Q15436 (SC23A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein transport protein Sec23A

Alternative name(s):
SEC23-related protein A

Gene names

Name:

SEC23A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	765 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the COPII coat, that covers ER-derived vesicles involved in transport from the endoplasmic reticulum to the Golgi apparatus. COPII acts in the cytoplasm to promote the transport of secretory, plasma membrane, and vacuolar proteins from the endoplasmic reticulum to the Golgi complex.
Subunit structure	COPII is composed of at least five proteins: the Sec23/24 complex, the Sec13/31 complex and Sar1. Interacts with SEC23IP. Interacts with HTR4 By similarity. Interacts with SLC6A4 By similarity. Interacts with SEC16A. Ref.5
Subcellular location	Smooth endoplasmic reticulum membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein Potential. Note: In the ribosome-free transitional face of the ER and associated vesicles.
Involvement in disease	Craniolenticulosutural dysplasia (CLSD) [MIM:607812]: Autosomal recessive syndrome characterized by late-closing fontanels, sutural cataracts, facial dysmorphisms and skeletal defects. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9
Sequence similarities	Belongs to the SEC23/SEC24 family. SEC23 subfamily.

Ontologies

Keywords
Biological process	ER-Golgi transport Protein transport Transport
Cellular component	Endoplasmic reticulum Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Disease	Disease mutation
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	COPII vesicle coating Traceable author statement. Source: Reactome antigen processing and presentation of exogenous peptide antigen via MHC class II Traceable author statement. Source: Reactome antigen processing and presentation of peptide antigen via MHC class I Traceable author statement. Source: Reactome intracellular protein transport Inferred from electronic annotation. Source: InterPro post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	COPII vesicle coat Inferred from electronic annotation. Source: InterPro ER to Golgi transport vesicle membrane Traceable author statement. Source: Reactome Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome endoplasmic reticulum membrane Traceable author statement. Source: Reactome perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara smooth endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDK16	Q00536	3	EBI-81088,EBI-726261
SEC24C	P53992	5	EBI-81088,EBI-81134

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 765

765

Protein transport protein Sec23A

PRO_0000205146

Amino acid modifications

Modified residue

308

1

Phosphothreonine Ref.6

Natural variations

Natural variant

211

1

L → V. Ref.1 Ref.2 Ref.4
Corresponds to variant rs8018720 [ dbSNP | Ensembl ].

VAR_031029

Natural variant

382

1

F → L in CLSD; loss of function mutation; cargo proteins retained in the endoplasmic reticulum. Ref.9

VAR_031030

Experimental info

Sequence conflict

623

1

L → M in AAH36649. Ref.4

Secondary structure

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765

Helix Strand Turn

Details...

