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8.A.26.1.1
Calveolin-1 of 178 aas and 2 TMSs.  Caveolae are membrane-budding structures in vertebrate cells, and calveolin-1 forms membrane curvature and endocytic vesicles. Caveolae-like structures can form in E. coli through the expression of caveolin-1.  These caveolae are ~100 nm in diameter and can harbor both animal and bacterial transmembrane proteins (Shin et al. 2015). Molecules from the outside can be taken up into these structures. Transport of fatty acids across the plasma membrane is modulated by caveolin-1 and cholesterol and is not dependent on the putative fatty acid transport proteins, CD36 and FATP (Meshulam et al. 2006).

Accession Number:Q03135
Protein Name:Caveolin-1
Length:178
Molecular Weight:20472.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:2
Location1 / Topology2 / Orientation3: Golgi apparatus membrane1 / Peripheral membrane protein2
Substrate NONE

Cross database links:

Genevestigator: Q03135
eggNOG: prNOG11341
DIP: DIP-5960N
Entrez Gene ID: 857   
Pfam: PF01146   
KEGG: hsa:857   

Gene Ontology

GO:0016324 C:apical plasma membrane
GO:0016323 C:basolateral plasma membrane
GO:0005901 C:caveola
GO:0005829 C:cytosol
GO:0030666 C:endocytic vesicle membrane
GO:0005783 C:endoplasmic reticulum
GO:0005768 C:endosome
GO:0000139 C:Golgi membrane
GO:0005811 C:lipid particle
GO:0048471 C:perinuclear region of cytoplasm
GO:0015485 F:cholesterol binding
GO:0050998 F:nitric-oxide synthase binding
GO:0016504 F:peptidase activator activity
GO:0005515 F:protein binding
GO:0032947 F:protein complex scaffold
GO:0005102 F:receptor binding
GO:0007596 P:blood coagulation
GO:0006816 P:calcium ion transport
GO:0070836 P:caveola assembly
GO:0071455 P:cellular response to hyperoxia
GO:0009267 P:cellular response to starvation
GO:0042632 P:cholesterol homeostasis
GO:0051480 P:cytosolic calcium ion homeostasis
GO:0000188 P:inactivation of MAPK activity
GO:0008624 P:induction of apoptosis by extracellular signals
GO:0044419 P:interspecies interaction between organisms
GO:0050900 P:leukocyte migration
GO:0019915 P:lipid storage
GO:0032507 P:maintenance of protein location in cell
GO:0060056 P:mammary gland involution
GO:0051899 P:membrane depolarization
GO:0030514 P:negative regulation of BMP signaling pathway
GO:0090090 P:negative regulation of canonical Wnt receptor signaling pathway
GO:0001937 P:negative regulation of endothelial cell proliferation
GO:0030857 P:negative regulation of epithelial cell differentiation
GO:0045019 P:negative regulation of nitric oxide biosynthetic process
GO:0033137 P:negative regulation of peptidyl-serine phosphorylation
GO:0032091 P:negative regulation of protein binding
GO:0000122 P:negative regulation of transcription from RNA polymerase II promoter
GO:0033484 P:nitric oxide homeostasis
GO:0046209 P:nitric oxide metabolic process
GO:0010524 P:positive regulation of calcium ion transport into cytosol
GO:0090263 P:positive regulation of canonical Wnt receptor signaling pathway
GO:0048554 P:positive regulation of metalloenzyme activity
GO:0033138 P:positive regulation of peptidyl-serine phosphorylation
GO:0045907 P:positive regulation of vasoconstriction
GO:0051260 P:protein homooligomerization
GO:2000286 P:receptor internalization involved in canonical Wnt receptor signaling pathway
GO:0030193 P:regulation of blood coagulation
GO:0019217 P:regulation of fatty acid metabolic process
GO:0050999 P:regulation of nitric-oxide synthase activity
GO:0006940 P:regulation of smooth muscle contraction
GO:0051592 P:response to calcium ion
GO:0043627 P:response to estrogen stimulus
GO:0001666 P:response to hypoxia
GO:0032570 P:response to progesterone stimulus
GO:0007519 P:skeletal muscle tissue development
GO:0031295 P:T cell costimulation
GO:0006641 P:triglyceride metabolic process
GO:0001570 P:vasculogenesis
GO:0016050 P:vesicle organization

