GORS1_HUMAN
ID GORS1_HUMAN Reviewed; 440 AA.
AC Q9BQQ3; B3KWC8; Q3SYG7; Q8N272; Q96H42;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Golgi reassembly-stacking protein 1;
DE AltName: Full=Golgi peripheral membrane protein p65;
DE AltName: Full=Golgi phosphoprotein 5;
DE Short=GOLPH5;
DE AltName: Full=Golgi reassembly-stacking protein of 65 kDa;
DE Short=GRASP65 {ECO:0000303|PubMed:11781572, ECO:0000303|PubMed:26363069};
GN Name=GORASP1; Synonyms=GOLPH5, GRASP65;
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 [MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RA Protopopov A., Kashuba V., Kvasha S., Klein G., Zabarovsky E.;
RT "Refined physical mapping and genomic structure of a 4-Mb region (AP-20) on
RT human chromosome 3p22-p21.33 implicated in lung and kidney
RT cancerogenesis.";
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Tongue;
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 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, 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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11781572; DOI=10.1038/ncb1201-1101;
RA Marra P., Maffucci T., Daniele T., Tullio G.D., Ikehara Y., Chan E.K.,
RA Luini A., Beznoussenko G., Mironov A., De Matteis M.A.;
RT "The GM130 and GRASP65 Golgi proteins cycle through and define a subdomain
RT of the intermediate compartment.";
RL Nat. Cell Biol. 3:1101-1113(2001).
RN [6]
RP FUNCTION, AND INTERACTION WITH GOLGA2.
RX PubMed=16489344; DOI=10.1038/ncb1366;
RA Puthenveedu M.A., Bachert C., Puri S., Lanni F., Linstedt A.D.;
RT "GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-
RT enzyme distribution.";
RL Nat. Cell Biol. 8:238-248(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-216, 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 [10]
RP FUNCTION.
RX PubMed=21884936; DOI=10.1016/j.cell.2011.07.021;
RA Gee H.Y., Noh S.H., Tang B.L., Kim K.H., Lee M.G.;
RT "Rescue of DeltaF508-CFTR trafficking via a GRASP-dependent unconventional
RT secretion pathway.";
RL Cell 146:746-760(2011).
RN [11]
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 [12] {ECO:0007744|PDB:4REY}
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) OF 2-210 IN COMPLEX WITH GOLGA2,
RP FUNCTION, AND SUBUNIT.
RX PubMed=26363069; DOI=10.1074/jbc.m115.657940;
RA Hu F., Shi X., Li B., Huang X., Morelli X., Shi N.;
RT "Structural basis for the interaction between the Golgi reassembly-stacking
RT protein GRASP65 and the Golgi matrix protein GM130.";
RL J. Biol. Chem. 290:26373-26382(2015).
CC -!- FUNCTION: Plays an important role in assembly and membrane stacking of
CC the Golgi cisternae, and in the reassembly of Golgi stacks after
CC breakdown during mitosis (PubMed:26363069). Key structural protein
CC required for the maintenance of the Golgi apparatus integrity: its
CC caspase-mediated cleavage is required for fragmentation of the Golgi
CC during apoptosis (By similarity). Also mediates, via its interaction
CC with GOLGA2/GM130, the docking of transport vesicles with the Golgi
CC membranes (PubMed:16489344). Mediates ER stress-induced unconventional
CC (ER/Golgi-independent) trafficking of core-glycosylated CFTR to cell
CC membrane (PubMed:21884936). {ECO:0000250|UniProtKB:O35254,
CC ECO:0000269|PubMed:16489344, ECO:0000269|PubMed:21884936,
CC ECO:0000269|PubMed:26363069}.
CC -!- SUBUNIT: Homodimer. Forms higher-order oligomers under interphase but
CC not mitotic conditions. Dimers of the protein on one membrane might be
CC able to interact with dimers on another and so stack cisternae
CC (PubMed:26363069). Interacts with the C-terminus of GOLGA2/GM130 under
CC both mitotic and non-mitotic conditions (PubMed:16489344,
CC PubMed:26363069). The interaction is critical for the correct targeting
CC of both proteins to the cis-Golgi. Interacts with TMED2 and TMED3 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:O35254,
CC ECO:0000269|PubMed:16489344, ECO:0000269|PubMed:26363069}.
CC -!- INTERACTION:
CC Q9BQQ3; O00116: AGPS; NbExp=7; IntAct=EBI-2561458, EBI-2838732;
CC Q9BQQ3; Q17RB8: LONRF1; NbExp=6; IntAct=EBI-2561458, EBI-2341787;
CC Q9BQQ3; P07196: NEFL; NbExp=3; IntAct=EBI-2561458, EBI-475646;
CC Q9BQQ3; Q12765: SCRN1; NbExp=3; IntAct=EBI-2561458, EBI-2690712;
CC Q9BQQ3; Q12765-2: SCRN1; NbExp=3; IntAct=EBI-2561458, EBI-12027936;
CC Q9BQQ3; Q9BUZ4: TRAF4; NbExp=3; IntAct=EBI-2561458, EBI-3650647;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, cis-Golgi network membrane
CC {ECO:0000269|PubMed:11781572}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Endoplasmic reticulum-
CC Golgi intermediate compartment membrane {ECO:0000269|PubMed:11781572}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BQQ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQQ3-2; Sequence=VSP_011307;
CC Name=3;
CC IsoId=Q9BQQ3-3; Sequence=VSP_011306, VSP_011308, VSP_011309;
CC -!- PTM: Phosphorylated by CDC2/B1 and PLK kinases during mitosis.