Helix

4 – 15

12

Beta strand

16 – 24

9

Helix

28 – 31

4

Beta strand

39 – 42

4

Turn

64 – 66

3

Beta strand

74 – 77

4

Turn

78 – 81

4

Beta strand

82 – 84

3

Beta strand

86 – 88

3

Beta strand

91 – 93

3

Helix

96 – 98

3

Helix

102 – 105

4

Helix

108 – 110

3

Helix

112 – 114

3

Beta strand

115 – 121

7

Beta strand

130 – 136

7

Helix

141 – 155

15

Beta strand

163 – 179

17

Turn

181 – 183

3

Beta strand

185 – 190

6

Helix

198 – 204

7

Beta strand

228 – 232

5

Helix

233 – 246

14

Helix

264 – 278

15

Beta strand

285 – 292

8

Beta strand

296 – 299

4

Helix

313 – 317

5

Helix

324 – 341

18

Beta strand

344 – 350

7

Helix

357 – 360

4

Helix

362 – 366

5

Beta strand

371 – 375

5

Beta strand

377 – 379

3

Helix

380 – 388

9

Beta strand

401 – 410

10

Beta strand

414 – 422

9

Beta strand

431 – 433

3

Beta strand

439 – 442

4

Beta strand

444 – 451

8

Beta strand

457 – 463

7

Beta strand

467 – 469

3

Beta strand

477 – 487

11

Beta strand

488 – 490

3

Beta strand

492 – 501

10

Helix

506 – 508

3

Helix

509 – 515

7

Helix

519 – 534

16

Helix

542 – 557

16

Beta strand

558 – 561

4

Helix

565 – 567

3

Turn

572 – 576

5

Helix

577 – 586

10

Turn

588 – 590

3

Helix

592 – 594

3

Helix

597 – 607

11

Helix

612 – 619

8

Beta strand

622 – 626

5

Beta strand

628 – 631

4

Beta strand

633 – 635

3

Helix

639 – 641

3

Beta strand

647 – 651

5

Beta strand

653 – 660

8

Helix

662 – 670

9

Turn

671 – 674

4

Helix

676 – 678

3

Helix

679 – 698

20

Beta strand

699 – 701

3

Beta strand

704 – 709

6

Turn

713 – 715

3

Helix

716 – 721

6

Helix

749 – 760

12

Sequences

	Sequence		Length	Mass (Da)
	Q15436 [UniParc]. Last modified March 6, 2007. Version 2. Checksum: 128DF9964B253313	FASTA	765	86,161
	10 20 30 40 50 60 MTTYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPVAA LFTPLKERPD LPPIQYEPVL 70 80 90 100 110 120 CSRTTCRAVL NPLCQVDYRA KLWACNFCYQ RNQFPPSYAG ISELNQPAEL LPQFSSIEYV 130 140 150 160 170 180 VLRGPQMPLI FLYVVDTCME DEDLQALKES MQMSLSLLPP TALVGLITFG RMVQVHELGC 190 200 210 220 230 240 EGISKSYVFR GTKDLSAKQL QEMLGLSKVP LTQATRGPQV QQPPPSNRFL QPVQKIDMNL 250 260 270 280 290 300 TDLLGELQRD PWPVPQGKRP LRSSGVALSI AVGLLECTFP NTGARIMMFI GGPATQGPGM 310 320 330 340 350 360 VVGDELKTPI RSWHDIDKDN AKYVKKGTKH FEALANRAAT TGHVIDIYAC ALDQTGLLEM 370 380 390 400 410 420 KCCPNLTGGY MVMGDSFNTS LFKQTFQRVF TKDMHGQFKM GFGGTLEIKT SREIKISGAI 430 440 450 460 470 480 GPCVSLNSKG PCVSENEIGT GGTCQWKICG LSPTTTLAIY FEVVNQHNAP IPQGGRGAIQ 490 500 510 520 530 540 FVTQYQHSSG QRRIRVTTIA RNWADAQTQI QNIAASFDQE AAAILMARLA IYRAETEEGP 550 560 570 580 590 600 DVLRWLDRQL IRLCQKFGEY HKDDPSSFRF SETFSLYPQF MFHLRRSSFL QVFNNSPDES 610 620 630 640 650 660 SYYRHHFMRQ DLTQSLIMIQ PILYAYSFSG PPEPVLLDSS SILADRILLM DTFFQILIYH 670 680 690 700 710 720 GETIAQWRKS GYQDMPEYEN FRHLLQAPVD DAQEILHSRF PMPRYIDTEH GGSQARFLLS 730 740 750 760 KVNPSQTHNN MYAWGQESGA PILTDDVSLQ VFMDHLKKLA VSSAA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and functional characterization of mammalian homologues of the COPII component Sec23." Paccaud J.-P., Reith W., Carpentier J.-L., Ravazzola M., Amherdt M., Schekman R., Orci L. Mol. Biol. Cell 7:1535-1546(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-211. Tissue: B-cell.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-211.
[3]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-211. Tissue: Testis.
[5]	"Two mammalian Sec16 homologues have nonredundant functions in endoplasmic reticulum (ER) export and transitional ER organization." Bhattacharyya D., Glick B.S. Mol. Biol. Cell 18:839-849(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SEC16A. Tissue: Liver.
[6]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-308, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]	"Solution structure of the ZF-SEC23_SEC24 from human SEC23A." RIKEN structural genomics initiative (RSGI) Submitted (OCT-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 57-108.
[9]	"Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-to-Golgi trafficking." Boyadjiev S.A., Fromme J.C., Ben J., Chong S.S., Nauta C., Hur D.J., Zhang G., Hamamoto S., Schekman R., Ravazzola M., Orci L., Eyaid W. Nat. Genet. 38:1192-1197(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CLSD LEU-382, CHARACTERIZATION OF VARIANT CLSD LEU-382.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X97064 mRNA. Translation: CAA65774.1.
AK312259 mRNA. Translation: BAG35191.1.
AL109628 Genomic DNA. No translation available.
BC036649 mRNA. Translation: AAH36649.1.

