Full text data of SCFD1
SCFD1
(C14orf163, KIAA0917, STXBP1L2)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Sec1 family domain-containing protein 1 (SLY1 homolog; Sly1p; Syntaxin-binding protein 1-like 2)
Sec1 family domain-containing protein 1 (SLY1 homolog; Sly1p; Syntaxin-binding protein 1-like 2)
hRBCD
IPI00165261
IPI00165261 Sec1 family domain containing protein 1 Involved in vesicular transport between the endoplasmic reticulum and the Golgi soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a golgi and ER n/a expected molecular weight found in band found in band around 188 kDa
IPI00165261 Sec1 family domain containing protein 1 Involved in vesicular transport between the endoplasmic reticulum and the Golgi soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a golgi and ER n/a expected molecular weight found in band found in band around 188 kDa
UniProt
Q8WVM8
ID SCFD1_HUMAN Reviewed; 642 AA.
AC Q8WVM8; A8K2Z5; B7Z4U7; B7Z594; O60754; O94990; Q7Z529; Q9BZI3;
read moreAC Q9UNL3; Q9Y6A8;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Sec1 family domain-containing protein 1;
DE AltName: Full=SLY1 homolog;
DE Short=Sly1p;
DE AltName: Full=Syntaxin-binding protein 1-like 2;
GN Name=SCFD1; Synonyms=C14orf163, KIAA0917, STXBP1L2; ORFNames=FKSG23;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Pituitary;
RA Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G.,
RA Luo M., Chen J., Hu R.;
RT "Human vesicle transport-related protein gene.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Wang Y.-G., Gong L.;
RT "Identification of FKSG23, a vesicle transport-related protein.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Dai F.Y., Yu L., Ding J.B., Lin W., Yang Y.M., Zhao S.Y.;
RT "Cloning of a novel human cDNA homology to R.norvegicus rsly1p mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
RP VARIANT ARG-63.
RC TISSUE=Heart, and Umbilical cord blood;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ARG-63.
RC TISSUE=Lymph;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-16.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [10]
RP PROTEIN SEQUENCE OF 2-16; 125-145; 382-395 AND 502-536, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Foreskin fibroblast, and Prostatic carcinoma;
RA Bienvenut W.V., Gao M., Leug H., Campbell A., Ozanne B.W.;
RL Submitted (JUL-2009) to UniProtKB.
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 572-642.
RC TISSUE=Placenta;
RA Page N.M., Butlin D.J., Manyonda I., Bicknell A.B., Lowry P.J.;
RT "Differential display of placental genes.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND MASS
RP SPECTROMETRY.
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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
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.,
RA Buerckstuemmer T., 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Plays a role in SNARE-pin assembly and Golgi-to-ER
CC retrograde transport via its interaction with COG4. Involved in
CC vesicular transport between the endoplasmic reticulum and the
CC Golgi (By similarity).
CC -!- SUBUNIT: Interacts with STX17. Interacts with STX5A. Interacts
CC with the COG complex via COG4 (By similarity).
CC -!- INTERACTION:
CC Q9H9E3:COG4; NbExp=10; IntAct=EBI-722569, EBI-368382;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Endoplasmic
CC reticulum membrane; Peripheral membrane protein (By similarity).
CC Golgi apparatus, Golgi stack membrane; Peripheral membrane protein
CC (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WVM8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WVM8-2; Sequence=VSP_047070;
CC Name=3;
CC IsoId=Q8WVM8-3; Sequence=VSP_047071;
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD40381.1; Type=Frameshift; Positions=Several;
CC Sequence=AAD48586.1; Type=Frameshift; Positions=Several;
CC Sequence=AAP97146.1; Type=Frameshift; Positions=5;
CC Sequence=BAA74940.2; Type=Erroneous initiation;
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DR EMBL; AB020724; BAA74940.2; ALT_INIT; mRNA.
DR EMBL; AF092139; AAD40381.1; ALT_FRAME; mRNA.
DR EMBL; AF110646; AAD48586.1; ALT_FRAME; mRNA.