CC Phosphorylation cycle correlates with the cisternal stacking cycle.
CC Phosphorylation of the homodimer prevents the association of dimers
CC into higher-order oligomers, leading to cisternal unstacking.
CC {ECO:0000250|UniProtKB:O35254}.
CC -!- PTM: Target for caspase-3 cleavage during apoptosis. The cleavage
CC contributes to Golgi fragmentation and occurs very early in the
CC execution phase of apoptosis. {ECO:0000250|UniProtKB:O35254}.
CC -!- PTM: Myristoylated. {ECO:0000250|UniProtKB:O35254}.
CC -!- SIMILARITY: Belongs to the GORASP family. {ECO:0000305}.
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DR EMBL; AJ409349; CAC35160.1; -; mRNA.
DR EMBL; AK091168; BAC03598.1; -; mRNA.
DR EMBL; AK124755; BAG54090.1; -; mRNA.
DR EMBL; CH471055; EAW64554.1; -; Genomic_DNA.
DR EMBL; BC008928; AAH08928.1; -; mRNA.
DR EMBL; BC075854; AAH75854.1; -; mRNA.
DR EMBL; BC103826; AAI03827.1; -; mRNA.
DR EMBL; BC103827; AAI03828.1; -; mRNA.
DR CCDS; CCDS2681.1; -. [Q9BQQ3-1]
DR RefSeq; NP_001265718.1; NM_001278789.1.
DR RefSeq; NP_001265719.1; NM_001278790.1.
DR RefSeq; NP_114105.1; NM_031899.3. [Q9BQQ3-1]
DR PDB; 4REY; X-ray; 1.96 A; A=2-210.
DR PDB; 6G8T; X-ray; 2.67 A; A=1-118.
DR PDB; 6G8W; X-ray; 2.12 A; A/B=108-204.
DR PDBsum; 4REY; -.
DR PDBsum; 6G8T; -.
DR PDBsum; 6G8W; -.
DR AlphaFoldDB; Q9BQQ3; -.
DR SMR; Q9BQQ3; -.
DR BioGRID; 122232; 112.
DR ComplexPortal; CPX-874; GRASP65-GM130 Golgi stacking complex.
DR CORUM; Q9BQQ3; -.
DR IntAct; Q9BQQ3; 52.
DR MINT; Q9BQQ3; -.
DR STRING; 9606.ENSP00000313869; -.
DR iPTMnet; Q9BQQ3; -.
DR PhosphoSitePlus; Q9BQQ3; -.
DR BioMuta; GORASP1; -.
DR DMDM; 51316077; -.
DR EPD; Q9BQQ3; -.
DR jPOST; Q9BQQ3; -.
DR MassIVE; Q9BQQ3; -.
DR MaxQB; Q9BQQ3; -.
DR PaxDb; Q9BQQ3; -.
DR PeptideAtlas; Q9BQQ3; -.
DR PRIDE; Q9BQQ3; -.
DR ProteomicsDB; 78706; -. [Q9BQQ3-1]
DR ProteomicsDB; 78707; -. [Q9BQQ3-2]
DR ProteomicsDB; 78708; -. [Q9BQQ3-3]
DR Antibodypedia; 28859; 280 antibodies from 33 providers.
DR DNASU; 64689; -.
DR Ensembl; ENST00000319283.8; ENSP00000313869.3; ENSG00000114745.14. [Q9BQQ3-1]
DR Ensembl; ENST00000431601.5; ENSP00000403552.1; ENSG00000114745.14. [Q9BQQ3-3]
DR Ensembl; ENST00000452389.6; ENSP00000403167.2; ENSG00000114745.14. [Q9BQQ3-2]
DR GeneID; 64689; -.
DR KEGG; hsa:64689; -.
DR MANE-Select; ENST00000319283.8; ENSP00000313869.3; NM_031899.4; NP_114105.1.
DR UCSC; uc003ciw.3; human. [Q9BQQ3-1]
DR CTD; 64689; -.
DR DisGeNET; 64689; -.
DR GeneCards; GORASP1; -.
DR HGNC; HGNC:16769; GORASP1.
DR HPA; ENSG00000114745; Low tissue specificity.
DR MIM; 606867; gene.
DR neXtProt; NX_Q9BQQ3; -.
DR OpenTargets; ENSG00000114745; -.
DR PharmGKB; PA28814; -.
DR VEuPathDB; HostDB:ENSG00000114745; -.
DR eggNOG; KOG3834; Eukaryota.
DR GeneTree; ENSGT00390000008686; -.
DR HOGENOM; CLU_025095_1_0_1; -.
