SCAM3_HUMAN
ID SCAM3_HUMAN Reviewed; 347 AA.
AC O14828; A9Z1W6; B1AVS6; O15128; Q96FR8; Q9BPY0;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Secretory carrier-associated membrane protein 3;
DE Short=Secretory carrier membrane protein 3;
GN Name=SCAMP3; Synonyms=C1orf3, PROPIN1;
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 [GENOMIC DNA] (ISOFORM 1), AND VARIANTS ARG-38;
RP ALA-235; ASN-239 AND ASP-242.
RC TISSUE=Brain;
RX PubMed=9331372; DOI=10.1101/gr.7.10.1020;
RA Winfield S.L., Tayebi N., Martin B.M., Ginns E.I., Sidransky E.;
RT "Identification of three additional genes contiguous to the
RT glucocerebrosidase locus on chromosome 1q21: implications for Gaucher
RT disease.";
RL Genome Res. 7:1020-1026(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9378760; DOI=10.1242/jcs.110.17.2099;
RA Singleton D.R., Wu T.T., Castle J.D.;
RT "Three mammalian SCAMPs (secretory carrier membrane proteins) are highly
RT related products of distinct genes having similar subcellular
RT distributions.";
RL J. Cell Sci. 110:2099-2107(1997).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Cervix, and Placenta;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-41, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-76, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP UBIQUITINATION, INTERACTION WITH NEDD4; NEDD4L AND TSG101, AND MUTAGENESIS
RP OF PRO-67.
RX PubMed=19158374; DOI=10.1091/mbc.e08-09-0894;
RA Aoh Q.L., Castle A.M., Hubbard C.H., Katsumata O., Castle J.D.;
RT "SCAMP3 negatively regulates epidermal growth factor receptor degradation
RT and promotes receptor recycling.";
RL Mol. Biol. Cell 20:1816-1832(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP INTERACTION WITH RNF126.
RX PubMed=23418353; DOI=10.1242/jcs.116129;
RA Smith C.J., Berry D.M., McGlade C.J.;
RT "The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of
RT the epidermal growth factor receptor.";
RL J. Cell Sci. 126:1366-1380(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; THR-37; SER-72 AND
RP SER-85, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-76, AND
RP IDENTIFICATION BY 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).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-313, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Functions in post-Golgi recycling pathways. Acts as a
CC recycling carrier to the cell surface.
CC -!- SUBUNIT: Interacts with NEDD4, NEDD4L and TSG101. Interacts with
CC RNF126. {ECO:0000269|PubMed:19158374, ECO:0000269|PubMed:23418353}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14828-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14828-2; Sequence=VSP_004381;
CC -!- TISSUE SPECIFICITY: Widely expressed, with highest expression in heart
CC and skeletal muscle.
CC -!- PTM: Monoubiquitinated.
CC -!- SIMILARITY: Belongs to the SCAMP family. {ECO:0000305}.
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DR EMBL; AF023268; AAC51821.1; -; Genomic_DNA.
DR EMBL; AF005039; AAB62724.1; -; mRNA.
DR EMBL; AL713999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53090.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53092.1; -; Genomic_DNA.
DR EMBL; BC000161; AAH00161.1; -; mRNA.
DR EMBL; BC005135; AAH05135.1; -; mRNA.
DR EMBL; BC010505; AAH10505.1; -; mRNA.
DR CCDS; CCDS1105.1; -. [O14828-1]
DR CCDS; CCDS1106.1; -. [O14828-2]
DR PIR; T08826; T08826.
DR RefSeq; NP_005689.2; NM_005698.3. [O14828-1]
DR RefSeq; NP_443069.1; NM_052837.2. [O14828-2]
DR AlphaFoldDB; O14828; -.
DR BioGRID; 115378; 217.
DR CORUM; O14828; -.
DR ELM; O14828; -.
DR IntAct; O14828; 68.
DR MINT; O14828; -.
DR STRING; 9606.ENSP00000307275; -.
DR TCDB; 8.A.103.1.3; the secretory carrier-associated membrane protein (scamp) family.
DR GlyGen; O14828; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14828; -.
DR PhosphoSitePlus; O14828; -.
DR SwissPalm; O14828; -.
DR BioMuta; SCAMP3; -.
DR EPD; O14828; -.
DR jPOST; O14828; -.
DR MassIVE; O14828; -.
DR MaxQB; O14828; -.
DR PaxDb; O14828; -.
DR PeptideAtlas; O14828; -.
DR PRIDE; O14828; -.
DR ProteomicsDB; 48259; -. [O14828-1]
DR ProteomicsDB; 48260; -. [O14828-2]
DR Antibodypedia; 20415; 145 antibodies from 25 providers.
DR CPTC; O14828; 1 antibody.
DR DNASU; 10067; -.