References (24)

[1] “The sequence of human caveolin reveals identity with VIP21, a component of transport vesicles.”  Glenney J.R. Jr.et.al.   1360410
[2] “Analysis of the CAVEOLIN-1 gene at human chromosome 7q31.1 in primary tumours and tumour-derived cell lines.”  Hurlstone A.F.et.al.   10086342
[3] “Sequence and detailed organization of the human caveolin-1 and -2 genes located near the D7S522 locus (7q31.1). Methylation of a CpG island in the 5' promoter region of the caveolin-1 gene in human breast cancer cell lines.”  Engelman J.A.et.al.   10218480
[4] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[5] “N-terminal processing and modifications of caveolin-1 in caveolae from human adipocytes.”  Vainonen J.P.et.al.   15219854
[6] “Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes.”  Aboulaich N.et.al.   15242332
[7] “Functional interaction of caveolin-1 with Bruton's tyrosine kinase and Bmx.”  Vargas L.et.al.   11751885
[8] “Identification and characterization of a novel human plant pathogenesis-related protein that localizes to lipid-enriched microdomains in the Golgi complex.”  Eberle H.B.et.al.   11865038
[9] “c-Abl is required for oxidative stress-induced phosphorylation of caveolin-1 on tyrosine 14.”  Sanguinetti A.R.et.al.   12531427
[10] “Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules.”  Zhang Y.et.al.   15951569
[11] “Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.”  Rush J.et.al.   15592455
[12] “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.”  Olsen J.V.et.al.   17081983
[13] “Translocation of endothelial nitric-oxide synthase involves a ternary complex with caveolin-1 and NOSTRIN.”  Schilling K.et.al.   16807357
[14] “The rotavirus enterotoxin NSP4 directly interacts with the caveolar structural protein caveolin-1.”  Parr R.D.et.al.   16501093
[15] “Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.”  Rikova K.et.al.   18083107
[16] “Caveolin-1 triggers T-cell activation via CD26 in association with CARMA1.”  Ohnuma K.et.al.   17287217
[17] “Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks.”  Wolf-Yadlin A.et.al.   17389395
[18] “Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis.”  Wang B.et.al.   19007248
[19] “A quantitative atlas of mitotic phosphorylation.”  Dephoure N.et.al.   18669648
[20] “An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells.”  Heibeck T.H.et.al.   19534553
[21] “Large-scale proteomics analysis of the human kinome.”  Oppermann F.S.et.al.   19369195
[22] “Lysine acetylation targets protein complexes and co-regulates major cellular functions.”  Choudhary C.et.al.   19608861
[23] “Caveolin-1 mutations (P132L and null) and the pathogenesis of breast cancer: caveolin-1 (P132L) behaves in a dominant-negative manner and caveolin-1 (-/-) null mice show mammary epithelial cell hyperplasia.”  Lee H.et.al.   12368209
[24] “Association of a homozygous nonsense caveolin-1 mutation with Berardinelli-Seip congenital lipodystrophy.”  Kim C.A.et.al.   18211975

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MSGGKYVDSE GHLYTVPIRE QGNIYKPNNK AMADELSEKQ VYDAHTKEID LVNRDPKHLN 
61:	DDVVKIDFED VIAEPEGTHS FDGIWKASFT TFTVTKYWFY RLLSALFGIP MALIWGIYFA 
121:	ILSFLHIWAV VPCIKSFLIE IQCISRVYSI YVHTVCDPLF EAVGKIFSNV RINLQKEI