLF DEAIKLGLTA IQTQNPGFYY QQAAYYAQER
     KQLAKTLCNH EASVMYPNPD PLETQTGVLD FYGQRSWRQG ILSFDLSDPE KEKVGILAIQ
     LKERNVVHSE IIITLLSNAV AQFKKYKCPR MKSHLMVQMG EEYYYAKDYT KALKLLDYVM
     CDYRSEGWWT LLTSVLTTAL KCSYLMAQLK DYITYSLELL GRASTLKDDQ KSRIEKNLIN
     VLMNESPDPE PDCDILAVKT AQKLWADRIS LAGSNIFTIG VQDFVPFVQC KAKFHAPSFH
     VDVPVQFDIY LKADCPHPIR FSKLCVSFNN QEYNQFCVIE EASKANEVLE NLTQGKMCLV
     PGKTRKLLFK FVAKTEDVGK KIEITSVDLA LGNETGRCVV LNWQGGGGDA ASSQEALQAA
     RSFKRRPKLP DNEVHWDSII IQASTMIISR VPNISVHLLH EPPALTNEMY CLVVTVQSHE
     KTQIRDVKLT AGLKPGQDAN LTQKTHVTLH GTELCDESYP ALLTDIPVGD LHPGEQLEKM
     LYVRCGTVGS RMFLVYVSYL INTTVEEKEI VCKCHKDETV TIETVFPFDV AVKFVSTKFE
     HLERVYADIP FLLMTDLLSA SPWALTIVSS ELQLAPSMTT VDQLESQVDN VILQTGESAS
     ECFCLQCPSL GNIEGGVATG HYIISWKRTS AMENIPIITT VITLPHVIVE NIPLHVNADL
     PSFGRVRESL PVKYHLQNKT DLVQDVEISV EPSDAFMFSG LKQIRLRILP GTEQEMLYNF
     YPLMAGYQQL PSLNINLLRF PNFTNQLLRR FIPTSIFVKP QGRLMDDTSI AAA
//