DR Ensembl; ENST00000302631.8; ENSP00000307275.3; ENSG00000116521.11. [O14828-1]
DR Ensembl; ENST00000355379.3; ENSP00000347540.3; ENSG00000116521.11. [O14828-2]
DR Ensembl; ENST00000570831.5; ENSP00000461521.1; ENSG00000263290.5. [O14828-1]
DR Ensembl; ENST00000573013.1; ENSP00000458542.1; ENSG00000263290.5. [O14828-2]
DR GeneID; 10067; -.
DR KEGG; hsa:10067; -.
DR MANE-Select; ENST00000302631.8; ENSP00000307275.3; NM_005698.4; NP_005689.2.
DR UCSC; uc001fjs.4; human. [O14828-1]
DR CTD; 10067; -.
DR DisGeNET; 10067; -.
DR GeneCards; SCAMP3; -.
DR HGNC; HGNC:10565; SCAMP3.
DR HPA; ENSG00000116521; Low tissue specificity.
DR MIM; 606913; gene.
DR neXtProt; NX_O14828; -.
DR OpenTargets; ENSG00000116521; -.
DR PharmGKB; PA34978; -.
DR VEuPathDB; HostDB:ENSG00000116521; -.
DR eggNOG; KOG3088; Eukaryota.
DR GeneTree; ENSGT00940000160917; -.
DR HOGENOM; CLU_066546_0_0_1; -.
DR InParanoid; O14828; -.
DR OMA; RPSTHYA; -.
DR OrthoDB; 995882at2759; -.
DR PhylomeDB; O14828; -.
DR TreeFam; TF313797; -.
DR PathwayCommons; O14828; -.
DR SignaLink; O14828; -.
DR SIGNOR; O14828; -.
DR BioGRID-ORCS; 10067; 16 hits in 1071 CRISPR screens.
DR ChiTaRS; SCAMP3; human.
DR GeneWiki; SCAMP3; -.
DR GenomeRNAi; 10067; -.
DR Pharos; O14828; Tbio.
DR PRO; PR:O14828; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O14828; protein.
DR Bgee; ENSG00000116521; Expressed in right adrenal gland cortex and 94 other tissues.
DR Genevisible; O14828; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0055038; C:recycling endosome membrane; IBA:GO_Central.
DR GO; GO:0032588; C:trans-Golgi network membrane; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR InterPro; IPR007273; SCAMP.
DR PANTHER; PTHR10687; PTHR10687; 1.
DR Pfam; PF04144; SCAMP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Ubl conjugation.
FT CHAIN 1..347
FT /note="Secretory carrier-associated membrane protein 3"
FT /id="PRO_0000191257"
FT TOPO_DOM 1..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..70
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..88
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 37
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 41
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT MOD_RES 53
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 83
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O35609"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 313
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VAR_SEQ 23..48
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_004381"
FT VARIANT 38
FT /note="L -> R (in dbSNP:rs760073)"
FT /evidence="ECO:0000269|PubMed:9331372"
FT /id="VAR_011885"
FT VARIANT 235
FT /note="V -> A (in dbSNP:rs1318328)"
FT /evidence="ECO:0000269|PubMed:9331372"
FT /id="VAR_011886"
FT VARIANT 239
FT /note="I -> N (in dbSNP:rs909106)"
FT /evidence="ECO:0000269|PubMed:9331372"
FT /id="VAR_011887"
FT VARIANT 242
FT /note="V -> D (in dbSNP:rs909107)"
FT /evidence="ECO:0000269|PubMed:9331372"
FT /id="VAR_011888"
FT MUTAGEN 67
FT /note="P->L: Abolishes interaction with TSG101."
FT /evidence="ECO:0000269|PubMed:19158374"
FT CONFLICT 3
FT /note="Q -> R (in Ref. 2; AAB62724)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="K -> M (in Ref. 2; AAB62724)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="A -> R (in Ref. 1; AAC51821)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 38287 MW; D5B0870C66B84F9F CRC64;
MAQSRDGGNP FAEPSELDNP FQDPAVIQHR PSRQYATLDV YNPFETREPP PAYEPPAPAP
LPPPSAPSLQ PSRKLSPTEP KNYGSYSTQA SAAAATAELL KKQEELNRKA EELDRREREL
QHAALGGTAT RQNNWPPLPS FCPVQPCFFQ DISMEIPQEF QKTVSTMYYL WMCSTLALLL
NFLACLASFC VETNNGAGFG LSILWVLLFT PCSFVCWYRP MYKAFRSDSS FNFFVFFFIF
FVQDVLFVLQ AIGIPGWGFS GWISALVVPK GNTAVSVLML LVALLFTGIA VLGIVMLKRI
HSLYRRTGAS FQKAQQEFAA GVFSNPAVRT AAANAAAGAA ENAFRAP