DR EMBL; AF319958; AAG50273.1; -; mRNA.
DR EMBL; AF086916; AAP97146.1; ALT_FRAME; mRNA.
DR EMBL; AK290410; BAF83099.1; -; mRNA.
DR EMBL; AK298622; BAH12830.1; -; mRNA.
DR EMBL; AK297873; BAH12683.1; -; mRNA.
DR EMBL; AK316212; BAH14583.1; -; mRNA.
DR EMBL; AL121852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65968.1; -; Genomic_DNA.
DR EMBL; BC017734; AAH17734.1; -; mRNA.
DR EMBL; AF067205; AAC17907.1; -; mRNA.
DR RefSeq; NP_001244305.1; NM_001257376.1.
DR RefSeq; NP_001269961.1; NM_001283032.1.
DR RefSeq; NP_057190.2; NM_016106.3.
DR RefSeq; NP_878255.1; NM_182835.2.
DR UniGene; Hs.369168; -.
DR ProteinModelPortal; Q8WVM8; -.
DR SMR; Q8WVM8; 13-459.
DR IntAct; Q8WVM8; 10.
DR MINT; MINT-1394008; -.
DR STRING; 9606.ENSP00000390783; -.
DR PhosphoSite; Q8WVM8; -.
DR DMDM; 51316882; -.
DR PaxDb; Q8WVM8; -.
DR PRIDE; Q8WVM8; -.
DR Ensembl; ENST00000396629; ENSP00000379870; ENSG00000092108.
DR Ensembl; ENST00000458591; ENSP00000390783; ENSG00000092108.
DR Ensembl; ENST00000544052; ENSP00000443010; ENSG00000092108.
DR GeneID; 23256; -.
DR KEGG; hsa:23256; -.
DR UCSC; uc001wqm.2; human.
DR CTD; 23256; -.
DR GeneCards; GC14P031091; -.
DR HGNC; HGNC:20726; SCFD1.
DR HPA; HPA003579; -.
DR neXtProt; NX_Q8WVM8; -.
DR PharmGKB; PA134946073; -.
DR eggNOG; COG5158; -.
DR HOVERGEN; HBG061536; -.
DR OMA; KGKQGKH; -.
DR PhylomeDB; Q8WVM8; -.
DR ChiTaRS; SCFD1; human.
DR GeneWiki; SCFD1; -.
DR GenomeRNAi; 23256; -.
DR NextBio; 44982; -.
DR PRO; PR:Q8WVM8; -.
DR ArrayExpress; Q8WVM8; -.
DR Bgee; Q8WVM8; -.
DR CleanEx; HS_SCFD1; -.
DR Genevestigator; Q8WVM8; -.
DR GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017119; C:Golgi transport complex; IEA:Ensembl.
DR GO; GO:0005798; C:Golgi-associated vesicle; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; ISS:UniProtKB.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEP:UniProtKB.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; ISS:UniProtKB.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:InterPro.
DR Gene3D; 3.40.50.1910; -; 2.
DR InterPro; IPR027482; Sec-1-like_dom2.
DR InterPro; IPR001619; Sec1-like.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR Pfam; PF00995; Sec1; 1.
DR PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Membrane; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 642 Sec1 family domain-containing protein 1.
FT /FTId=PRO_0000206287.
FT COMPBIAS 2 13 Poly-Ala.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 303 303 Phosphoserine.
FT VAR_SEQ 1 92 Missing (in isoform 2).
FT /FTId=VSP_047070.
FT VAR_SEQ 1 67 Missing (in isoform 3).
FT /FTId=VSP_047071.
FT VARIANT 63 63 K -> R (in dbSNP:rs229150).
FT /FTId=VAR_019616.
FT CONFLICT 42 42 V -> I (in Ref. 3; AAG50273).
FT CONFLICT 136 137 AA -> EL (in Ref. 2; AAD40381).
FT CONFLICT 201 206 FVTLGA -> YGTRGD (in Ref. 2; AAD48586).
FT CONFLICT 201 202 FV -> YG (in Ref. 2; AAD40381 and 4;
FT AAP97146).