IPI

IPI00017375.

PIR

T09574.

RefSeq

NP_006355.2. NM_006364.2.

UniGene

Hs.272927.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2NUP	X-ray	2.80	A	1-765	[»]
2NUT	X-ray	2.30	A	1-765	[»]
2YRC	NMR	-	A	57-108	[»]
2YRD	NMR	-	A	57-108	[»]
3EFO	X-ray	2.70	A	1-765	[»]
3EG9	X-ray	3.00	A	1-764	[»]
3EGD	X-ray	2.70	A	1-764	[»]
3EGX	X-ray	3.30	A	1-764	[»]

ProteinModelPortal

Q15436.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15436. 24 interactions.

MINT

MINT-4998885.

STRING

9606.ENSP00000306881.

PTM databases

PhosphoSite

Q15436.

Polymorphism databases

DMDM

143811354.

Proteomic databases

PaxDb

Q15436.

PRIDE

Q15436.

Protocols and materials databases

DNASU

10484.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000307712; ENSP00000306881; ENSG00000100934.

GeneID

10484.

KEGG

hsa:10484.

UCSC

uc001wup.1. human.

Organism-specific databases

CTD

10484.

GeneCards

GC14M039501.

H-InvDB

HIX0011611.

HGNC

HGNC:10701. SEC23A.

MIM

607812. phenotype.
610511. gene.

neXtProt

NX_Q15436.

Orphanet

50814. Craniolenticulosutural dysplasia.

PharmGKB

PA35624.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5047.

HOGENOM

HOG000231690.

HOVERGEN

HBG055039.

InParanoid

Q15436.

KO

K14006.

OMA

KFGEYSK.

OrthoDB

EOG4BVRT0.

PhylomeDB

Q15436.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.
REACT_11123. Membrane Trafficking.
REACT_17015. Metabolism of proteins.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q15436.

Bgee

Q15436.

CleanEx

HS_SEC23A.

Genevestigator

Q15436.

GermOnline

ENSG00000100934. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.410. 1 hit.

InterPro

IPR007123. Gelsolin_dom.
IPR006900. Sec23/24_helical_dom.
IPR006896. Sec23/24_trunk_dom.
IPR012990. Sec23_24_beta_S.
IPR002035. VWF_A.
IPR006895. Znf_Sec23_Sec24.
[Graphical view]

Pfam

PF00626. Gelsolin. 1 hit.
PF08033. Sec23_BS. 1 hit.
PF04815. Sec23_helical. 1 hit.
PF04811. Sec23_trunk. 1 hit.
PF04810. zf-Sec23_Sec24. 1 hit.
[Graphical view]

SUPFAM

SSF81811. Sec23_helical. 1 hit.
SSF82919. Znf_Sec23_Sec24. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

SEC23A. human.

EvolutionaryTrace

Q15436.

GenomeRNAi

10484.

NextBio

39780.

SOURCE

Search...

Entry information

Entry name

SC23A_HUMAN

Accession

Primary (citable) accession number: Q15436
Secondary accession number(s): B2R5P4, Q8NE16

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	March 6, 2007
Last modified:	May 29, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.