DR InParanoid; Q9BQQ3; -.
DR OMA; RQDDYME; -.
DR OrthoDB; 1366434at2759; -.
DR PhylomeDB; Q9BQQ3; -.
DR PathwayCommons; Q9BQQ3; -.
DR Reactome; R-HSA-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR SignaLink; Q9BQQ3; -.
DR SIGNOR; Q9BQQ3; -.
DR BioGRID-ORCS; 64689; 12 hits in 1088 CRISPR screens.
DR ChiTaRS; GORASP1; human.
DR GeneWiki; GORASP1; -.
DR GenomeRNAi; 64689; -.
DR Pharos; Q9BQQ3; Tbio.
DR PRO; PR:Q9BQQ3; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9BQQ3; protein.
DR Bgee; ENSG00000114745; Expressed in right lobe of thyroid gland and 198 other tissues.
DR ExpressionAtlas; Q9BQQ3; baseline and differential.
DR Genevisible; Q9BQQ3; HS.
DR GO; GO:0005801; C:cis-Golgi network; IC:ComplexPortal.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061951; P:establishment of protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0050774; P:negative regulation of dendrite morphogenesis; IMP:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR007583; GRASP55_65.
DR InterPro; IPR024958; GRASP_PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR12893; PTHR12893; 1.
DR Pfam; PF04495; GRASP55_65; 1.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS51865; PDZ_GRASP; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Golgi apparatus; Lipoprotein; Membrane;
KW Metal-binding; Myristate; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Transport; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..440
FT /note="Golgi reassembly-stacking protein 1"
FT /id="PRO_0000087570"
FT DOMAIN 15..105
FT /note="PDZ GRASP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01212"
FT DOMAIN 111..199
FT /note="PDZ GRASP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01212"
FT REGION 15..215
FT /note="GRASP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01214"
FT REGION 190..202
FT /note="Essential for interaction with GOLGA2/GM130"
FT /evidence="ECO:0000250"
FT REGION 205..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..240
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O35254"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O35254"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O35254"
FT MOD_RES 216
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91X51"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35254"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q91X51"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250|UniProtKB:O35254"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011306"
FT VAR_SEQ 176..440
FT /note="VTVTPNAAWGGEGSLGCGIGYGYLHRIPTQPPSYHKKPPGTPPPSALPLGAP
FT PPDALPPGPTPEDSPSLETGSRQSDYMEALLQAPGSSMEDPLPGPGSPSHSAPDPDGLP
FT HFMETPLQPPPPVQRVMDPGFLDVSGISLLDNSNASVWPSLPSSTELTTTAVSTSGPED
FT ICSSSSSHERGGEATWSGSEFEVSFLDSPGAQAQADHLPQLTLPDSLTSAASPEDGLSA
FT ELLEAQAEEEPASTEGLDTGTEAEGLDSQAQISTTE -> SGMWHWLWVSTPDPNSAPQ
FT LPQEATWHPTTFCSTTWCPTT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011307"
FT VAR_SEQ 306..319
FT /note="GFLDVSGISLLDNS -> AMPVCGPACPLPQN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011308"
FT VAR_SEQ 320..440
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011309"
FT VARIANT 425
FT /note="T -> M (in dbSNP:rs1109643)"
FT /id="VAR_051016"
FT CONFLICT 271
FT /note="G -> E (in Ref. 2; BAC03598)"
FT /evidence="ECO:0000305"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:4REY"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:4REY"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:4REY"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:4REY"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:4REY"
FT HELIX 54..61
FT /evidence="ECO:0007829|PDB:4REY"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:4REY"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:4REY"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:4REY"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:4REY"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:4REY"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:4REY"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:4REY"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:4REY"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:4REY"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:4REY"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:4REY"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:4REY"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:6G8W"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:4REY"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:4REY"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:4REY"
FT STRAND 184..190
FT /evidence="ECO:0007829|PDB:4REY"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:4REY"
SQ SEQUENCE 440 AA; 46482 MW; 1187C0356E16CE00 CRC64;
MGLGVSAEQP AGGAEGFHLH GVQENSPAQQ AGLEPYFDFI ITIGHSRLNK ENDTLKALLK
ANVEKPVKLE VFNMKTMRVR EVEVVPSNMW GGQGLLGASV RFCSFRRASE QVWHVLDVEP
SSPAALAGLR PYTDYVVGSD QILQESEDFF TLIESHEGKP LKLMVYNSKS DSCREVTVTP
NAAWGGEGSL GCGIGYGYLH RIPTQPPSYH KKPPGTPPPS ALPLGAPPPD ALPPGPTPED
SPSLETGSRQ SDYMEALLQA PGSSMEDPLP GPGSPSHSAP DPDGLPHFME TPLQPPPPVQ
RVMDPGFLDV SGISLLDNSN ASVWPSLPSS TELTTTAVST SGPEDICSSS SSHERGGEAT
WSGSEFEVSF LDSPGAQAQA DHLPQLTLPD SLTSAASPED GLSAELLEAQ AEEEPASTEG
LDTGTEAEGL DSQAQISTTE