FT CONFLICT 206 206 A -> D (in Ref. 4; AAP97146).
FT CONFLICT 453 453 K -> N (in Ref. 2; AAD48586).
FT CONFLICT 484 485 GC -> EM (in Ref. 2; AAD40381).
FT CONFLICT 485 485 Missing (in Ref. 2; AAD48586).
FT CONFLICT 562 563 ET -> KL (in Ref. 2; AAD40381).
SQ SEQUENCE 642 AA; 72380 MW; 0340FB9F05CD24CE CRC64;
MAAAAAATAA AAASIRERQT VALKRMLNFN VPHIKNSTGE PVWKVLIYDR FGQDIISPLL
SVKELRDMGI TLHLLLHSDR DPIPDVPAVY FVMPTEENID RMCQDLRNQL YESYYLNFIS
AISRSKLEDI ANAALAASAV TQVAKVFDQY LNFITLEDDM FVLCNQNKEL VSYRAINRPD
ITDTEMETVM DTIVDSLFCF FVTLGAVPII RCSRGTAAEM VAVKLDKKLR ENLRDARNSL
FTGDTLGAGQ FSFQRPLLVL VDRNIDLATP LHHTWTYQAL VHDVLDFHLN RVNLEESSGV
ENSPAGARPK RKNKKSYDLT PVDKFWQKHK GSPFPEVAES VQQELESYRA QEDEVKRLKS
IMGLEGEDEG AISMLSDNTA KLTSAVSSLP ELLEKKRLID LHTNVATAVL EHIKARKLDV
YFEYEEKIMS KTTLDKSLLD IISDPDAGTP EDKMRLFLIY YISTQQAPSE ADLEQYKKAL
TDAGCNLNPL QYIKQWKAFT KMASAPASYG STTTKPMGLL SRVMNTGSQF VMEGVKNLVL
KQQNLPVTRI LDNLMEMKSN PETDDYRYFD PKMLRGNDSS VPRNKNPFQE AIVFVVGGGN
YIEYQNLVDY IKGKQGKHIL YGCSELFNAT QFIKQLSQLG QK
//
ID SCFD1_HUMAN Reviewed; 642 AA.
AC Q8WVM8; A8K2Z5; B7Z4U7; B7Z594; O60754; O94990; Q7Z529; Q9BZI3;
read moreAC Q9UNL3; Q9Y6A8;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 113.
DE RecName: Full=Sec1 family domain-containing protein 1;
DE AltName: Full=SLY1 homolog;
DE Short=Sly1p;
DE AltName: Full=Syntaxin-binding protein 1-like 2;
GN Name=SCFD1; Synonyms=C14orf163, KIAA0917, STXBP1L2; ORFNames=FKSG23;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M.,
RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Pituitary;
RA Song H., Peng Y., Dai M., Huang Q., Mao Y., Zhang Q., Mao M., Fu G.,
RA Luo M., Chen J., Hu R.;
RT "Human vesicle transport-related protein gene.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Wang Y.-G., Gong L.;
RT "Identification of FKSG23, a vesicle transport-related protein.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Dai F.Y., Yu L., Ding J.B., Lin W., Yang Y.M., Zhao S.Y.;
RT "Cloning of a novel human cDNA homology to R.norvegicus rsly1p mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND
RP VARIANT ARG-63.
RC TISSUE=Heart, and Umbilical cord blood;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP ARG-63.
RC TISSUE=Lymph;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP PROTEIN SEQUENCE OF 2-16.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [10]
RP PROTEIN SEQUENCE OF 2-16; 125-145; 382-395 AND 502-536, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Foreskin fibroblast, and Prostatic carcinoma;
RA Bienvenut W.V., Gao M., Leug H., Campbell A., Ozanne B.W.;
RL Submitted (JUL-2009) to UniProtKB.
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 572-642.
RC TISSUE=Placenta;
RA Page N.M., Butlin D.J., Manyonda I., Bicknell A.B., Lowry P.J.;
RT "Differential display of placental genes.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND MASS
RP SPECTROMETRY.
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 [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
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.,
RA Buerckstuemmer T., 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Plays a role in SNARE-pin assembly and Golgi-to-ER
CC retrograde transport via its interaction with COG4. Involved in
CC vesicular transport between the endoplasmic reticulum and the
CC Golgi (By similarity).
CC -!- SUBUNIT: Interacts with STX17. Interacts with STX5A. Interacts
CC with the COG complex via COG4 (By similarity).
CC -!- INTERACTION:
CC Q9H9E3:COG4; NbExp=10; IntAct=EBI-722569, EBI-368382;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Endoplasmic
CC reticulum membrane; Peripheral membrane protein (By similarity).
CC Golgi apparatus, Golgi stack membrane; Peripheral membrane protein
CC (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8WVM8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WVM8-2; Sequence=VSP_047070;
CC Name=3;
CC IsoId=Q8WVM8-3; Sequence=VSP_047071;
CC -!- SIMILARITY: Belongs to the STXBP/unc-18/SEC1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD40381.1; Type=Frameshift; Positions=Several;
CC Sequence=AAD48586.1; Type=Frameshift; Positions=Several;
CC Sequence=AAP97146.1; Type=Frameshift; Positions=5;
CC Sequence=BAA74940.2; Type=Erroneous initiation;
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DR EMBL; AB020724; BAA74940.2; ALT_INIT; mRNA.
DR EMBL; AF092139; AAD40381.1; ALT_FRAME; mRNA.
DR EMBL; AF110646; AAD48586.1; ALT_FRAME; mRNA.
DR EMBL; AF319958; AAG50273.1; -; mRNA.
DR EMBL; AF086916; AAP97146.1; ALT_FRAME; mRNA.
DR EMBL; AK290410; BAF83099.1; -; mRNA.
DR EMBL; AK298622; BAH12830.1; -; mRNA.
DR EMBL; AK297873; BAH12683.1; -; mRNA.
DR EMBL; AK316212; BAH14583.1; -; mRNA.
DR EMBL; AL121852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65968.1; -; Genomic_DNA.
DR EMBL; BC017734; AAH17734.1; -; mRNA.
DR EMBL; AF067205; AAC17907.1; -; mRNA.
DR RefSeq; NP_001244305.1; NM_001257376.1.
DR RefSeq; NP_001269961.1; NM_001283032.1.
DR RefSeq; NP_057190.2; NM_016106.3.
DR RefSeq; NP_878255.1; NM_182835.2.
DR UniGene; Hs.369168; -.
DR ProteinModelPortal; Q8WVM8; -.
DR SMR; Q8WVM8; 13-459.
DR IntAct; Q8WVM8; 10.
DR MINT; MINT-1394008; -.
DR STRING; 9606.ENSP00000390783; -.
DR PhosphoSite; Q8WVM8; -.
DR DMDM; 51316882; -.
DR PaxDb; Q8WVM8; -.
DR PRIDE; Q8WVM8; -.
DR Ensembl; ENST00000396629; ENSP00000379870; ENSG00000092108.
DR Ensembl; ENST00000458591; ENSP00000390783; ENSG00000092108.
DR Ensembl; ENST00000544052; ENSP00000443010; ENSG00000092108.
DR GeneID; 23256; -.
DR KEGG; hsa:23256; -.
DR UCSC; uc001wqm.2; human.
DR CTD; 23256; -.
DR GeneCards; GC14P031091; -.
DR HGNC; HGNC:20726; SCFD1.
DR HPA; HPA003579; -.
DR neXtProt; NX_Q8WVM8; -.
DR PharmGKB; PA134946073; -.
DR eggNOG; COG5158; -.
DR HOVERGEN; HBG061536; -.
DR OMA; KGKQGKH; -.
DR PhylomeDB; Q8WVM8; -.
DR ChiTaRS; SCFD1; human.
DR GeneWiki; SCFD1; -.
DR GenomeRNAi; 23256; -.
DR NextBio; 44982; -.
DR PRO; PR:Q8WVM8; -.
DR ArrayExpress; Q8WVM8; -.
DR Bgee; Q8WVM8; -.
DR CleanEx; HS_SCFD1; -.
DR Genevestigator; Q8WVM8; -.
DR GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017119; C:Golgi transport complex; IEA:Ensembl.
DR GO; GO:0005798; C:Golgi-associated vesicle; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0019905; F:syntaxin binding; ISS:UniProtKB.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEP:UniProtKB.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to ER; ISS:UniProtKB.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IEA:InterPro.
DR Gene3D; 3.40.50.1910; -; 2.
DR InterPro; IPR027482; Sec-1-like_dom2.
DR InterPro; IPR001619; Sec1-like.
DR PANTHER; PTHR11679; PTHR11679; 1.
DR Pfam; PF00995; Sec1; 1.
DR PIRSF; PIRSF005715; VPS45_Sec1; 1.
DR SUPFAM; SSF56815; SSF56815; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Membrane; Phosphoprotein; Polymorphism;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 642 Sec1 family domain-containing protein 1.
FT /FTId=PRO_0000206287.
FT COMPBIAS 2 13 Poly-Ala.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 303 303 Phosphoserine.
FT VAR_SEQ 1 92 Missing (in isoform 2).
FT /FTId=VSP_047070.
FT VAR_SEQ 1 67 Missing (in isoform 3).
FT /FTId=VSP_047071.
FT VARIANT 63 63 K -> R (in dbSNP:rs229150).
FT /FTId=VAR_019616.
FT CONFLICT 42 42 V -> I (in Ref. 3; AAG50273).
FT CONFLICT 136 137 AA -> EL (in Ref. 2; AAD40381).
FT CONFLICT 201 206 FVTLGA -> YGTRGD (in Ref. 2; AAD48586).
FT CONFLICT 201 202 FV -> YG (in Ref. 2; AAD40381 and 4;
FT AAP97146).
FT CONFLICT 206 206 A -> D (in Ref. 4; AAP97146).
FT CONFLICT 453 453 K -> N (in Ref. 2; AAD48586).
FT CONFLICT 484 485 GC -> EM (in Ref. 2; AAD40381).
FT CONFLICT 485 485 Missing (in Ref. 2; AAD48586).
FT CONFLICT 562 563 ET -> KL (in Ref. 2; AAD40381).
SQ SEQUENCE 642 AA; 72380 MW; 0340FB9F05CD24CE CRC64;
MAAAAAATAA AAASIRERQT VALKRMLNFN VPHIKNSTGE PVWKVLIYDR FGQDIISPLL
SVKELRDMGI TLHLLLHSDR DPIPDVPAVY FVMPTEENID RMCQDLRNQL YESYYLNFIS
AISRSKLEDI ANAALAASAV TQVAKVFDQY LNFITLEDDM FVLCNQNKEL VSYRAINRPD
ITDTEMETVM DTIVDSLFCF FVTLGAVPII RCSRGTAAEM VAVKLDKKLR ENLRDARNSL
FTGDTLGAGQ FSFQRPLLVL VDRNIDLATP LHHTWTYQAL VHDVLDFHLN RVNLEESSGV
ENSPAGARPK RKNKKSYDLT PVDKFWQKHK GSPFPEVAES VQQELESYRA QEDEVKRLKS
IMGLEGEDEG AISMLSDNTA KLTSAVSSLP ELLEKKRLID LHTNVATAVL EHIKARKLDV
YFEYEEKIMS KTTLDKSLLD IISDPDAGTP EDKMRLFLIY YISTQQAPSE ADLEQYKKAL
TDAGCNLNPL QYIKQWKAFT KMASAPASYG STTTKPMGLL SRVMNTGSQF VMEGVKNLVL
KQQNLPVTRI LDNLMEMKSN PETDDYRYFD PKMLRGNDSS VPRNKNPFQE AIVFVVGGGN
YIEYQNLVDY IKGKQGKHIL YGCSELFNAT QFIKQLSQLG QK
//